-- dump date   	20140619_015907
-- class       	Genbank::CDS
-- table       	cds_note
-- id	note
YP_556591.1	binds to the dnaA-box as an ATP-bound complex at the origin of replication during the initiation of chromosomal replication; can also affect transcription of multiple genes including itself.
YP_556592.1	binds the polymerase to DNA and acts as a sliding clamp
YP_556593.1	negatively supercoils closed circular double-stranded DNA
YP_556610.1	catalyzes the formation of acetaldehyde from ethanolamine
YP_556617.1	exhibits an RNA-dependent ATPase activity, specifically stimulated by bacterial 23S rRNA
YP_556618.1	catalyzes the transfer of an amino moiety
YP_556630.1	catalyzes the phosphorylation and decarboxylation of oxaloacetate to form phosphoenolpyruvate using GTP
YP_556633.1	decatenates replicating daughter chromosomes
YP_556636.1	cleaves off formyl group from N-terminal methionine residues of newly synthesized proteins; binds iron(2+)
YP_556637.1	modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet) which is important in translation initiation; inactivation of this gene in Escherichia coli severely impairs growth
YP_556653.1	in some organisms this protein is a transmembrane protein while in others it is periplasmic; involved in some organisms with other components of the MreBCD complex and with penicillin binding proteins in the periplasm or cell wall
YP_556654.1	functions in MreBCD complex in some organisms
YP_556655.1	allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases; reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA; some Mycoplasma proteins contain an N-terminal fusion to an unknown domain
YP_556656.1	allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases; reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA
YP_556657.1	allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases; reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA
YP_556664.1	Catalyzes the conversion of acetyl-CoA and L-homoserine to CoA and O-acetyl-L-homoserine
YP_556665.2	FtsZ binding protein; synthetically lethal with a defect in the Min system; this protein is the first identified nucleoid occlusion factor which works along with the Min system to properly position the FtsZ ring assembly
YP_556667.1	catalyzes the phosphorylation of N-acetyl-L-glutamate to form N-acetyl-L-glutamate 5-phosphate
YP_556671.1	heat shock protein involved in degradation of misfolded proteins
YP_556672.1	heat shock protein involved in degradation of misfolded proteins
YP_556677.1	site-specific tyrosine recombinase which cuts and rejoins DNA molecules; binds cooperatively to specific DNA consensus sites; forms a heterotetrameric complex with XerC; XerCD exhibit similar sequences; essential to convert chromosome dimers to monomers during cell division and functions during plasmid segregation; cell division protein FtsK may regulate the XerCD complex; enzyme from Streptococcus group has unusual active site motifs
YP_556679.1	involved in lysine biosynthesis; DAP epimerase; produces DL-diaminopimelate from LL-diaminopimelate
YP_556680.1	Acylates the intermediate (KDO)2-lipid IVA to form (KDO)2-(lauroyl)-lipid IVA
YP_556681.1	catalyzes the formation of S-adenosylmethionine from methionine and ATP; methionine adenosyltransferase
YP_556692.1	catalyzes the phosphorylation of protein substrates at serine and threonine residues in vitro; specific substrate in vivo has not been identified yet; plays a role in long-term cell survival and expression of surface appendages
YP_556700.1	Citation: Appl. Environ. Microbiol. 69 (12),7257- 7265 (2003)
YP_556761.1	catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates
YP_556781.1	catalyzes the formation of acetoacetate and acetyl-CoA from 3-hydroxy-3-methylglutaryl-CoA
YP_556787.1	DTB synthetase; dethiobiotin synthase; involved in production of dethiobiotin from ATP and 7,8-diaminononanoate and carbon dioxide; contains magnesium
YP_556788.1	catalyzes the formation of 8-amino-7-oxononanoate from 6-carboxyhexanoyl-CoA and L-alanine
YP_556789.1	catalyzes the formation of S-adenosyl-4-methylthionine-2-oxobutanoate and 7,8-diaminononanoate from S-adenosyl-L-methionine and 8-amino-7-oxononanoate
YP_556797.1	Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation
YP_556799.1	catalyzes the phosphorylation/dephosphorylation of the enzyme isocitrate dehydrogenase on a specific serine which regulates activity; unphosphorylated IDH is fully active when cells are grown on glucose while the enzyme becomes phosphorylated and inactive in the presence of acetate or ethanol
YP_556807.1	catalyzes a two-step reaction, first charging an arginine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; class-I aminoacyl-tRNA synthetase
YP_556819.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_556825.1	type III; catalyzes the formation of (R)-4'-phosphopantothenate from (R)-pantothenate in coenzyme A biosynthesis; type III pantothenate kinases are not subject to feedback inhibition from coenzyme A and have a high Km for ATP
YP_556826.1	catalyzes the formation of biotinyl-5'-AMP, also acts as a transcriptional repressor of the biotin operon
YP_556837.1	Glycine cleavage system transcriptional activator; activates the gcvTHP operon in the presence of glycine and represses the operon in its absence
YP_556839.1	lipoyl/octanoyltransferase; catalyzes the transfer of the lipoyl/octanoyl moiety of lipoyl/octanoyl-ACP onto lipoate-dependent enzymes like pyruvate dehydrogenase and the glycine cleavage system H protein
YP_556840.1	catalyzes the radical-mediated insertion of two sulfur atoms into an acyl carrier protein (ACP) bound to an octanoyl group to produce a lipoyl group
YP_556850.1	hydrolyzes diesters during transport at the inner face of the cytoplasmic membrane to glycerol-3-phosphate and alcohol; induced when cells are starved for inorganic phosphate
YP_556855.1	involved in the transport of C4-dicarboxylates across the membrane
YP_556865.1	catalyzes the second step in the glutathione biosynthesis pathway, where it synthesizes ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
YP_556871.1	2,3-bisphosphoglycerate-dependent; catalyzes the interconversion of 2-phosphoglycerate to 3-phosphoglycerate
YP_556874.1	molecular chaperone that is required for the normal export of envelope proteins out of the cell cytoplasm; in Escherichia coli this proteins forms a homotetramer in the cytoplasm and delivers proteins to be exported to SecA
YP_556875.1	catalyzes the NAD(P)H-dependent reduction of glycerol 3-phosphate to glycerone phosphate
YP_556883.1	involved in the insertion of copper into subunit I of cytochrome C oxidase
YP_556890.1	converts protoheme IX and farnesyl diphosphate to heme O
YP_556906.1	binds with the catalytic core of RNA polymerase to produce the holoenzyme; this sigma factor is responsible for the expression of heat shock promoters
YP_556911.1	Homogentisate pathway; Citation: J Bacteriol. 2001 Jan;183(2):700-8
YP_556914.1	Catalyzes the conversion of ATP and pantetheine 4'-phosphate to diphosphate and 3'-dephospho-coA
YP_556916.1	catalyzes the formation of L-histidinol phosphate from imidazole-acetol phosphate and glutamate in histidine biosynthesis
YP_556917.1	Enables the recycling of peptidyl-tRNAs produced at termination of translation
YP_556918.1	the Ctc family of proteins consists of two types, one that contains the N-terminal ribosomal protein L25 domain only which in Escherichia coli binds the 5S rRNA while a subset of proteins contain a C-terminal extension that is involved in the stress response
YP_556919.1	catalyzes the formation of 5-phospho-alpha-D-ribose 1-phosphate from D-ribose 5-phosphate and ATP
YP_556920.1	An essential enzyme in the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl diphosphate biosynthesis
YP_556921.1	Incorporates lipoproteins in the outer membrane after they are released by the LolA protein
YP_556923.1	Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases
YP_556927.1	catalyzes the phosphorylation of the phosphocarrier protein HPr of the bacterial phosphotransferase system
YP_556930.1	sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released; sigma 54 factor is responsible for the expression of enzymes involved in nitrogen assimilation and metabolism; the rhizobia often have 2 copies of this sigma factor; in Rhizobium etli RpoN1 shown to be involved in the assimilation of several nitrogen and carbon sources during free-living aerobic growth and RpoN2 is involved in symbiotic nitrogen fixation; in Bradyrhizobium both RpoN1 and N2 are functional in free-living and symbiotic conditions, rpoN1 gene was regulated in response to oxygen
YP_556937.1	catalyzes a salvage reaction resulting in the formation of AMP which is metabolically less costly than a de novo synthesis
YP_556940.1	produces formate from formyl-tetrahydrofolate which is the major source of formate for PurT in de novo purine nucleotide biosynthesis; has a role in one-carbon metabolism; forms a homohexamer; activated by methionine and inhibited by glycine
YP_556945.1	binds to single stranded DNA and may facilitate the binding and interaction of other proteins to DNA
YP_556995.1	catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1) in queuosine biosynthesis
YP_556997.1	threonine deaminase; threonine dehydratase; in Escherichia coli, IlvA is part of the isoleucine biosynthetic pathway
YP_557001.1	Catalyzes the carbon methylation reaction in the biosynthesis of ubiquinone
YP_557004.1	an Escherichia coli mutant results in accumulation of octaprenylphenol and no ubiquinone; functions in the formation of 2-octaprenyl-6-hydroxy-phenol from 2-octaprenylphenol in ubiquinone (coenzyme Q) biosynthesis; similar to eukaryotic proteins that exhibit kinase functions
YP_557008.1	catalyzes a two-step reaction, first charging an aspartate molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; contains discriminating and non-discriminating subtypes
YP_557009.1	converts dATP to dAMP and pyrophosphate
YP_557015.1	Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation
YP_557016.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_557029.1	catalyzes oxidation of 4-(phosphohydroxy)-L-threonine into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which decarboxylates to form 1-amino-3-(phosphohydroxy)propan-2-one (3-amino-2-oxopropyl phosphate)
YP_557030.1	catalyzes the transfer of a total of four methyl groups from S-adenosyl-l-methionine (S-AdoMet) to two adjacent adenosine bases A1518 and A1519 in 16S rRNA; mutations in ksgA causes resistance to the translation initiation inhibitor kasugamycin
YP_557037.1	Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate
YP_557038.1	glycine--tRNA ligase beta chain; glyS; class II aminoacyl tRNA synthetase; tetramer of alpha(2)beta(2); catalyzes a two-step reaction; first charging a glycine molecule by linking the carboxyl group to the alpha-phosphate of ATP; second by transfer of the aminoacyl-adenylate to its tRNA
YP_557039.1	glycine--tRNA ligase alpha chain; GlyRS; class II aminoacyl tRNA synthetase; tetramer of alpha(2)beta(2); catalyzes a two-step reaction; first charging a glycine molecule by linking its carboxyl group to the alpha-phosphate of ATP; second by transfer of the aminoacyl-adenylate to its tRNA
YP_557041.1	catalyzes a sulfuration reaction to synthesize 2-thiouridine at the U34 position of tRNAs
YP_557058.1	forms a complex with SecD and YajC; SecDFyajC stimulates the proton motive force-driven protein translocation; seems to modulate the cycling of SecA by stabilizing its membrane-inserted state and appears to be required for the release of mature proteins from the extracytoplasmic side of the membrane; in some organisms, such as Bacillus subtilis, SecD is fused to SecF
YP_557059.1	part of the preprotein secretory system; when complexed with proteins SecF and YajC, SecDFyajC stimulates the proton motive force-driven protein translocation, and appears to be required for the release of mature proteins from the extracytoplasmic side of the membrane
YP_557060.1	member of preprotein translocase; forms a heterotrimer with SecD and SecF; links the SecD/SecF/YajC/YidC complex with the SecY/SecE/SecG complex
YP_557061.1	Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr)
YP_557062.1	Synthesizes oQ from preQ1 in a single S-adenosylmethionine-requiring step
YP_557063.1	catalyzes branch migration in Holliday junction intermediates
YP_557069.1	catalyzes the formation of L-proline from pyrroline-5-carboxylate
YP_557078.1	catalyzes the formation of 3-deoxy-D-arabino-hept-2-ulosonate 7 phosphate from phosphoenolpyruvate and D-erythrose 4-phosphate, phenylalanine sensitive
YP_557082.1	catalyzes the ATP-dependent addition of AMP to a subunit of glutamine synthetase; also catalyzes the reverse reaction - deadenylation; adenylation/deadenylation of glutamine synthetase subunits is important for the regulation of this enzyme
YP_557084.1	catalyzes the phosphorylation of NAD to NADP
YP_557085.1	Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons
YP_557086.1	protoheme ferro-lyase; catalyzes the insertion of a ferrous ion into protoporphyrin IX to form protoheme; involved in protoheme biosynthesis; in some organisms this protein is membrane-associated while in others it is cytosolic
YP_557088.1	with DnaK and DnaJ acts in response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins; may act as a thermosensor
YP_557090.1	heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria
YP_557091.1	chaperone Hsp40; co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, dnaK-independent fashion
YP_557093.1	catalyzes the formation of tetrahydrofolate and 2-dehydropantoate from 5,10-methylenetetrahydrofolate and 3-methyl-2-oxobutanoate
YP_557115.1	catalyzes the formation of 1-(5-phosphoribosyl)-5-aminoimidazole from 2-(formamido)-N1-(5-phosphoribosyl)acetamidine and ATP in purine biosynthesis
YP_557116.1	IPP transferase; isopentenyltransferase; involved in tRNA modification; in Escherichia coli this enzyme catalyzes the addition of a delta2-isopentenyl group from dimethylallyl diphosphate to the N6-nitrogen of adenosine adjacent to the anticodon of tRNA species that read codons starting with uracil; further tRNA modifications may occur; mutations in miaA result in defects in translation efficiency and fidelity
YP_557117.1	This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. Promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex
YP_557129.1	forms dimers; may be involved in cell envelope integrity; interacts with outer membrane proteins and with the C-terminal domain of inner membrane protein TolA
YP_557135.1	catalyzes the reaction of glycine with 5,10-methylenetetrahydrofolate to form L-serine and tetrahydrofolate
YP_557149.1	An oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanine
YP_557150.1	Homogentisate pathway; Citation: J. Bacteriol. 186 (15), 5062-5077 (2004)
YP_557153.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_557158.1	catalyzes the formation of oxalozcetate and L-glutamate from L-aspartate and 2-oxoglutarate
YP_557234.1	10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring
YP_557235.1	60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is essential for growth
YP_557240.1	similar to RuvC resolvase with substantial differences; NMR structural information suggests this protein is monomeric; unknown cellular function
YP_557241.1	regulates pyrimidine biosynthesis by binding to the mRNA of the pyr genes, also has been shown to have uracil phosphoribosyltransferase activity
YP_557242.1	catalyzes the transfer of the carbamoyl moiety from carbamoyl phosphate to L- aspartate in pyrimidine biosynthesis
YP_557243.1	Catalyzes the reversible hydrolysis of the amide bond within dihydroorotate. This metabolic intermediate is required for the biosynthesis of pyrimidine nucleotides
YP_557245.1	hydrolyzes P(1),P(4)-bis(5'-adenosyl) tetraphosphate to form 2 ADP
YP_557343.1	catalyzes the transfer of 2-keto-3-deoxy-D-manno-octulosonic acid to lipid A
YP_557346.1	involved in the assembly of the urease metallocenter; possible nickel donor
YP_557347.1	ureases catalyze the hydrolysis of urea into ammonia and carbon dioxide; in Helicobacter pylori the ammonia released plays a key role in bacterial survival by neutralizing acids when colonizing the gastric mucosa; the holoenzyme is composed of 3 ureC (alpha) and 3 ureAB (gamma/beta) subunits
YP_557349.1	UreA, with UreB and UreC catalyzes the hydrolysis of urea into ammonia and carbon dioxide; nickel metalloenzyme; accessory proteins UreD, UreE, UreF, and UreG are necessary for assembly of the metallocenter
YP_557378.1	catalyzes the reduction of 3'-phosphoadenylyl sulfate into sulfite
YP_557379.1	with CysN catalyzes the formation of adenylylsulfate from sulfate and ATP
YP_557381.1	catalyzes 2 sequential methylations, the formation of precorrin-1 and S-adenosyl-L-homocysteine from S-adenosyl-L-methionine and uroporphyrin III, and the formation of precorrin-2 and S-adenosyl-L-homocysteine from S-adenosyl-L-methionine and precorrin-1
YP_557402.1	catalyzes the removal of N-terminal amino acids preferably leucine from various peptides
YP_557403.1	binds to single-strand binding (SSB) protein and acts as a bridge between the DnaX clamp loader complex and the SSB
YP_557406.1	catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis
YP_557408.1	transfers the N-acyl diglyceride moiety to the prospective N-terminal cysteine in prolipoprotein
YP_557468.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_557477.1	p-cymene pathway; Citation: J. Bacteriol. 179 (10), 3171-3180 (1997)
YP_557478.1	p-cymene pathway; Citation: J. Bacteriol. 179 (10), 3171-3180 (1997)
YP_557479.1	p-cymene pathway; Citation:  J. Bacteriol. 179 (10), 3171-3180(1997)
YP_557481.1	p-cymene pathway; Citation: J. Bacteriol. 179 (10), 3171-3180 (1997).Biochem. Biophys. Res. Commun. 233 (2), 502-506 (1997)
YP_557482.1	p-cymene pathway; Citation: J. Bacteriol. 178 (5), 1351-1362 (1996)
YP_557483.1	p-cumate pathway; Citation: J. Bacteriol. 178 (5), 1351-1362 (1996)
YP_557484.1	p-cumate pathway; Citation: J. Bacteriol. 178 (5), 1351-1362 (1996)
YP_557485.1	p-cumate pathway; Citation: J. Bacteriol. 178 (5), 1351-1362 (1996)
YP_557486.1	p-cumate pathway; Citation: J. Bacteriol. 178 (5), 1351-1362 (1996)
YP_557487.1	p-cumate pathway; Citation: J. Bacteriol. 178 (5), 1351-1362 (1996)
YP_557488.1	p-cumate pathway; Citation: J. Bacteriol. 178 (5), 1351-1362 (1996)
YP_557489.1	p-cumate pathway; Citation: J. Bacteriol. 178 (5), 1351-1362 (1996)
YP_557490.1	Citation: J. Bacteriol. 178 (5), 1351-1362 (1996); p-cymene pathway
YP_557491.1	p-cumate pathway; Citation: J. Bacteriol. 178 (5), 1351-1362 (1996)
YP_557492.1	p-cumate pathway; Citation: J. Bacteriol. 178 (5), 1351-1362 (1996)
YP_557493.1	catalyzes the formation of acetyl-CoA from acetalaldehyde
YP_557494.1	catalyzes the formation of pyruvate and acetaldehyde from 4-hydroxy-2-ketovaleric acid; involved in the degradation of phenylpropionate
YP_557538.1	catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide and 5,6-dimethylbenzimidazole
YP_557539.1	catalyzes the formation of adenosylcobalamin from Ado-cobinamide-GDP and alpha-ribazole
YP_557542.1	cobalamin biosynthesis protein; decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin; structurally similar to histidinol phosphate aminotransferase
YP_557543.1	CobD; CbiD in Salmonella; converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group
YP_557545.1	catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation
YP_557548.1	Converts L-aspartate to beta-alanine and provides the major route of beta-alanine production in bacteria. Beta-alanine is essential for the biosynthesis of pantothenate (vitamin B5)
YP_557549.1	catalyzes the formation of (R)-pantothenate from pantoate and beta-alanine
YP_557554.1	methionine--tRNA ligase; MetRS; adds methionine to tRNA(Met) with cleavage of ATP to AMP and diphosphate; some MetRS enzymes form dimers depending on a C-terminal domain that is also found in other proteins such as Trbp111 in Aquifex aeolicus and the cold-shock protein CsaA from Bacillus subtilis while others do not; four subfamilies exist based on sequence motifs and zinc content
YP_557559.1	Catalyzes the formation of dUTP from dCTP in thymidylate biosynthesis
YP_557574.1	catalyzes the formation of L-ornithine from N(2)-acetyl-L-ornithine
YP_557583.1	glucokinase catalyzes the conversion of ATP and D-glucose to ADP and D-glucose 6-phosphate
YP_557585.1	catalyzes the formation of D-glucono-1,5-lactone 6-phosphate from D-glucose 6-phosphate
YP_557596.1	participates with LolB in the incorporation of lipoprotein into the outer membrane
YP_557602.1	catalyzes a two-step reaction, first charging a serine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA
YP_557612.1	blocks the formation of polar Z-ring septums
YP_557614.1	works in conjunction with MinC and MinD to enable cell division at the midpoint of the long axis of the cell
YP_557622.1	catalyzes the formation of arginine from (N-L-arginino)succinate
YP_557625.1	catalyzes the formation of oxaloacetate from phosphoenolpyruvate
YP_557627.1	catalyzes the formation of uroporphyrinogen-III from hydroxymethylbilane and the formation of precorrin-2 from uroporphyrin III and S-adenosyl-L-methionine by two sequential methylation reactions; functions in tetrapyrrole and heme biosynthesis
YP_557635.1	Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis
YP_557637.1	catalyzes the hydrolysis of pyrophosphate to phosphate
YP_557641.1	NH(3)-dependent; catalyzes the formation of nicotinamide adenine dinucleotide (NAD) from nicotinic acid adenine dinucleotide (NAAD) using either ammonia or glutamine as the amide donor and ATP; ammonia-utilizing enzymes include the ones from Bacillus and Escherichia coli while glutamine-utilizing enzymes include the Mycobacterial one; forms homodimers
YP_557682.1	NAD-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; does not decarboxylate oxaloacetate
YP_557696.1	decatenates newly replicated chromosomal DNA and relaxes positive and negative DNA supercoiling
YP_557697.1	decatenates newly replicated chromosomal DNA and relaxes positive and negative DNA supercoiling
YP_557706.1	molecular chaperone
YP_557725.1	Involved in the electron transport chain
YP_557734.1	non-folate utilizing enzyme, catalyzes the production of beta-formyl glycinamide ribonucleotide from formate, ATP, and beta-GAR and a side reaction producing acetyl phosphate and ADP from acetate and ATP; involved in de novo purine biosynthesis
YP_557737.1	catalyzes the condensation of two pyruvates to form acetolactate, implicated in pH homeostasis via the acetoin-2,3-butanediol pathway or in valine biosynthesis
YP_557741.1	this tRNA synthetase lacks the tRNA anticodon interaction domain; instead this enzyme modifies tRNA(Asp) with glutamate by esterifying glutamate to the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of queosine generating a modified nucleoside at the first anticodon position of tRNAAsp; the modified tRNA does not bind elongation factor Tu
YP_557743.1	catalyzes DNA-template-directed extension of the 3'- end of a DNA strand by one nucleotide at a time; main replicative polymerase
YP_557751.1	Required for efficient pilin antigenic variation
YP_557768.1	Maf; overexpression in Bacillus subtilis inhibits septation in the dividing cell
YP_557770.1	SPOUT methyltransferase family protein; crystal structure shows homodimer; in Escherichia coli this protein methylates pseudouridine at position 1915 of the 23S ribosomal RNA
YP_557772.1	catalyzes the formation of deamido-NAD(+) from nicotinate ribonucleotide and ATP
YP_557773.1	catalyzes the conversion of the propionic acid groups of rings I and III to vinyl groups during heme synthesis
YP_557774.1	catalyzes the formation of N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-D-ribosylamine and glycine in purine biosynthesis
YP_557776.1	Catalyzes the formation of uracil and 5-phospho-alpha-D-ribosy 1-diphosphate from UMP and diphosphate
YP_557778.1	catalyzes the formation of methylglyoxal from glycerone phosphate
YP_557782.1	catalyzes the hydrolysis of ATP coupled with the exchange of hydrogen and potassium ions
YP_557783.1	One of the components of the high-affinity ATP-driven potassium transport (or KDP) system, which catalyzes the hydrolysis of ATP coupled with the exchange of hydrogen and potassium ions
YP_557784.1	One of the components of the high-affinity ATP-driven potassium transport (or KDP)system, which catalyzes the hydrolysis of ATP coupled with the exchange of hydrogen and potassium ions. The C subunit may be involved in assembly of the KDP complex
YP_557785.1	Citation: Walderhaug,M.O., Polarek,J.W.,Voelkner,P., et al. J. Bacteriol. 174 (7), 2152-2159(1992)
YP_557786.1	Citation: Walderhaug,M.O., Polarek,J.W.,Voelkner,P., et al. J. Bacteriol. 174 (7), 2152-2159(1992)
YP_557793.1	Converts glucose to D-glucono-1,5 lactone
YP_557802.1	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
YP_557803.1	acetolactate synthase large subunit; catalyzes the formation of 2-acetolactate from pyruvate
YP_557804.1	with IlvI catalyzes the formation of 2-acetolactate from pyruvate, the small subunit is required for full activity and valine sensitivity; E.coli produces 3 isoenzymes of acetolactate synthase which differ in specificity to substrates, valine sensitivity and affinity for cofactors; also known as acetolactate synthase 3 small subunit
YP_557805.1	catalyzes the formation of (R)-2,3-dihydroxy-3-methylbutanoate from (S)-2-hydroxy-2-methyl-3-oxobutanoate in valine and isoleucine biosynthesis
YP_557806.1	catalyzes the decarboxylaton of phospatidyl-L-sering to phosphatidylethanolamine
YP_557809.1	catalyzes the formation of 2-isopropylmalate from acetyl-CoA and 2-oxoisovalerate in leucine biosynthesis
YP_557813.1	primary rRNA binding protein; helps nucleate assembly of 30S; binds directly to the 16S rRNA and an intersubunit bridge to the 23S rRNA; autoregulates translation through interactions with the mRNA leader sequence
YP_557816.1	Reversibly isomerizes the ketone sugar dihydroxyacetone phosphate to the aldehyde sugar glyceraldehyde-3-phosphate
YP_557818.1	Catalyzes the transfer of electrons from NADH to quinone
YP_557819.1	The point of entry for the majority of electrons that traverse the respiratory chain eventually resulting in the reduction of oxygen
YP_557820.1	Catalyzes the transfer of electrons from NADH to quinone
YP_557821.1	Catalyzes the transfer of electrons from NADH to quinone
YP_557822.1	Catalyzes the transfer of electrons from NADH to quinone
YP_557824.1	Catalyzes the transfer of electrons from NADH to ubiquinone
YP_557825.1	Catalyzes the transfer of electrons from NADH to quinone
YP_557826.1	Catalyzes the transfer of electrons from NADH to quinone
YP_557827.1	Catalyzes the transfer of electrons from NADH to quinone
YP_557828.1	Catalyzes the transfer of electrons from NADH to quinone
YP_557829.1	Catalyzes the transfer of electrons from NADH to ubiquinone
YP_557830.1	Catalyzes the transfer of electrons from NADH to quinone
YP_557831.1	Catalyzes the transfer of electrons from NADH to quinone
YP_557836.1	Citation:  Roffey,P.E. and Pemberton, J.M.Curr.Microbiol. 21, 329-337 (1990)
YP_557841.1	Citation: Larimer,F.W., Chain,P., Hauser,L., et al.Nat. Biotechnol. 22 (1), 55-61 (2004)
YP_557847.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_557848.1	converts 3-hydroxyadipyl-CoA to beta-ketoadipyl-CoA in phenylacetate degradation
YP_557850.1	catalyzes the transfer of an amino moiety
YP_557861.1	Citation: Guyer,D.M., Kao,J.S. andMobley, H.L.Infect. Immun. 66 (9), 4411-4417 (1998)
YP_557864.1	similar to Hp3 E. coli pathogenicity island; Citation: Guyer,D.M., Kao,J.S. andMobley, H.L.Infect. Immun. 66 (9), 4411-4417 (1998); similar to Hp3
YP_557873.1	Citation: Kim,Y.R., Lee,S.E., Kim,C.M., etal.Infect. Immun. 71 (10), 5461-5471 (2003)
YP_557875.1	catalyzes the formation of acetoacetate from 3-hydroxybutyrate
YP_557877.1	catalyzes the formation of L-glutamate and an aromatic oxo acid from an aromatic amino acid and 2-oxoglutarate
YP_557878.1	The UvrABC repair system catalyzes the recognition and processing of DNA lesions. The beta-hairpin of the Uvr-B subunit is inserted between the strands, where it probes for the presence of a lesion
YP_557893.1	converts L-glutamate to D-glutamate, a component of peptidoglycan
YP_557904.1	Citation: Salanoubat,M., Genin,S., Artiguenave,F., et al. Nature 415 (6871), 497-502 (2002)
YP_557909.1	part of a set of proteins involved in the infection of eukaryotic cells; in plant pathogens involved in the hypersensitivity response
YP_557918.1	Acs; catalyzes the conversion of acetate and CoA to acetyl-CoA
YP_558012.1	PAAR motiff-containing
YP_558067.1	specific inhibitor of chromosomal initiation of replication in vitro; binds the three 13-mers in the origin (oriC) to block initiation of replication; also controls genes involved in arginine transport
YP_558082.1	catalyzes the degradation of histidine to urocanate and ammmonia
YP_558084.1	catalyzes the formation of 4-imidazolone-5-propanoate from urocanate during histidine metabolism
YP_558086.1	catalyzing the hydrolysis of 4-imidazolone-5-propionate to N-formimidoyl-L-glutamate, the third step in the histidine degradation pathway
YP_558087.1	catalyzes the deimination of N-formimino-L-glutamate to ammonia and N-formyl-L-glutamate
YP_558090.1	similar to transglutaminase/cysteine proteases
YP_558094.1	catalyzes the formation of alpha-1,4-glucan chains from ADP-glucose
YP_558095.1	catalyzes the formation of ADP-glucose and diphosphate from ATP and alpha-D-glucose 1-phosphate
YP_558104.1	Citation: Nishijyo,T., Park,S.M., Lu,C.D., Itoh, Y.and Abdelal,A.T.J. Bacteriol. 180 (21), 5559-5566 (1998)
YP_558105.1	DapATase; bifunctional enzyme that functions in arginine and lysine biosynthetic pathways; catalyzes the formation of N-acetyl-L-glutamate 5-semialdehyde from 2-oxoglutarate and N(2)-acetyl-L-ornithine or N-succinyl-2-L-amino-6-oxoheptanedioate from 2-oxoglutarate and N-succinyl-L-2,6-diaminoheptanedioate
YP_558108.1	a high throughput screen identified this enzyme as an aldehyde dehydrogenase with broad substrate specificity; converts succinylglutamate semialdehyde and NAD to succinylglutamate and NADH
YP_558109.1	catalyzes the hydrolysis of 2-N-succinylarginine into 2-N-succinylornithine, ammonia and carbon dioxide in arginine degradation
YP_558110.1	catalyzes the formation of succinate and glutamate from N(2)-succinylglutamate in arginine catabolism
YP_558112.1	converts acetoacetate to acetone and carbon dioxide
YP_558123.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_558124.1	lipoprotein signal peptidase; integral membrane protein that removes signal peptides from prolipoproteins during lipoprotein biosynthesis
YP_558125.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_558126.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_558155.1	may be involved in chromosome condensation; overexpression in Escherichia coli protects against decondensation by camphor; overexpressing the protein results in an increase in supercoiling
YP_558180.1	Peptidyl-tRNA hydrolase domain
YP_558190.1	catalyzes the formation of oxalozcetate and L-glutamate from L-aspartate and 2-oxoglutarate
YP_558193.1	in Streptococcus pneumoniae this gene was found to be essential; structure determination of the Streptococcus protein shows that it is similar to a number of other proteins
YP_558194.1	modifies transcription through interactions with RNA polymerase affecting elongation, readthrough, termination, and antitermination
YP_558195.1	Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits during initiation of protein synthesis. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex
YP_558196.1	associates with free 30S ribosomal subunits; essential for efficient processing of 16S rRNA; in Escherichia coli rbfA is induced by cold shock
YP_558197.1	catalyzes isomerization of specific uridines in RNA to pseudouridine; responsible for residues in T loops of many tRNAs
YP_558203.1	SucA; E1 component of the oxoglutarate dehydrogenase complex which catalyzes the formation of succinyl-CoA from 2-oxoglutarate; SucA catalyzes the reaction of 2-oxoglutarate with dihydrolipoamide succinyltransferase-lipoate to form dihydrolipoamide succinyltransferase-succinyldihydrolipoate and carbon dioxide
YP_558204.1	component of 2-oxoglutarate dehydrogenase complex; catalyzes the transfer of succinyl coenzyme A to form succinyl CoA as part of the conversion of 2-oxoglutarate to succinyl-CoA
YP_558205.1	E3 component of 2-oxoglutarate dehydrogenase complex; catalyzes the oxidation of dihydrolipoamide to lipoamide
YP_558209.1	Citation: Cope,L.D., Yogev,R., Muller-Eberhard, U.and Hansen,E.J. A gene cluster involved in the utilizationof both free heme and heme:hemopexin by Haemophilusinfluenzae type b. J. Bacteriol. 177 (10), 2644- 2653(1995)
YP_558232.1	Citation: Matsui,H., Sano,Y., Ishihara,H. andShinomiya,T. Regulation of pyocin genes in Pseudomonasaeruginosa by positive (prtN) and negative (prtR)regulatory genes. J. Bacteriol. 175 (5), 1257-1263 (1993)
YP_558233.1	similar to surface antigen LipA
YP_558238.1	Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation
YP_558240.1	Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis
YP_558241.1	functions in fatty acid oxidation; converts acyl-CoA and FAD to FADH2 and delta2-enoyl-CoA
YP_558257.1	Citation: Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M., Garcia,J.L. andDiaz,E.J. Biol. Chem. 273 (40), 25974-25986 (1998); similar to MaoC (Phenylacetic acid degradation protein paaZ)
YP_558273.1	Citation: Bourne,P.C., Isupov,M.N. andLittlechild, J.A.The atomic-resolution structure of a novelbacterial esterase.  Structure Fold. Des. 8 (2), 143-151(2000)
YP_558284.1	dehydratase component, catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate
YP_558289.1	Citation:  J. Bacteriol. 179 (8), 2573-2581 (1997).J.Chem. Biol. 9 (9), 1017-1026 (2002)
YP_558291.1	An oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanine
YP_558292.1	Homogentisate pathway; Citation: J. Bacteriol. 186 (15), 5062-5077 (2004).Environ Microbiol. 2002 Dec;4(12):824-41.
YP_558293.1	Homogentisate pathway; Citation: J Bacteriol. 2001 Jan;183(2):700-8. J.Bacteriol. 186 (15), 5062-5077 (2004). Biochem J. 1997 Dec15;328 ( Pt 3):929-35
YP_558321.1	member of a large family of NAD or NADP-dependent oxidoreductases; paralogs occur in many bacteria
YP_558329.2	catalyzes the reduction of nitroaromatic compounds such as nitrofurazone, quinones and the anti-tumor agent CB1954; NAD(P)H-dependent; oxygen insensitive
YP_558343.1	specific inhibitor of chromosomal initiation of replication in vitro; inds the three 13-mers in the origin (oriC) to block initiation of replication; also controls genes involved in arginine transport
YP_558358.1	Citation: Tauch,A., Schneiker,S.,Selbitschka,W., Microbiology (Reading, Engl.) 148 (PT 6),1637-1653 (2002). Schneiker,S., Keller,M., Droge,M.,Lanka,E.,Nucleic Acids Res. 29 (24), 5169-5181 (2001)
YP_558366.1	Citation: Tauch,A., Schneiker,S.,Selbitschka,W., Microbiology (Reading, Engl.) 148 (PT 6),1637-1653 (2002). Schneiker,S., Keller,M., Droge,M.,Lanka,E.,Nucleic Acids Res. 29 (24), 5169-5181 (2001)
YP_558367.1	Citation: Tauch,A., Schneiker,S.,Selbitschka,W., Microbiology (Reading, Engl.) 148 (PT 6),1637-1653 (2002). Schneiker,S., Keller,M., Droge,M.,Lanka,E.,Nucleic Acids Res. 29 (24), 5169-5181 (2001)
YP_558376.1	Gentisate pathway; Citation: J. Bacteriol. 183 (2), 700-708 (2001)
YP_558377.1	Gentisate pathway; Citation: Microbiol. Res. 160 (1), 53-59 (2005). J.Bacteriol. 183 (2), 700-708 (2001)
YP_558378.1	Gentisate pathway; Citation: Microbiol. Res. 160 (1), 53-59 (2005).Gene 312, 239-248 (2003). Appl Environ Microbiol. 1999Mar; 65(3): 946-950. J. Bacteriol. 183 (2), 700- 708(2001)
YP_558394.1	60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; the rhizobia and the high GC gram-positive bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the S. meliloti protein in this cluster is associated with a groES gene and is required for regulation of the early genes involved in nodular formation
YP_558406.1	Gentisate pathway; Citation: J. Bacteriol. 183 (2), 700-708 (2001)
YP_558407.1	Gentisate pathway; Citation: Microbiol. Res. 160 (1), 53-59 (2005). J.Bacteriol. 183 (2), 700-708 (2001)
YP_558408.1	Gentisate pathway; Citation: Microbiol. Res. 160 (1), 53-59 (2005).Gene 312, 239-248 (2003). Appl Environ Microbiol. 1999Mar; 65(3): 946-950. J. Bacteriol. 183 (2), 700- 708(2001)
YP_558424.1	60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; the rhizobia have multiple copies of the groEL gene which are active under different environmental conditions; the S. meliloti protein in this cluster is not associated with a groES gene
YP_558479.1	Citation: Ohtsubo,H., Nyman,K., Doroszkiewicz,W.and Ohtsubo,E.Nature 292 (5824), 640-643 (1981)
YP_558486.1	Catalyzes D-ribose 5-phosphate --> D-ribulose 5-phosphate in the nonoxidative branch of the pentose phosphate pathway
YP_558488.1	Citation: Liu,D., Haase,A.M., Lindqvist,L.,Lindberg, A.A. and Reeves,P.R.J. Bacteriol. 175 (11),3408-3413 (1993)
YP_558499.1	Involved in the biosynthetic pathways of fatty acids, phospholipids, lipopolysaccharides, and oligosaccharides
YP_558512.1	Citation: Priefert,H., O'Brien,X.M., Lessard,P.A., et al Appl. Microbiol. Biotechnol. 65 (2), 168-176 (2004)
YP_558518.1	catalyzes the conversion of dihydroorotate to orotate in the pyrimidine biosynthesis pathway; uses a flavin nucleotide as an essential cofactor; class 2 enzymes are monomeric and compared to the class 1 class 2 possess an extended N terminus, which plays a role in the membrane association of the enzyme and provides the binding site for the respiratory quinones that serve as physiological electron acceptors
YP_558519.1	Conjugates Arg from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate
YP_558520.1	leucyltransferase; phenylalanyltransferse; functions in the N-end rule pathway; transfers Leu, Phe, Met, from aminoacyl-tRNAs to N-terminal of proteins with Arg or Lys
YP_558521.1	Citation: Sheikh,S., O'Handley,S.F., Dunn,C.A. andBessman,M.J.J. Biol. Chem. 273 (33), 20924-20928 (1998)
YP_558523.1	Citation: Paulsen,I.T., Littlejohn,T.G.,Radstrom,P., Sundstrom,L., Skold,O., Swedberg,G. andSkurray, R.A.Antimicrob. Agents Chemother. 37 (4), 761-768(1993)
YP_558528.1	Citation: Sun,Y., Zhou,X., Dong,H., Tu,G., Wang,M., Wang,B. and Deng,Z.Chem. Biol. 10, 431-441 (2003
YP_558530.1	catalyzes the formation of 3-hydroxy-2-methylpropanoate from 3-hydroxy-2-methylpropanoyl-CoA
YP_558532.1	catalyzes the release of sulfite from alkanesulfonates
YP_558550.1	involved in the export of lipooligosaccharides during nodulation
YP_558554.1	Represses a number of genes involved in the response to DNA damage
YP_558565.1	catalyzes the formation of 2-hydroxy-3-oxopropanoate (tartronate semialdehyde) from two molecules of glyoxylate
YP_558567.1	Bacteria have multiple sigma factors which are active under specific conditions; the sigma factor binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription
YP_558569.1	binds cooperatively with S18 to the S15-16S complex, allowing platform assembly to continue with S11 and S21
YP_558571.1	binds as a heterodimer with protein S6 to the central domain of the 16S rRNA; helps stabilize the platform of the 30S subunit
YP_558572.1	in Escherichia coli this protein is wrapped around the base of the L1 stalk
YP_558573.1	unwinds double stranded DNA
YP_558640.1	broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor
YP_558641.1	catalyzes the formation of L-aspartate 4-semialdehyde from L-homoserine
YP_558642.1	catalyzes the formation of L-threonine from O-phospho-L-homoserine
YP_558655.1	RpmE2; there appears to be two types of ribosomal proteins L31 in bacterial genomes; some contain a CxxC motif while others do not; Bacillus subtilis has both types; the proteins in this cluster do not have the CXXC motif; RpmE is found in exponentially growing Bacilli while YtiA was found after exponential growth; expression of ytiA is controlled by a zinc-specific transcriptional repressor; RpmE contains one zinc ion and a CxxC motif is responsible for this binding; forms an RNP particle along with proteins L5, L18, and L25 and 5S rRNA; found crosslinked to L2 and L25 and EF-G; may be near the peptidyltransferase site of the 50S ribosome
YP_558659.1	An RNA-DNA helicase that actively releases nascent mRNAs from paused transcription complexes
YP_558663.1	involved in a recombinational process of DNA repair, independent of the recBC complex
YP_558669.1	catalyzes the conversion of a phosphate monoester to an alcohol and a phosphate
YP_558672.1	sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released; this sigma factor controls a regulon of genes required for protection against external stresses
YP_558674.2	in Escherichia coli this enzyme catalyzes the SAM-dependent methylation of U1939 in the 23S ribomal RNA; binds an iron-sulfur cluster [4Fe-4S]
YP_558680.1	Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; in Rhizobia and Ralstonia is involved in PHB biosynthesis
YP_558681.1	catalyzes the formation of 3-hydroxybutyryl-CoA from acetoacetyl-CoA in polyhydroxyalkanoate synthesis
YP_558685.1	catalyzes the methylthiolation of an aspartic acid residue of the S12 protein of the 30S ribosomal subunit
YP_558687.1	catalyzes the formation of beta-ketovaleryl-CoA from acetyl-CoA and propionyl-CoA
YP_558689.1	catalyzes the formation of L-homocysteine from cystathionine
YP_558692.1	Citation: Cupp-Vickery,J.R., Garcia,C., Hofacre, A.and McGee-Estrada,K.J. Mol. Biol. 311 (1), 101-110 (2001)
YP_558706.1	homopentamer; channel that opens in response to pressure or hypoosmotic shock
YP_558708.1	catalyzes the formation of L-ornithine from N(2)-acetyl-L-ornithine
YP_558710.1	4-diphosphocytidyl-2C-methyl-D-erythritol synthase; MEP cytidylyltransferase; MCT; catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate; involved in isoprenoid and isopentenyl-PP biosynthesis; forms homodimers
YP_558711.1	catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate into 2-C-methyl-D-erythritol 2,4-cyclodiphosphate
YP_558715.1	part of two-component system EnvZ/OmpR; regulates transcription of outer membrane porin genes ompC/F; under high osmolarity EnvZ functions as kinase/phosphotransferase and phosphorylates OmpR; the result is increased expression of ompC and repression of ompF; also functions in regulation of other genes; forms dimers upon phosphorylation
YP_558725.1	Tig; RopA; peptidyl-prolyl cis/trans isomerase; promotes folding of newly synthesized proteins; binds ribosomal 50S subunit; forms a homodimer
YP_558726.1	hydrolyzes proteins to small peptides; with the ATPase subunits ClpA or ClpX, ClpP degrades specific substrates
YP_558727.1	binds and unfolds substrates as part of the ClpXP protease
YP_558734.1	functions in sugar metabolism in glycolysis and the Embden-Meyerhof pathways (EMP) and in gluconeogenesis; catalyzes reversible isomerization of glucose-6-phosphate to fructose-6-phosphate; member of PGI family
YP_558738.1	catalyzes the formation of 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine from N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide and L-glutamine in purine biosynthesis
YP_558743.1	Involved in cell division; probably involved in intracellular septation
YP_558744.1	this stereospecific enzymes reduces the R isomer of methionine sulfoxide while MsrA reduces the S form; provides protection against oxidative stress
YP_558746.1	activates fatty acids by binding to coenzyme A
YP_558748.1	Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation
YP_558753.1	probable dehydrogenase
YP_558758.1	catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to thymidine monophosphate (dTMP) to form thymidine diphosphate (dTDP)
YP_558759.1	catalyzes the DNA-template-directed extension of the 3'-end of a DNA strand; the delta' subunit seems to interact with the gamma subunit to transfer the beta subunit on the DNA
YP_558770.1	Citation: Metcalf,W.W., Steed,P.M. andWanner,B.L.J. Bacteriol. 172 (6), 3191-3200 (1990)
YP_558791.1	70% identity B. pseudomallei
YP_558793.1	Citation: Liu,D., Haase,A.M., Lindqvist,L.,Lindberg, A.A. and Reeves,P.R.J. Bacteriol. 175 (11),3408-3413 (1993)
YP_558798.1	catalyzes the formation of malate from glyoxylate and acetyl-CoA
YP_558823.1	enzyme from Treponema denticola exhibits NADH-dependent trans-2-enoyl-CoA reductase activity
YP_558834.1	Citation: Takeda,Y. and Shimizu,T.J. Ferment.Bioeng. 72, 1-6 (1991)Kondo,K. and Horinouchi, S.Appl.Environ. Microbiol. 63 (3), 1131-1138 (1997).
YP_558841.1	Bacteria have multiple sigma factors which are active under specific conditions; the sigma factor binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription
YP_558848.1	Citation: Flemetakis,E., Agalou,A., Kavroulakis,N., et al. Mol. Plant Microbe Interact. 15 (4), 313-322(2002)
YP_558854.1	Citation: Appia-Ayme,C., Little,P.J., Matsumoto,Y., Leech,A.P. and Berks,B.C.J. Bacteriol. 183 (20), 6107- 6118(2001)
YP_558861.1	Citation: Kahnert,A. and Kertesz,M.A. J. Biol.Chem. 275 (41), 31661-31667 (2000)
YP_558862.1	Citation: Kahnert,A. and Kertesz,M.A. J. Biol.Chem. 275 (41), 31661-31667 (2000)
YP_558863.1	Citation: Kahnert,A. and Kertesz,M.A.J. Biol. Chem.275 (41), 31661-31667 (2000)
YP_558864.1	Citation: Kahnert,A. and Kertesz,M.A. J. Biol.Chem. 275 (41), 31661-31667 (2000)
YP_558865.1	Citation: Denome,S.A., Oldfield,C., Nash,L.J. etal. Bacteriol. 176 (21), 6707-6716 (1994).Piddington,C.S., Kovacevich,B.R. and Rambosek,AEM 61 (2),468-475 (1995). Kahnert,A. and Kertesz,M.A. J. Biol. Chem.275 (41), 31661- 31667 (2000)
YP_558870.1	Citation:  Schubel,U., Kraut,M., Morsdorf,G. andMeyer,O J. Bacteriol. 177 (8), 2197-2203(1995)Santiago, B., Schubel,U., Egelseer,C. andMeyer,O.Gene 236 (1), 115- 124 (1999)
YP_558871.1	Citation: Schubel,U., Kraut,M., Morsdorf,G. andMeyer,O J. Bacteriol. 177 (8), 2197-2203(1995)Santiago, B., Schubel,U., Egelseer,C. andMeyer,O.Gene 236 (1), 115- 124 (1999)
YP_558872.1	Citation: Schubel,U., Kraut,M., Morsdorf,G. andMeyer,O J. Bacteriol. 177 (8), 2197-2203(1995)Santiago, B., Schubel,U., Egelseer,C. andMeyer,O.Gene 236 (1), 115- 124 (1999)
YP_558874.1	96% amino acid identity to the protein described byKing G.M. (AEM, 2003), the latter which is located onmegaplasmid); Citation: Appl. Environ. Microbiol. 69 (12),7257- 7265 (2003)
YP_558900.1	Catalyzes the deamination of cytosine to uracil and ammonia
YP_558903.1	catalyzes the degradation of phosphonoacetaldehyde to acetaldehyde and phosphate
YP_558904.1	catalyzes the formation of phosphonoacetaldehyde from 2-aminoethylphosphonate and pyruvate
YP_558910.1	Citation: Annu Rev Microbiol. 50:553-90 (1996). J.Bacteriol. 179 (16), 5226-5231 (1997)
YP_558911.1	Citation: Annu Rev Microbiol. 50:553-90 (1996).Gene 226 (2), 189-198 (1999)
YP_558912.1	Citation: Annu Rev Microbiol. 1996;50:553-90. Gene226 (2), 189-198 (1999)
YP_558913.1	Citation: Annu Rev Microbiol. 1996;50:553-90
YP_558921.1	Citation: Tralau,T., Cook,A.M. and Ruff, J.Appl.Environ. Microbiol. 67 (4), 1508-1516 (2001)
YP_558924.1	Citation: Watanabe YH, Takano M, Yoshida M.J BiolChem. 2005 Apr 4; [Epub ahead of print]. Shorter J, Lindquist S.Nat Struct Mol Biol. 2005 Jan;12(1):4-6.
YP_558925.1	Citation: Srinivasa Rao,P.S., Yamada,Y., Tan, Y.P.and Leung,K.Y.Mol. Microbiol. 53 (2), 573-586 (2004); similar to virulence factor EvpA
YP_558926.1	Citation: Srinivasa Rao,P.S., Yamada,Y., Tan, Y.P.and Leung,K.Y.Mol. Microbiol. 53 (2), 573-586 (2004); similar to virulence factor EvpB
YP_558929.1	Citation: Srinivasa Rao,P.S., Yamada,Y., Tan, Y.P.and Leung,K.Y.Mol. Microbiol. 53 (2), 573-586 (2004); similar to virulence factor EvpC
YP_558931.1	Citation: Bladergroen MR, Badelt K, Spaink HP.MolPlant Microbe Interact. 2003 Jan;16(1):53-64.
YP_558933.1	Citation: McAdam,R.A., Hermans,P.W., vanSoolingen, D.,et al Mol. Microbiol. 4 (9), 1607-1613 (1990)
YP_558946.1	Citation: Schenk,S., Hoelz,A., Krauss,B. andDecker, K.J. Mol. Biol. 284 (5), 1323-1339 (1998)
YP_558951.1	Citation: Keyhani,N.O. and Roseman,S.Proc. Natl.Acad. Sci. U.S.A. 94 (26), 14367-14371 (1997)
YP_558954.1	part of two component quorum sensing system; Citation: Sperandio,V., Torres,A.G. andKaper, J.B.Mol. Microbiol. 43 (3), 809-821 (2002)
YP_558955.1	part of two component quorum sensing system; Citation: Sperandio,V., Torres,A.G. andKaper, J.B.Mol. Microbiol. 43 (3), 809-821 (2002)
YP_558973.1	Citation: Hoffmaster,A.R., Ravel,J., Rasko,D.A., etal Proc. Natl. Acad. Sci. U.S.A. (2004) 101(22):8449-54
YP_558974.1	Citation: J. Bacteriol. 180 (24), 6529-6537 (1998)
YP_558978.1	catalyzes the formation of protocatechuate from 4-hydroxybenzoate
YP_558979.1	threonine deaminase; threonine dehydratase; in Escherichia coli, IlvA is part of the isoleucine biosynthetic pathway
YP_558981.1	Involved in the biosynthetic pathways of fatty acids, phospholipids, lipopolysaccharides, and oligosaccharides
YP_558984.1	Citation: Vinuesa,P., Neumann-Silkow,F.,Pacios-Bras, C., Spaink,H.P.,Martinez-Romero,E. andWerner,D.Mol. Plant Microbe Interact. 16 (2), 159-168(2003)
YP_559011.1	Citation: Beall,B. and Moran,C.P. Jr.. Bacteriol.176 (7), 2003-2012 (1994.Noback,M.A.,Holsappel, S.,Kiewiet,R.,Terpstra,P.Wambutt,R.,Wedler,H.,Venema,G. and Bron,S.Microbiology (Reading, Engl.) 144 (PT4), 859- 875 (1998)
YP_559012.1	Citation: Pragai,Z. and Harwood, C.R.Microbiology(Reading, Engl.) 148 (PT 5), 1593-1602 (2002)
YP_559013.1	Citation: Fischer,C., Geourjon,C., Bourson,C. andDeutscher,J.Gene 168 (1), 55-60 (1996)
YP_559051.1	Citation: Klein,J.R., Henrich,B. and Plapp, R.Mol.Gen. Genet. 230 (1-2), 230-240 (1991)
YP_559055.1	Acylates the intermediate (KDO)2-lipid IVA to form (KDO)2-(lauroyl)-lipid IVA
YP_559056.1	Citation:  Meberg BM, Sailer FC, Nelson DE, YoungKD. J Bacteriol. 2001 183(20):6148-9.   Denome SA, Elf PK,Henderson TA, Nelson DE, Young KD. J Bacteriol. 1999181(13):3981-93
YP_559058.1	Citation: Kobayashi H, Yamamoto M, AonoR.Microbiology. 1998 Feb;144 ( Pt 2):353-9.
YP_559061.1	Citation: Kamerbeek,N.M., Moonen,M.J., Van DerVen, J.G., Van Berkel,W.J.,  Fraaije,M.W. and Janssen,D.B.Eur. J. Biochem. 268 (9), 2547-2557 (2001)
YP_559081.1	catalyzes the transformation of hydroxyatrazine to N-isopropylammelide and ethylamine in the atrazine degradation pathway.
YP_559088.1	catalyzes the formation of glyoxylate from (S)-ureidoglycolate
YP_559089.1	catalyzes the formation of S-ureidoglycolate and urea from allantoate
YP_559096.1	catalyzes the release of D-alanine from L-alanyl-D-glutamyl-meso-diaminopimelyl-D-alanine
YP_559098.1	SP/TREMBL, no PFAM, COGS. B. cepacia id asmetal- accepting chemotaxis protein does not stand -significantly larger proteins.
YP_559115.1	LemA family protein
YP_559132.1	produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a catalytic subunit
YP_559134.1	produces ATP from ADP in the presence of a proton gradient across the membrane; subunit C is part of the membrane proton channel F0
YP_559135.1	produces ATP from ADP in the presence of a proton gradient across the membrane; subunit A is part of the membrane proton channel F0
YP_559137.1	produces ATP from ADP in the presence of a proton gradient across the membrane; the epsilon subunit is part of the catalytic core of the ATP synthase complex
YP_559138.1	produces ATP from ADP in the presence of a proton gradient across the membrane; the beta chain is a regulatory subunit
YP_559141.1	catalyzes the degradation of arginine to citruline and ammonia
YP_559143.1	reversible synthesis of carbamate and ATP from carbamoyl phosphate and ADP
YP_559145.1	Containing CBS domains
YP_559161.1	in group A Streptococci this protein was found to cross react with anti myosin antibodies and may play a role in rheumatic fever
YP_559179.1	catalyzes the formation of acetate from pyruvate
YP_559181.1	YghU; B2989; one of eight  glutathione transferases from E. coli
YP_559189.1	Weak similarity to coenzyme PQQ synthesis proteinC
YP_559210.1	Partial similarity to helicases
YP_559241.1	Citation: Tauch,A., Schneiker,S.,Selbitschka,W., Microbiology (Reading, Engl.) 148 (PT 6),1637-1653 (2002). Schneiker,S., Keller,M., Droge,M.,Lanka,E.,Nucleic Acids Res. 29 (24), 5169-5181 (2001)
YP_559242.1	Citation: Tauch,A., Schneiker,S.,Selbitschka,W., Microbiology (Reading, Engl.) 148 (PT 6),1637-1653 (2002). Schneiker,S., Keller,M., Droge,M.,Lanka,E.,Nucleic Acids Res. 29 (24), 5169-5181 (2001)
YP_559243.1	Citation: Tauch,A., Schneiker,S.,Selbitschka,W., Microbiology (Reading, Engl.) 148 (PT 6),1637-1653 (2002). Schneiker,S., Keller,M., Droge,M.,Lanka,E.,Nucleic Acids Res. 29 (24), 5169-5181 (2001)
YP_559264.1	specific inhibitor of chromosomal initiation of replication in vitro; inds the three 13-mers in the origin (oriC) to block initiation of replication; also controls genes involved in arginine transport
YP_559284.1	possibly involved in scaffolding for murein- synthesizing holoenzyme
YP_559299.1	contains glutamine-hydrolyzing domain and glutamine amidotransferase; GMP-binding domain; functions to produce GMP from XMP in the IMP pathway
YP_559301.1	catalyzes the synthesis of xanthosine monophosphate by the NAD+ dependent oxidation of inosine monophosphate
YP_559305.1	binds to ssrA RNA (tmRNA) and is required for its successful binding to ribosomes; also appears to function in the trans-translation step by promoting accommodation of tmRNA into the ribosomal A site; SmpB protects the tmRNA from RNase R degradation in Caulobacter crescentus; both the tmRNA and SmpB are regulated in cell cycle-dependent manner; functions in release of stalled ribosomes from damaged mRNAs and targeting proteins for degradation
YP_559308.1	catalyzes the formation of phosphoenolpyruvate from pyruvate
YP_559311.1	RNH2; RNase HII; binds manganese; endonuclease which specifically degrades the RNA of RNA-DNA hybrids
YP_559312.1	catalyzes the formation of lipid A disaccharide from UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate, lipid A disaccharide is a precursor of lipid A that anchors LPS to the OM
YP_559313.1	catalyzes the addition of (R)-3-hydroxytetradecanoyl to the glucosamine disaccharide in lipid A biosynthesis
YP_559314.1	in Pseudomonas aeruginosa this enzyme is a trimer of dimers; essential for membrane formation; performs third step of type II fatty acid biosynthesis; catalyzes dehydration of (3R)-hydroxyacyl-ACP to trans-2-acyl-ACP
YP_559315.1	adds the O-linked and N-linked 3(R)-hydroxy fatty acids to the glucosamine disaccharide during lipid A biosynthesis
YP_559319.1	catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate
YP_559322.1	Rrf; Frr; ribosome-recycling factor; release factor 4; RF4; recycles ribosomes upon translation termination along with release factor RF-3 and elongation factor EF-G; A GTPase-dependent process results in release of 50S from 70S; inhibited by release factor RF-1; essential for viability; structurally similar to tRNAs
YP_559323.1	Catalyzes the phosphorylation of UMP to UDP
YP_559324.1	EF-Ts; functions during elongation stage of protein translation; forms a dimer; associates with EF-Tu-GDP complex and promotes exchange of GDP to GTP resulting in regeneration of the active form of EF-Tu
YP_559325.1	one of the last subunits in the assembly of the 30S subunit; absence of S2 does not inhibit assembly but results in an inactive subunit
YP_559327.1	catalyzes the removal of N-terminal amino acids from peptides and arylamides; generally Co(II) however activity has been shown for some methionine aminopeptidases with Zn, Fe, or Mn
YP_559328.1	catalyzes the uridylylation or deuridylylation of the PII nitrogen regulatory protein
YP_559330.1	cleaves off formyl group from N-terminal methionine residues of newly synthesized proteins; binds iron(2+)
YP_559336.1	catalyzes the formation of succinyldiaminopimelate from N-succinyl-2-amino-6-ketopimelate
YP_559337.1	catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway
YP_559339.1	dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE), catalyzes the hydrolysis of N-succinyl-L,Ldiaminopimelate L,L-SDAP to L,L-diaminopimelate and succinate. It is a metalloprotease containing dinuclear active sites. Its structure is similar to the carboxypeptidase G2 from Pseudomonas sp. strain RS-16 and the aminopeptidase from Aeromonas proteolytica.
YP_559340.1	involved in methylation of ribosomal protein L3
YP_559341.1	catalyzes the transfer of a phosphatidyl group to phosphodidylglycerol to form cardiolipin (diphosphatidylglycerol)
YP_559346.1	Sms; stabilizes the strand-invasion intermediate during the DNA repair; involved in recombination of donor DNA and plays an important role in DNA damage repair after exposure to mutagenic agents
YP_559347.1	converts L-alanine to D-alanine which is used in cell wall biosynthesis; binds one pyridoxal phosphate per monomer; forms a homodimer
YP_559360.1	Catalyzes the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle
YP_559362.1	regulator of RNase E; increases half-life and abundance of RNAs; interacts with RNase E possibly inhibiting catalytic activity
YP_559365.1	Charges one glutamine molecule and pairs it to its corresponding RNA trinucleotide during protein translation
YP_559372.1	Catalyzes a key regulatory step in fatty acid biosynthesis
YP_559377.1	catalyzes the formation of 4-phospho-L-aspartate from L-aspartate and ATP, in Bacillus, lysine sensitive; regulated by response to starvation.
YP_559379.1	catalyzes the carboxylation of acetyl-CoA to malonyl-CoA; forms a tetramer composed of two alpha (AccA) and two beta (AccD) subunits; one of the two catalytic subunits that can form the acetyl CoA carboxylase enzyme together with a carrier protein
YP_559381.1	catalyzes a two-step reaction; charges a cysteine by linking its carboxyl group to the alpha-phosphate of ATP then transfers the aminoacyl-adenylate to its tRNA
YP_559382.1	Tetratricopeptide repeat present
YP_559385.1	catalyzes the formation of 2,3=diacylglucosamine 1-phosphate from UDP-2,3=diacylglucosamine
YP_559390.1	This protein performs the mismatch recognition step during the DNA repair process
YP_559401.1	catalyzes the formation of N6-(1,2,-dicarboxyethyl)-AMP from L-aspartate, inosine monophosphate and GTP in AMP biosynthesis
YP_559402.1	May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine
YP_559408.1	Stimulates the elongation of poly(A) tails
YP_559409.1	EngA; essential Neisserial GTPase; synchronizes cellular events by interacting with multiple targets with tandem G-domains; overexpression in Escherichia coli suppresses rrmJ mutation; structural analysis of the Thermotoga maritima ortholog shows different nucleotide binding affinities in the two binding domains
YP_559412.1	catalyzes a two-step reaction, first charging a histidine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; class II aminoacyl-tRNA synthetase; forms homodimers; some organisms have a paralogous gene, hisZ, that is similar to hisS and produces a protein that performs the first step in histidine biosynthesis along with HisG
YP_559413.1	catalyzes the conversion of 2C-methyl-D-erythritol 2,4-cyclodiphosphate into 4-hydroxy-3-methyl-2-en-1-yl diphosphate; involved in isoprenoid synthesis
YP_559416.1	catalyzes the formation of nucleoside triphosphate from ATP and nucleoside diphosphate
YP_559422.1	catalyzes the formation of dihydrodipicolinate from L-aspartate 4-semialdehyde and pyruvate in lysine and diaminopimelate biosynthesis
YP_559424.1	catalyzes a two-step reaction, first charging a tryptophan molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA
YP_559427.1	Phosphoesterase PHP domain present
YP_559433.1	forms a complex with FtsL and FtsQ; colocalizes to the septal region of the dividing cell; membrane protein
YP_559434.1	enolase; catalyzes the formation of phosphoenolpyruvate from 2-phospho-D-glycerate in glycolysis
YP_559435.1	catalyzes the formation of 2-dehydro-3-deoxy-D-octonate 8-phosphate from phosphoenolpyruvate and D-arabinose 5-phosphate in LPS biosynthesis
YP_559436.1	CTP synthase; cytidine triphosphate synthetase; catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen; in Escherichia coli this enzyme forms a homotetramer
YP_559446.1	class II; LysRS2; catalyzes a two-step reaction, first charging a lysine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Methanosarcina barkeri, LysRS2 charges both tRNA molecules for lysine that exist in this organism and in addition can charge the tRNAPyl with lysine in the presence of LysRS1
YP_559450.1	involved in the maturation of iron-sulfur cluster-containing proteins
YP_559451.1	J-type co-chaperone that regulates the ATPase and peptide-binding activity of Hsc66 chaperone; may function in biogenesis of iron-sulfur proteins
YP_559454.1	catalyzes the removal of elemental sulfur from cysteine to produce alanine; involved in NAD biosynthesis
YP_559466.1	E1 component; part of pyruvate dehydrogenase; forms a complex with DlaT and LpdC
YP_559471.1	catalyzes the formation of 5,10-methenyltetrahydrofolate from 5,10-methylenetetrahydrofolate and subsequent formation of 10-formyltetrahydrofolate from 5,10-methenyltetrahydrofolate
YP_559474.1	Catalyzes the deamination of cytosine to uracil and ammonia
YP_559492.1	Haemagluttinin motif present
YP_559494.1	catalyzes the formation of N-acetyl-L-glutamate from L-glutamate and acetyl-CoA in arginine biosynthesis
YP_559510.1	Enables the enzymatic reduction of mercuric ions to elemental mercury
YP_559524.1	catalyzes the degradation of histidine to urocanate and ammmonia
YP_559557.1	required for the synthesis of the hydromethylpyrimidine moiety of thiamine
YP_559575.1	catalyzes the hydrolytic cleavage of hydantoin with aromatic side chains at the 5'position
YP_559577.1	catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines
YP_559578.1	function undetermined; similar to glutamate synthase beta subunit and related oxidoreductases which transfer electrons from NADPH to an acceptor protein or protein domain
YP_559579.1	allantoate amidohydrolase and N-carbamoyl-L-amino acid amidohydrolase are very similar; the allantoate amidohydrolase from Escherichia coli forms a dimer and binds zinc ions for catalytic activity and catalyzes the conversion of allantoate to (S)-ureidoglycolate and ammonia; carbamoyl amidohydrolase from Bacillus sp. converts N-carbamoyl amino acids to amino acids, ammonia, and carbon dioxide
YP_559582.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Mol. Microbiol. 2004 Oct;54(1):223-38. Appl EnvironMicrobiol. 2004 Aug;70(8):4961-70.
YP_559583.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Mol. Microbiol. 2004 Oct;54(1):223-38. Appl EnvironMicrobiol. 2004 Aug;70(8):4961-70.
YP_559584.1	cleaves the ring of 2,3-dihydro-2,3-dihydroxybenzoyl-CoA forming 6-hydroxy-3-hexenoyl-CoA
YP_559585.1	consists of N-terminal helix-turn-helix domain and C-terminal shikimate kinase-like domain which may bind benzoyl-CoA; controls inducible expression of the bzd catabolic operon that is involved in the anaerobic catabolism of benzoate
YP_559586.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Appl Environ Microbiol. 2004 Aug;70(8):4961-70.
YP_559587.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Appl Environ Microbiol. 2004 Aug;70(8):4961-70.
YP_559588.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Appl Environ Microbiol. 2004 Aug;70(8):4961-70.
YP_559589.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Appl Environ Microbiol. 2004 Aug;70(8):4961-70.
YP_559592.1	weak similarity to monoxygenases
YP_559597.1	Radical SAM domain present
YP_559628.1	This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control
YP_559629.1	catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a tetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 2 subfamily
YP_559630.2	catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a heterotetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 1 subfamily
YP_559631.1	binds directly to 23S ribosomal RNA prior to in vitro assembly of the 50S ribosomal subunit
YP_559634.1	catalyzes a two-step reaction, first charging a threonine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; catalyzes the formation of threonyl-tRNA(Thr) from threonine and tRNA(Thr)
YP_559636.1	Endoribonuclease L-PSP domain present
YP_559644.1	Tetratricopeptide repeat present
YP_559645.1	catalyzes the formation of chorismate from 5-O-(1-carboxyvinyl)-3-phosphoshikimate in aromatic amino acid biosynthesis
YP_559647.1	CBS domain present
YP_559648.1	catalyzes the formation of L-methionine and acetate from O-acetyl-L-homoserine and methanethiol
YP_559666.1	catalyzes the formation of propionyl-CoA using propionate as a substrate; PrpE from Ralstonia solanacearum can produce acetyl-, propionyl-, butyryl- and acrylyl-coenzyme A, and Salmonella enterica produces propionyl- and butyryl-coenzyme A; not expressed in Escherichia coli when grown on propionate/minimal media; ATP-dependent
YP_559667.1	enables the cleavage of the glycosidic bond in both 5'-methylthioadenosine and S-adenosylhomocysteine
YP_559670.1	valine--tRNA ligase; ValRS; converts valine ATP and tRNA(Val) to AMP PPi and valyl-tRNA(Val); class-I aminoacyl-tRNA synthetase type 1 subfamily; has a posttransfer editing process to hydrolyze mischarged Thr-tRNA(Val) which is done by the editing domain
YP_559672.1	SirA-like domain present
YP_559694.1	Catalyzes a two-step reaction, first charging an alanyl molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA
YP_559698.1	catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA
YP_559706.1	phosphatase activity in Escherichia coli not kinase; involved in bacitracin resistance as bacitracin supposedly sequesters UDP disphosphate which reduces the pool of lipid carrier available to the cell
YP_559711.1	Pentapeptide repeat present
YP_559732.1	catalyzes the reversible transfer of the terminal phosphate of ATP to form a long chain polyphosphate
YP_559736.1	ATP-binding protein; PstABCS is an ATP dependent phosphate uptake system which is responsible for inorganic phosphate uptake during phosphate starvation
YP_559737.1	Part of the ABC transporter complex PstABCS responsible for inorganic phosphate (Pi) uptake under Pi starvation conditions
YP_559738.1	part of the ATP-dependent phosphate uptake system PstABCS responsible for inorganic phosphate (Pi) uptake under Pi starvation conditions
YP_559741.1	catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate
YP_559747.1	necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites; arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus
YP_559748.1	four CarB-CarA dimers form the carbamoyl phosphate synthetase holoenzyme that catalyzes the production of carbamoyl phosphate; CarB is responsible for the amidotransferase activity
YP_559749.1	catalyzes production of carbamoyl phosphate from bicarbonate and glutamine in pyrimidine and arginine biosynthesis pathways; forms an octamer composed of four CarAB dimers
YP_559755.1	3'-5' exonuclease of DNA polymerase III
YP_559781.1	binds to single stranded DNA and may facilitate the binding and interaction of other proteins to DNA
YP_559782.1	decatenates replicating daughter chromosomes
YP_559805.1	weak similarity to pilin, pilL protein
YP_559838.1	Citation: J. Bacteriol. 173 (1), 168-175 (1991)
YP_559848.1	catalyzes the formation of pyruvate and acetaldehyde from 4-hydroxy-2-ketovaleric acid; involved in the degradation of phenylpropionate
YP_559849.1	catalyzes the formation of acetyl-CoA from acetalaldehyde
YP_559850.1	Citation: Arch Microbiol. 2000 Oct;174(4):265-72
YP_559851.1	Citation: Arch Microbiol. 2000 Oct;174(4):265-72
YP_559852.1	Citation: Arch Microbiol. 2000 Oct;174(4):265-72
YP_559853.1	Citation: Arch Microbiol. 2000 Oct;174(4):265-72
YP_559854.1	Citation: Arch Microbiol. 2000 Oct;174(4):265-72
YP_559855.1	Citation: Arch Microbiol. 2000 Oct;174(4):265-72
YP_559874.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_559879.1	lipoprotein signal peptidase; integral membrane protein that removes signal peptides from prolipoproteins during lipoprotein biosynthesis
YP_559880.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_559881.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_559886.1	YCII-related domain present
YP_559889.1	Citation: Appl Environ Microbiol. 1999May;65(5):2151-62
YP_559890.1	Rieske-type ring-hydroxylating dioxygenase, beta subunit; Citation: Appl Environ Microbiol. 1999May;65(5):2151-62
YP_559891.1	Rieske-type ring hydroxylating dioxygenase, alpha subunit; Citation: Appl Environ Microbiol. 1999May;65(5):2151-62
YP_559892.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_559893.1	lipoprotein signal peptidase; integral membrane protein that removes signal peptides from prolipoproteins during lipoprotein biosynthesis
YP_559894.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_559895.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_559896.1	Rieske [2Fe-2S] domain
YP_559900.1	YCII-related domain
YP_559903.1	The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision
YP_559905.1	Involved in peptide bond synthesis; alters the affinity of the ribosome for aminoacyl-tRNA
YP_559906.1	Weak similarity to CsbD-like domain, involved ingeneral stress response
YP_559908.1	hydrolyzes the terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides
YP_559909.1	Catalyzes the formation of holo-ACP, which mediates the essential transfer of acyl fatty acid intermediates during the biosynthesis of fatty acids and lipids
YP_559910.1	involved in the de novo synthesis of pyridoxine (Vitamin B6)
YP_559911.1	involved in DNA repair and RecFOR pathway recombination; RecFOR proteins displace ssDNA-binding protein and facilitate the production of RecA-coated ssDNA
YP_559912.1	Era; Escherichia coli Ras-like protein; Bex; Bacillus Era-complementing segment; essential protein in Escherichia coli that is involved in many cellular processes; GTPase; binds the cell membrane through apparent C-terminal domain; mutants are arrested during the cell cycle; Streptococcus pneumoniae Era binds to RNA and Escherichia coli Era binds 16S rRNA and 30S ribosome
YP_559913.1	cytoplasmic enzyme involved in processing rRNA and some mRNAs; substrates typically have dsRNA regions; forms a homodimer; have N-terminal nuclease and C-terminal RNA-binding domains; requires magnesium as preferred ion for activity
YP_559915.1	binds to the ribosome on the universally-conserved alpha-sarcin loop
YP_559920.1	Member of the extracytoplasmic function sigma factors which are active under specific conditions; binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription; this sigma factor is involved in heat shock and oxidative stress response
YP_559922.1	FabF; beta-ketoacyl-ACP synthase II, KASII; catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP; required for the elongation of short-chain unsaturated acyl-ACP
YP_559923.1	carries the fatty acid chain in fatty acid biosynthesis
YP_559924.1	Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis
YP_559926.1	FabH; beta-ketoacyl-acyl carrier protein synthase III; catalyzes the condensation of acetyl-CoA with malonyl-ACP to initiate cycles of fatty acid elongation; differs from 3-oxoacyl-(acyl carrier protein) synthase I and II in that it utilizes CoA thioesters as primers rather than acyl-ACPs
YP_559927.1	involved in acylation of glycerol-3-phosphate to form 1-acyl-glycerol-3 phosphate for use in phospholipid biosynthesis; functions with PlsY
YP_559928.1	some L32 proteins have zinc finger motifs consisting of CXXC while others do not
YP_559930.1	Maf; overexpression in Bacillus subtilis inhibits septation in the dividing cell
YP_559931.1	Weak similarity to tetrapyrrole (Corrin/Porphyrin)methyltransferase
YP_559938.1	together with moaC, is involved in the conversion of a guanosine derivative (GXP) into molybdopterin precursor Z
YP_559939.1	in Escherichia coli MobA links a guanosine 5'-phosphate to molydopterin to form molybdopterin guanine dinucleotide during molybdenum cofactor biosynthesis
YP_559947.1	catalyzes the formation of nictonate and 5-phospho-alpha-D-ribose 1-diphosphate from nicotinate D-ribonucleotide and diphosphate
YP_559961.1	class II family (does not require metal); tetrameric enzyme; fumarase C; reversibly converts (S)-malate to fumarate and water; functions in the TCA cycle
YP_559968.1	ThyA; catalyzes formation of dTMP and 7,8-dihydrofolate from 5,10-methylenetetrahydrofolate and dUMP; involved in deoxyribonucleotide biosynthesis; there are 2 copies in some Bacilli, one of which appears to be phage-derived
YP_559982.1	forms a trimer; related to eukaryotic protein gephyrin; functions during molybdenum cofactor biosynthesis
YP_559983.1	3'-5' exoribonuclease specific for small oligoribonuclotides
YP_559985.1	EngC; RsgA; CpgA; circularly permuted GTPase; ribosome small subunit-dependent GTPase A; has the pattern G4-G1-G3 as opposed to other GTPases; interacts strongly with 30S ribosome which stimulates GTPase activity
YP_559988.1	catalyzes the formation of adenosylcobinamide-phosphate from adenosylcobyric acid
YP_559990.1	this protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site
YP_559991.1	methylates guanosine-37 in various tRNAs; uses S-adenosyl-L-methionine to transfer methyl group to tRNA
YP_559992.1	Essential for efficient processing of 16S rRNA
YP_559993.1	binds to lower part of 30S body where it stabilizes two domains; required for efficient assembly of 30S; in Escherichia coli this protein has nuclease activity
YP_559996.1	Radical SAM domain present
YP_559998.1	catalyzes the oxidative deamination of D-amino acids
YP_560004.1	part of the metNIQ transport system for methionine
YP_560006.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_560009.1	catalyzes the formation of cysteine from 3-O-acetyl-L-serine and hydrogen sulfide
YP_560010.1	Helix-hairpin-helix motif present
YP_560014.1	TPR domain present
YP_560016.1	This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control
YP_560017.2	in Escherichia coli this protein is involved in binding to the leader sequence of mRNAs and is itself bound to the 30S subunit; autoregulates expression via a C-terminal domain; in most gram negative organisms this protein is composed of 6 repeats of the S1 domain while in gram positive there are 4 repeats; the S1 nucleic acid-binding domain is found associated with other proteins
YP_560018.1	Catalyzes the formation of (d)CDP from ATP and (d)CMP
YP_560019.1	catalyzes the formation of 5-O-(1-carboxyvinyl)-3-phosphoshikimate from phosphoenolpyruvate and 3-phosphoshikimate in tryptophan biosynthesis
YP_560021.1	catalyzes the formation of L-histidinol phosphate from imidazole-acetol phosphate and glutamate in histidine biosynthesis
YP_560023.2	catalyzes the formation of 3-phosphonooxypyruvate and glutamate from O-phospho-L-serine and 2-oxoglutarate; required both in major phosphorylated pathway of serine biosynthesis and in the biosynthesis of pyridoxine
YP_560025.1	negatively supercoils closed circular double-stranded DNA
YP_560027.1	Involved in ubiquinone biosynthesis
YP_560039.1	TPR domain present
YP_560046.1	catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia
YP_560047.1	disulfide oxidoreductase; integral membrane protein; required for perioplasmic disulfide bond formation; oxidizes DsbA protein
YP_560051.1	catalyzes the formation of inosine from adenosine
YP_560052.1	Catalyzes the deamination of guanine
YP_560058.1	FabB; beta-ketoacyl-ACP synthase I, KASI; catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP; required for the elongation of short-chain unsaturated acyl-ACP
YP_560060.1	weak similarity to dehydrase family
YP_560061.1	FabB; beta-ketoacyl-ACP synthase I, KASI; catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP; required for the elongation of short-chain unsaturated acyl-ACP
YP_560066.1	Transmembrane and glycosyl transferase domains
YP_560069.1	carries the fatty acid chain in fatty acid biosynthesis
YP_560076.1	Helix-turn-helix motif present
YP_560077.1	catalyzes the formation of D-fructose 6-phosphate from fructose-1,6-bisphosphate
YP_560082.1	catalyzes the interconversion of chorismate to prephenate
YP_560088.1	necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites; arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus
YP_560091.1	Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits
YP_560092.1	Essential for recycling GMP and indirectly, cGMP
YP_560094.1	RNase PH; tRNA nucleotidyltransferase; forms hexamers in Bacillus subtilis; phosphoroltic 3'-5' exoribonuclease; involved in maturation of tRNA precursors and removes terminal nucleotides near CCA acceptor arms of mature tRNAs
YP_560095.1	HAM1-like protein; Rec-dependent growth; RgdB; yggV; it is suspected that this protein functions to remove misincorporated bases such as xanthine or hypoxanthine
YP_560096.1	catalyzes the oxygen-independent formation of protoporphyrinogen-IX from coproporphyrinogen-III
YP_560097.1	Endoribonuclease L-PSP domain present
YP_560101.1	Converts (S)-4-amino-5-oxopentanoate to 5-aminolevulinate during the porphyrin biosynthesis pathway
YP_560103.1	catalyzes the formation of riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazine
YP_560104.1	bifunctional enzyme DHBP synthase/GTP cyclohydrolase II-like protein; functions in riboflavin synthesis
YP_560105.1	RibE; 6,7-diimethyl-8-ribityllumazine synthase; DMRL synthase; lumazine synthase; beta subunit of riboflavin synthase; condenses 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate to generate 6,6-dimethyl-8-lumazine (DMRL); riboflavin synthase then uses 2 molecules of DMRL to produce riboflavin (vitamin B12); involved in the last steps of riboflavin biosynthesis; forms a 60mer (icosahedral shell) in both Bacillus subtilis and Escherichia coli; in Bacillus subtilis this 60mer is associated with the riboflavin synthase subunit (alpha) while in Escherichia coli it is not
YP_560106.1	Regulates rRNA biosynthesis by transcriptional antitermination
YP_560111.1	catalyzes the formation of 2-oxobutanoate from L-threonine or the formation of pyruvate from serine
YP_560127.1	tRNA (guanine-N(7)-)-methyltransferase; catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA by transferring the methyl residue from S-adenosyl-L-methionine
YP_560128.1	BacA; phosphatase activity in Escherichia coli not kinase; involved in bacitracin resistance as bacitracin supposedly sequesters UDP disphosphate which reduces the pool of lipid carrier available to the cell
YP_560131.1	catalyzes the oxygen-independent formation of protoporphyrinogen-IX from coproporphyrinogen-III
YP_560137.1	Weak similarity to helicase domain proteins
YP_560157.1	catalyzes the formation of 3,6-dideoxy-D-glycero-D-glycero-4-hexulose
YP_560159.1	DapATase; functions in arginine biosynthetic pathway; catalyzes the formation of N-acetyl-L-glutamate 5-semialdehyde from 2-oxoglutarate and N(2)-acetyl-L-ornithine
YP_560166.1	catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP); functions in the nonmevalonate isoprenoid biosynthesis pathway
YP_560168.1	Involved in DNA double-strand break repair and recombination. Promotes the annealing of complementary single-stranded DNA and by simulation of RAD51 recombinase
YP_560169.1	required for 70S ribosome assembly
YP_560170.1	in Escherichia coli BM108, a mutation that results in lack of L33 synthesis had no effect on ribosome synthesis or function; there are paralogous genes in several bacterial genomes, and a CXXC motif for zinc binding and an upstream regulation region of the paralog lacking this motif that are regulated by zinc similar to other ribosomal proteins like L31; the proteins in this group lack the CXXC motif
YP_560171.1	catalyzes the formation of oxaloacetate from L-aspartate
YP_560172.1	catalyzes the formation of pyridine-2,3-dicarboxylate and 5-phospho-alpha-D-ribose 1-diphosphate from nictinate D-ribonucleotide
YP_560173.1	3 different subfamilies; catalyzes the formation of quinolinate from iminoaspartate and dihydroxyacetone phosphate
YP_560178.1	catalyzes the formation of FMN from riboflavin and the formation of FAD from FMN; in Bacillus the ribC gene has both flavokinase and FAD synthetase activities
YP_560179.1	IleRS; catalyzes the formation of isoleucyl-tRNA(Ile) from isoleucine and tRNA(Ile); since isoleucine and other amino acids such as valine are similar, there are additional editing function in this enzyme; one is involved in hydrolysis of activated valine-AMP and the other is involved in deacylation of mischarged Val-tRNA(Ile); there are two active sites, one for aminoacylation and one for editing; class-I aminoacyl-tRNA synthetase family type 1 subfamily; some organisms carry two different copies of this enzyme
YP_560180.1	lipoprotein signal peptidase; integral membrane protein that removes signal peptides from prolipoproteins during lipoprotein biosynthesis
YP_560181.1	catalyzes the conjugation of cysteine to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, which is then decarboxylated to form 4'-phosphopantotheine
YP_560183.1	catalyzes the formation of dUMP from dUTP
YP_560186.1	involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation; binds to the N-terminal domain of the chaperone ClpA
YP_560189.1	Converts isocitrate to alpha ketoglutarate
YP_560193.1	EF-G; promotes GTP-dependent translocation of the ribosome during translation; many organisms have multiple copies of this gene
YP_560208.1	EAL domain present
YP_560218.1	bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides
YP_560220.1	Transfers the gamma-phosphate of ATP to the 4' position of a tetraacyldisaccharide 1-phosphate intermediate to form tetraacyldisaccharide 1,4'-bis-phosphate
YP_560222.2	CMP-2-keto-3-deoxyoctulosonic acid synthetase; catalyzes the formation of CMP-3-deoxy-D-manno-octulosonate from CTP and 3-deoxy-D-manno-octulosonate which is incorporated into LPS
YP_560223.1	essential enzyme that recycles AMP in active cells; converts ATP and AMP to two molecules of ADP
YP_560227.1	binds directly to the 16S rRNA and is involved in post-translational inhibition of arginine and ornithine decarboxylase
YP_560229.1	catalyzes the formation of L-citrulline from carbamoyl phosphate and L-ornithine in arginine biosynthesis and degradation
YP_560230.1	catalyzes the formation of 2-N(omega)-(L-arginino)succinate from L-citrulline and L-aspartate in arginine biosynthesis, AMP-forming
YP_560231.1	catalyzes the reduction of UDP-N-acetylglucosamine enolpyruvate to form UDP-N-acetylmuramate in peptidoglycan biosynthesis
YP_560232.1	nucleotide binding property based on structural studies of Haemophilus influenzae crystallized protein in PDB Accession Number 1IN0 and NMR studies of Escherichia coli YajQ; the YajQ protein from Pseudomonas synringae appears to play a role in activation of bateriophage phi6 segment L transcription
YP_560233.1	involved in acylation of glycerol-3-phosphate to form 1-acyl-glycerol-3 phosphate for use in phospholipid biosynthesis; functions with PlsX
YP_560234.1	YbaK/prolyl-tRNA synthetase associated domain
YP_560236.1	site-specific tyrosine recombinase which cuts and rejoins DNA molecules; binds cooperatively to specific DNA consensus sites; forms a heterotetrameric complex with XerC; XerCD exhibit similar sequences; essential to convert chromosome dimers to monomers during cell division and functions during plasmid segregation; XerD specifically exchanges the bottom strands; cell division protein FtsK may regulate the XerCD complex; enzyme from Streptococcus group has unusual active site motifs
YP_560242.1	Pirin, N-terminal, domain present
YP_560245.1	catalyzes the formation of pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate
YP_560251.1	Citation: Mol Microbiol. 2004 Apr;52(2):371-84.
YP_560258.1	sugar-binding domain present
YP_560261.1	FAD-linked oxidase, N-terminal, domain present
YP_560267.1	Converts D-sorbitol to L-sorbose
YP_560273.1	Function confirmed by biochemical assay & mutantanalysis; Citation: J Bacteriol, 186:2173-2178
YP_560289.1	similarity to sterol desaturase family
YP_560292.1	With PurE catalyzes the conversion of aminoimidazole ribonucleotide to carboxyaminoimidazole ribonucleotide in the de novo purine nucleotide biosynthetic pathway
YP_560294.1	catalyzes the formation of (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate and L-aspartate in purine biosynthesis; SAICAR synthase
YP_560295.1	class II aldolase; catalyzes the reversible aldol condensation of dihydroxyacetonephosphate and glyceraldehyde 3-phosphate in the Calvin cycle, glycolysis and gluconeogenesis
YP_560296.1	catalyzes the formation of phosphoenolpyruvate from pyruvate
YP_560297.1	Converts 3-phospho-D-glycerate to 3-phospho-D-glyceroyl phosphate during the glycolysis pathway
YP_560299.1	involved in branched-chain amino acid transport
YP_560300.1	catalyzes the transamination of the branched-chain amino acids to their respective alpha-keto acids
YP_560307.1	MoaC; along with MoaA is involved in conversion of a guanosine derivative into molybdopterin precursor Z; involved in molybdenum cofactor biosynthesis
YP_560311.1	Catalyzes the only substrate-level phosphorylation in the TCA cycle
YP_560312.1	catalyzes the interconversion of succinyl-CoA and succinate
YP_560315.1	catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs
YP_560347.1	in Escherichia coli this homodimeric enzyme is expressed under aerobic conditions; anaerobic expression is repressed by the arcAB system; converts sn-glycerol-3-phosphate and ubiquinone-8 to dihydroxy acetone phosphate and ubiquinol-8; associates with the cytoplasmic membrane
YP_560348.1	Converts glycerol and ADP to glycerol-3-phosphate and ADP
YP_560356.1	catalyzes the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine from N6-(dimethylallyl)adenosine (i(6)A)
YP_560359.1	involved in cation transport
YP_560361.1	Transfers the fatty acyl group on membrane lipoproteins
YP_560367.1	involved in de novo purine biosynthesis
YP_560369.1	endonuclease; resolves Holliday structures; forms a complex of RuvABC; the junction binding protein RuvA forms a hexameric ring along with the RuvB helicase and catalyzes branch migration; RuvC then interacts with RuvAB to resolve the Holliday junction by nicking DNA strands of like polarity
YP_560370.1	plays an essential role in ATP-dependent branch migration of the Holliday junction
YP_560371.1	promotes strand exchange during homologous recombination; RuvAB complex promotes branch migration; RuvABC complex scans the DNA during branch migration and resolves Holliday junctions at consensus sequences; forms hexameric rings around opposite DNA arms; requires ATP for branch migration and orientation of RuvAB complex determines direction of migration
YP_560374.1	hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr); possible defense mechanism against a harmful effect of D-tyrosine
YP_560375.1	catalyzes the formation of tyrosyl-tRNA(Tyr) from tyrosine and tRNA(Tyr)
YP_560376.1	catalyzes hydrolysis of 1,6-anhydro bond of anyhydro-N-acetylmuramic acid (anhMurNAc) and phosphorylates anhMurNAc to produce N-acetyl-muramate-6-phosphate; involved in murein recycling
YP_560377.1	essential respiratory protein A; may be involved in the transfer of iron-sulfur clusters; essential for growth using oxygen or alternate electron acceptors
YP_560378.1	forms a direct contact with the tRNA during translation
YP_560379.1	in Escherichia coli this protein is one of the earliest assembly proteins in the large subunit
YP_560383.1	catalyzes the formation of N-carbamoyl-L-aspartate from (S)-dihydroorotate in pyrimidine biosynthesis
YP_560392.1	Catalyzes two discrete reactions in the de novo synthesis of purines: the cleavage of adenylosuccinate and succinylaminoimidazole carboxamide ribotide
YP_560396.1	catalyzes the formation of 2-dehydro-3-deoxy-6-phospho-D-gluconate from 6-phospho-D-gluconate
YP_560406.1	Catalyzes the phosphorylation of L-glutamate during the proline biosynthesis pathway
YP_560407.1	required for the assembly and function of the DNAX complex which is required for the assembly of the beta subunit onto primed DNA
YP_560409.1	leucine--tRNA ligase; LeuRS; class-I aminoacyl-tRNA synthetase; charges leucine by linking carboxyl group to alpha-phosphate of ATP and then transfers aminoacyl-adenylate to its tRNA; due to the large number of codons that tRNA(Leu) recognizes, the leucyl-tRNA synthetase does not recognize the anticodon loop of the tRNA, but instead recognition is dependent on a conserved discriminator base A37 and a long arm; an editing domain hydrolyzes misformed products; in Methanothermobacter thermautotrophicus this enzyme associates with prolyl-tRNA synthetase
YP_560412.2	catalyzes the reduction of 2,3-dihydrodipicolinate to 2,3,4,5-tetrahydrodipicolinate in lysine and diaminopimelate biosynthesis
YP_560415.1	catalyzes the formation of glyoxylate from (S)-ureidoglycolate
YP_560416.1	catalyzes the formation of S-ureidoglycolate and urea from allantoate
YP_560417.1	involved in the transport of C4-dicarboxylates across the membrane
YP_560420.1	catalyzes the formation of ribose 5-phosphate and xylulose 5-phosphate from sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate; can transfer ketol groups between several groups; in Escherichia coli there are two tkt genes, tktA expressed during exponential growth and the tktB during stationary phase
YP_560421.1	catalyzes the formation of spermidine from putrescine and S-adenosylmethioninamine
YP_560424.1	in Escherichia coli RsmE methylates the N3 position of the U1498 base in 16S rRNA; cells lacking this function can grow, but are outcompeted by wild-type; SAM-dependent m(3)U1498 methyltransferase
YP_560428.1	NAD-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; does not decarboxylate oxaloacetate
YP_560429.1	catalyzes the formation of thiamine diphosphate from thiamine phosphate ant ATP
YP_560433.1	type 2 subfamily; involved in last step of pyrimidine biosynthesis; converts orotidine 5'-phosphate to UMP and carbon dioxide; OMP decarboxylase; OMPDCase; OMPdecase
YP_560437.1	Part of the ABC transporter complex AraFGH involved in the high affinity transport of arabinose
YP_560438.1	Part of the ABC transporter complex AraFGH involved in the high affinity transport of arabinose
YP_560441.1	catalyzes the formation of D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-galactonate 6-phosphate; functions in galactonate metabolism
YP_560445.1	glycosyltransferase; polymerizes glycan strands in the peptidoglycan
YP_560446.1	AroE; catalyzes the conversion of shikimate to 3-dehydroshikimate
YP_560452.1	catalyzes the formation of 3-dehydroshikimate from 3-dehydroquinate in chorismate biosynthesis
YP_560453.1	composes the biotin carboxyl carrier protein subunit of the acetyl-CoA carboxylase complex, the enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, which in turn controls the rate of fatty acid metabolism
YP_560454.2	an AccC homodimer forms the biotin carboxylase subunit of the acetyl CoA carboxylase, an enzyme that catalyzes the formation of malonyl-CoA, which in turn controls the rate of fatty acid metabolism
YP_560455.1	methylates ribosomal protein L11 at multiple amino acid positions; mutations of these genes in Escherichia coli or Thermus thermophilus has no apparent phenotype
YP_560462.1	Catalyzes the rate-limiting step in dNTP synthesis
YP_560464.1	Catalyzes the rate-limiting step in dNTP synthesis
YP_560470.1	Catalyzes the salvage synthesis of inosine-5'-monophosphate (IMP) and guanosine-5'-monophosphate (GMP) from the purine bases hypoxanthine and guanine, respectively
YP_560472.1	catalyzes the formation of prolyl-tRNA(Pro) from proline and tRNA(Pro)
YP_560475.1	catalyzes the formation of glutamate 5-phosphate from glutamate in proline biosynthesis
YP_560476.1	essential GTPase; exhibits high exchange rate for GTP/GDP; associates with 50S ribosomal subunit; involved in regulation of chromosomal replication
YP_560477.1	involved in the peptidyltransferase reaction during translation
YP_560484.1	catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A; involved in coenzyme A biosynthesis
YP_560489.1	bifunctional arginine biosynthesis protein ArgJ; functions at the 1st and 5th steps in arginine biosynthesis; involved in synthesis of acetylglutamate from glutamate and acetyl-CoA and ornithine by transacetylation between acetylornithine and glutmate
YP_560490.1	functions in protein export; can interact with acidic membrane phospholipids and the SecYEG protein complex; binds to preproteins; binds to ATP and undergoes a conformational change to promote membrane insertion of SecA/bound preprotein; ATP hydrolysis appears to drive release of the preprotein from SecA and deinsertion of SecA from the membrane; additional proteins SecD/F/YajC aid SecA recycling; exists in an equilibrium between monomers and dimers; may possibly form higher order oligomers; proteins in this cluster correspond SecA1; SecA2 is not essential and seems to play a role in secretion of a subset of proteins
YP_560492.1	zinc-dependent; catalyzes the deacetylation of UDP-(3-O-acyl)-N-acetylglucosamine to UDP-3-O-(3-hydroxytetradecanoyl)-glucosamine in the second step of lipid A biosynthesis
YP_560494.1	GTPase; similar structure to tubulin; forms ring-shaped polymers at the site of cell division; other proteins such as FtsA, ZipA, and ZapA, interact with and regulate FtsZ function
YP_560495.1	Citation: Corbin BD, Geissler B, Sadasivam M, Margolin W.J Bacteriol. 2004 Nov;186(22):7736-44.
YP_560496.1	Citation: Azzolina BA, Yuan X, Anderson MS,El- Sherbeini M.Protein Expr Purif. 2001 Apr;21(3):393- 400.Fiskus W, Padmalayam I, Kelly T, Guibao C, BaumstarkBR.DNA Cell Biol. 2003 Nov;22(11):743-52.
YP_560497.1	D-alanine--D-alanine ligase; DdlA; DdlB; cytoplasmic; catalyzes the formation of D-alanyl-D-alanine from two D-alanines in peptidoglycan synthesis; there are two forms of this enzyme in Escherichia coli
YP_560498.1	Catalyzes the formation of UDP-N-acetylmuramoyl-L-alanine from UDP-N-acetylmuramate and L-alanine in peptidoglycan synthesis
YP_560499.1	UDP-N-acetylglucosamine--N-acetylmuramyl- (pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase; involved in cell wall formation; inner membrane-associated; last step of peptidoglycan synthesis
YP_560500.1	Citation: Francis F, Ramirez-Arcos S, Salimnia H, Victor C, Dillon JR.Gene. 2000 Jun 27;251(2):141-51.Mengin- Lecreulx D, Ayala J, Bouhss A, van Heijenoort J,Parquet C, Hara H. J Bacteriol. 1998 Sep;180(17):4406-12.
YP_560501.1	UDP-N-acetylmuramoylalanine--D-glutamate ligase; involved in peptidoglycan biosynthesis; cytoplasmic; catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine during cell wall formation
YP_560502.1	First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan
YP_560503.1	Citation: Francis F, Ramirez-Arcos S, Salimnia H, Victor C, Dillon JR.Gene. 2000 Jun 27;251(2):141-51.
YP_560504.1	involved in cell wall formation; peptidoglycan synthesis; cytoplasmic enzyme; catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-aceylmuramoyl-l-alanyl-d-glutamate
YP_560505.1	Citation: Francis F, Ramirez-Arcos S, Salimnia H, Victor C, Dillon JR.Gene. 2000 Jun 27;251(2):141-51.
YP_560507.1	Citation: Carrion M, Gomez MJ, Merchante-SchubertR, Dongarra S, Ayala JA.Biochimie. 1999Aug-Sep;81(8-9):879- 88.
YP_560508.1	MraZ; UPF0040; crystal structure shows similarity to AbrB
YP_560511.1	activates fatty acids by binding to coenzyme A
YP_560514.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_560515.1	Phenylacetyl-CoA pathway; Citation:  J. Bacteriol. 182 (2), 286-294 (2000).J. Bacteriol. 180 (5), 1063-1071 (1998). Mol. Genet.Genomics 267 (5), 656-663 (2002). Environ Microbiol. 2002Dec;4(12):824-41
YP_560516.1	catalyzes the thiolytic cleavage of beta-ketoadipyl-CoA to succinate and acetyl-CoA
YP_560517.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_560518.1	Phenylacetyl-CoA pathway; Citation: Gene 341, 167-179 (2004). EnvironMicrobiol. 2002 Dec;4(12):824-41
YP_560519.1	Phenylacetyl-CoA pathway; Citation: J. Bacteriol. 180 (5), 1063-1071 (1998).Proc. Natl. Acad. Sci. U.S.A. 95 (11), 6419-6424 (1998).FEBS Lett. 406 (1-2), 23-27 (1997). Environ Microbiol.2002 Dec;4(12):824-41
YP_560521.1	protein associated with Co2+ and Mg2+ efflux
YP_560522.1	catalyzes the interconversion of D-ribulose 5-phosphate to xylulose 5-phosphate
YP_560524.1	with component II, the glutamine amidotransferase, catalyzes the formation of anthranilate from chorismate and glutamine
YP_560525.1	TrpG; with TrpE catalyzes the formation of anthranilate and glutamate from chorismate and glutamine; TrpG provides the glutamine amidotransferase activity
YP_560526.1	Catalyzes the conversion of N-(5-phospho-D-ribosyl)-anthranilate and diphosphate to anthranilate and 5-phospho-alpha-D-ribose 1-diphosphate
YP_560527.1	involved in tryptophan biosynthesis; amino acid biosynthesis; converts 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate to C(1)-(3-indolyl)-glycerol 3-phosphate and carbon dioxide and water
YP_560528.1	Citation: Iyer LM, Aravind L. BMC Genomics. 2002Nov 27;3(1):33. Sismeiro O, Trotot P, Biville F, VivaresC, Danchin A.J Bacteriol. 1998 Jul;180(13):3339-44.
YP_560529.1	Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine
YP_560533.1	Citation: Nakahigashi,K., Miyamoto,K., Nishimura, K.and Inokuchi,H.J. Bacteriol. 174 (22), 7352-7359 (1992)
YP_560535.1	translation-associated GTPase; the crystal structure of the Haemophilus influenzae YchF protein showed similarity to the yeast structure (PDB: 1NI3); fluorescence spectroscopy revealed nucleic acid binding; the yeast protein YBR025c interacts with the translation elongation factor eEF1
YP_560537.1	with UgpACE is involved in the uptake of glycerol-3-phosphate
YP_560539.1	with UgpABC is involved in uptake of glycerol-3-phosphate
YP_560540.1	part of the UgpABCE glycerol-3-phosphate uptake system
YP_560542.1	ChvD; in Agrobacterium tumefaciens, mutations in both Walker boxes were found to affect virulence
YP_560544.1	Citation: Janssen D.B. , Oppentocht J.E. , Poelarends G.J.Curr. Opin. Biotechnol. 12: 254-258 (2001)[PubMed: 11404103]
YP_560548.1	catalyzes the formation of glutamate-1-semialdehyde from glutamyl-tRNA(Glu) and NADPH; the second step of the pathway is catalyzed by glutamate-1-semialdehyde aminomutase which results in the formation of 5-aminolevulinic acid; functions in porphyrin (tetrapyrroles) biosynthesis; the crystal structure showed a C-terminal dimerization domain that appears to be absent in Chlamydial proteins
YP_560549.1	recognizes the termination signals UAG and UAA during protein translation a specificity which is dependent on amino acid residues residing in loops of the L-shaped tRNA-like molecule of RF1; this protein is similar to release factor 2
YP_560552.1	catalyzes the formation of 2-octaprenylphenol from 3-octaprenyl-4-hydroxybenzoate
YP_560553.1	Citation: Christinet,L., Burdet,F.X., Zaiko,M.,Hinz, U. and Zryd,J.P.Plant Physiol. 134 (1), 265-274(2004)
YP_560576.1	TatA; similar to TatE that is found in some proteobacteria; part of system that translocates proteins with a conserved twin arginine motif across the inner membrane; capable of translocating folded substrates typically those with bound cofactors; similar to a protein import system in thylakoid membranes
YP_560579.1	catalyzes the formation of 1-(5-phosphoribosyl)-AMP from 1-(5-phosphoribolsyl)-ATP in histidine biosynthesis
YP_560580.1	PR-AMP cyclohydrolase; functions in histidine biosynthesis from PRPP; converts 1-(5-phosphoribosyl)-AMP to 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino]imidazole-4- carboxyamide during the histidine biosynthesis pathway; binds zinc and magnesium; forms homodimers
YP_560581.1	catalyzes the conversion of 5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]- 1-(5-phosphoribosyl)imidazole-4-carboxamideand glutamine to imidazole-glycerol phosphate, 5-aminoimidazol-4-carboxamideribonucleotide and glutamate; the HisF subunit acts as a cyclase
YP_560582.1	catalyzes the formation of 5-(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino-l- (5-phosphoribosyl)imidazole-4-carboxamide from 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide
YP_560583.1	with HisF IGPS catalyzes the conversion of phosphoribulosyl-formimino-5-aminoimidazole-4-carboxamide ribonucleotide phosphate and glutamine to imidazole-glycerol phosphate, 5-aminoimidazol-4-carboxamide ribonucleotide, and glutamate in histidine biosynthesis; the HisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to HisF for the synthesis of imidazole-glycerol phosphate and 5-aminoimidazol-4-carboxamide ribonucleotide
YP_560585.1	catalyzes the dehydration of D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate to 3-(imidazol-4-yl)-2-oxopropyl phosphate in histidine biosynthesis
YP_560586.1	catalyzes the formation of L-histidinol phosphate from imidazole-acetol phosphate and glutamate in histidine biosynthesis
YP_560587.1	catalyzes the oxidation of L-histidinol to L-histidinaldehyde and then to L-histidine in histidine biosynthesis; functions as a dimer
YP_560588.1	short form of enzyme; requires HisZ for function; catalyzes the formation of N'-5'-phosphoribosyl-ATP from phosphoribosyl pyrophosphate; crucial role in histidine biosynthesis; forms heteromultimer of HisG and HisZ
YP_560589.1	adds enolpyruvyl to UDP-N-acetylglucosamine as a component of cell wall formation; gram-positive bacteria have 2 copies of MurA which are active
YP_560594.1	Citation: Kim K,Lee S, Lee K,Lim DJ Bacteriol. 1998July; 180(14): 3692-3696
YP_560596.1	Citation: Kim K,Lee S, Lee K,Lim DJ Bacteriol. 1998July; 180(14): 3692-3696.
YP_560597.1	Citation: Kim K,Lee S, Lee K,Lim DJ Bacteriol. 1998July; 180(14): 3692-3696.
YP_560598.1	Citation: Kim K,Lee S, Lee K,Lim DJ Bacteriol. 1998July; 180(14): 3692-3696.
YP_560600.1	functions in thiamine (vitamin B1) biosynthesis; in Bacillus subtilis this enzyme catalyzes the formation of thiazole from dehydroxyglycine and 1-deoxy-D-xylulose-5-phosphate and ThiS-thiocarboxylate
YP_560601.1	with ThiF, ThiG, and ThiO catalyzes the formation of the thiazole moiety of thiamine pyrophosphate
YP_560619.1	glutamate synthase is composed of subunits alpha and beta; beta subunit is a flavin adenine dinucleotide-NADPH dependent oxidoreductase; provides electrons to the alpha subunit, which binds L-glutamine and 2-oxoglutarate and forms L-glutamate
YP_560624.1	dGTPase family type 2 subfamily; presumably hydrolyzes dGTP to deoxyguanosine and triphosphate
YP_560625.1	catalyzes the formation of 3-dehydroquinate from 3-deoxy-arabino-heptulonate 7-phosphate; functions in aromatic amino acid biosynthesis
YP_560626.1	catalyzes the formation of shikimate 3-phosphate from shikimate in aromatic amino acid biosynthesis
YP_560630.1	partial resemblance to pilus assembly ATPase PilM
YP_560632.1	defects in the mitochondrial frataxin protein cause Friedreich ataxis which is an autosomal recessive neurodegenerative disease; based on phylogenomic distribution this protein may have a role in iron-sulfur cluster protein assembly
YP_560635.1	in Escherichia coli this inner membrane protein was found to anchor the periplasmic catalytic oxidoreductase YedY; sulfite oxidase activity not demonstrated; contains heme
YP_560636.1	in Escherichia coli this periplasmic enzyme was found to encode the periplasmic catalytic subunit of an oxidoreductase; sulfite oxidase activity not demonstrated; requires inner membrane anchor protein YedZ
YP_560640.1	binds guanine nucleotides; in Escherichia coli depletion results in defective cell division and filamentation; in Bacillus subtilis this gene is essential
YP_560641.1	catalyzes the formation of porphobilinogen from 5-aminolevulinate
YP_560644.1	is a component of the macrolide binding site in the peptidyl transferase center
YP_560645.1	catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Dimerization of the alpha subunit is the first step in the sequential assembly of subunits to form the holoenzyme
YP_560646.1	primary rRNA binding protein; nucleates 30S assembly; involved in translational accuracy with proteins S5 and S12; interacts with protein S5; involved in autogeneously regulating ribosomal proteins by binding to pseudoknot structures in the polycistronic mRNA; interacts with transcription complex and functions similar to protein NusA in antitermination
YP_560647.1	located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA; forms part of the Shine-Dalgarno cleft in the 70S ribosome; interacts with S7 and S18 and IF-3
YP_560648.1	located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA; makes contact with the large subunit via RNA-protein interactions and via protein-protein interactions with L5; contacts P-site tRNA
YP_560649.1	smallest protein in the large subunit; similar to what is found with protein L31 and L33 several bacterial genomes contain paralogs which may be regulated by zinc; the protein from Thermus thermophilus has a zinc-binding motif and contains a bound zinc ion; the proteins in this group have the motif
YP_560650.1	stimulates the activities of the other two initiation factors, IF-2 and IF-3
YP_560651.1	forms heterotrimeric complex in the membrane; in bacteria the complex consists of SecY which forms the channel pore and SecE and SecG; the SecG subunit is not essential; in bacteria translocation is driven via the SecA ATPase
YP_560652.1	late assembly protein
YP_560653.1	L30 binds domain II of the 23S rRNA and the 5S rRNA; similar to eukaryotic protein L7
YP_560654.1	located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body; contacts S4 and S8; with S4 and S12 plays a role in translational accuracy; mutations in this gene result in spectinomycin resistance
YP_560655.1	binds 5S rRNA along with protein L5 and L25
YP_560656.1	ribosomal protein L6 appears to have arisen as a result of an ancient gene duplication as based on structural comparison of the Bacillus stearothermophilus protein; RNA-binding appears to be in the C-terminal domain; mutations in the L6 gene confer resistance to aminoglycoside antibiotics such as gentamicin and these occur in truncations of the C-terminal domain; it has been localized to a region between the base of the L7/L12 stalk and the central protuberance
YP_560657.1	binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit
YP_560658.1	located in the peptidyl transferase center and involved in assembly of 30S ribosome subunit; similar to what is observed with proteins L31 and L33, some proteins in this family contain CXXC motifs that are involved in zinc binding; if two copies are present in a genome, then the duplicated copy appears to have lost the zinc-binding motif and is instead regulated by zinc; the proteins in this group do not appear to have the zinc-binding motif
YP_560659.1	part of 50S and 5S/L5/L18/L25 subcomplex; contacts 5S rRNA and P site tRNA; forms a bridge to the 30S subunit in the ribosome by binding to S13
YP_560660.1	assembly initiator protein; binds to 5' end of 23S rRNA and nucleates assembly of the 50S; surrounds polypeptide exit tunnel
YP_560661.1	binds to the 23S rRNA between the centers for peptidyl transferase and GTPase
YP_560662.1	primary binding protein; helps mediate assembly; involved in translation fidelity
YP_560663.1	one of the stabilizing components for the large ribosomal subunit
YP_560664.1	located in the peptidyl transferase center and may be involved in peptidyl transferase activity; similar to archaeal L10e
YP_560665.1	forms a complex with S10 and S14; binds the lower part of the 30S subunit head and the mRNA in the complete ribosome to position it for translation
YP_560666.1	binds specifically to 23S rRNA during the early stages of 50S assembly; makes contact with all 6 domains of the 23S rRNA in the assembled 50S subunit and ribosome; mutations in this gene result in erythromycin resistance; located near peptidyl-transferase center
YP_560667.1	protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA
YP_560668.1	one of the primary rRNA-binding proteins; required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation
YP_560669.1	binds third domain of 23S rRNA and protein L29; part of exit tunnel
YP_560670.1	L4 is important during the early stages of 50S assembly; it initially binds near the 5' end of the 23S rRNA
YP_560671.1	binds directly near the 3' end of the 23S rRNA, where it nucleates assembly of the 50S subunit; essential for peptidyltransferase activity; mutations in this gene confer resistance to tiamulin
YP_560672.1	NusE; involved in assembly of the 30S subunit; in the ribosome, this protein is involved in the binding of tRNA; in Escherichia coli this protein was also found to be involved in transcription antitermination; NusB/S10 heterodimers bind boxA sequences in the leader RNA of rrn operons which is required for antitermination; binding of NusB/S10 to boxA nucleates assembly of the antitermination complex
YP_560673.1	EF-Tu; promotes GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis; when the tRNA anticodon matches the mRNA codon, GTP hydrolysis results; the inactive EF-Tu-GDP leaves the ribosome and release of GDP is promoted by elongation factor Ts; many prokaryotes have two copies of the gene encoding EF-Tu
YP_560674.1	EF-G; promotes GTP-dependent translocation of the ribosome during translation; many organisms have multiple copies of this gene
YP_560675.1	binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit
YP_560676.1	interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone; located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side; mutations in the S12 gene confer streptomycin resistance
YP_560678.1	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Subunit beta' binds to sigma factor allowing it to bind to the -10 region of the promoter
YP_560679.1	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates; beta subunit is part of the catalytic core which binds with a sigma factor to produce the holoenzyme
YP_560680.1	present in two forms; L12 is normal, while L7 is aminoacylated at the N-terminal serine; the only multicopy ribosomal protein; 4:1 ratio of L7/L12 per ribosome; two L12 dimers bind L10; critically important for translation efficiency and fidelity; stimulates GTPase activity of translation factors
YP_560681.1	binds the two ribosomal protein L7/L12 dimers and anchors them to the large ribosomal subunit
YP_560682.1	in Escherichia coli and Methanococcus, this protein autoregulates expression; the binding site in the mRNA mimics the binding site in the 23S rRNA
YP_560683.1	binds directly to 23S ribosomal RNA
YP_560684.1	Modulates Rho-dependent transcription termination
YP_560685.1	forms a complex with SecY and SecG; SecYEG forms a protein-conducting channel to which secA binds and translocates targeted polypeptides across the cytoplasmic membrane, a process driven by ATP and a proton-motive force
YP_560686.1	EF-Tu; promotes GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis; when the tRNA anticodon matches the mRNA codon, GTP hydrolysis results; the inactive EF-Tu-GDP leaves the ribosome and release of GDP is promoted by elongation factor Ts; many prokaryotes have two copies of the gene encoding EF-Tu
YP_560690.1	with PaaBCDE catalyzes the hydroxylation of phenylacetyl-CoA
YP_560691.1	with PaaBCDE catalyzes the hydroxylation of phenylacetyl-CoA; involved in phenylacetate degradation
YP_560692.1	Phenylacetyl-CoA pathway; Citation: J. Bacteriol. 182 (2), 286-294 (2000).Mol. Genet. Genomics 267 (5), 656-663 (2002). J.Bacteriol. 180 (5), 1063-1071 (1998). Environ Microbiol.2002 Dec;4(12):824-41
YP_560693.1	Phenylacetyl-CoA pathway; Citation: J. Bacteriol. 182 (2), 286-294 (2000). J.Bacteriol. 180 (5), 1063-1071 (1998). FEBS Lett. 406(1- 2), 23-27 (1997). Environ Microbiol. 2002Dec;4(12):824-41
YP_560694.1	Phenylacetyl-CoA pathway; Citation: J. Bacteriol. 182 (2), 286-294 (2000). J.Bacteriol. 180 (5), 1063-1071 (1998). Proc. Natl. Acad.Sci. U.S.A. 95 (11), 6419-6424 (1998). Environ Microbiol.2002 Dec;4(12):824-41
YP_560696.1	Citation: J. Bacteriol. 187 (4), 1493-1503 (2005).Environ Microbiol. 2002 Dec;4(12):824-41.; Phenylacetyl-CoA pathway
YP_560699.1	Tyrosine degradation; Citation: Structure Fold. Des. 7 (8), 977-988(1999)
YP_560700.1	Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates
YP_560702.1	NADP-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; decarboxylates oxaloacetate
YP_560704.1	involved in fifth step of pyrimidine biosynthesis; converts orotidine 5'-phosphate and diphosphate to orotate and 5-phospho-alpha-D-ribose 1-diphosphate
YP_560708.1	catalyzes the reduction of N-acetyl-5-glutamyl phosphate to N-acetyl-L-glutamate 5-semialdehyde in arginine biosynthesis
YP_560775.1	Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source
YP_560777.1	TtcA; YdaO; catalyzes the thiolation of cytosine 32 in specific tRNAs
YP_560782.2	catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template; phosphohydrolase activities include hydrolysis of pyrophosphate, 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi, metal-dependent phosphodiesterase activity for 2',3'-cAMP, 2',3'-cGMP, and 2',3'-cCMP, and hydrolysis 2',3'-cyclic substrates with the formation of 2'-nucleotides and 3'-nucleotides; these phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases
YP_560797.1	Part of the ABC transporter complex DppABCDF involved in the transport of dipeptides
YP_560805.1	catalyzes the formation of L-homocysteine from S-adenosyl-L-homocysteine
YP_560817.1	the MS-ring anchors the flagellum to the cytoplasmic membrane; part of the flagellar basal body which consists of four rings L, P, S, and M mounted on a central rod
YP_560818.1	One of three proteins involved in switching the direction of the flagellar rotation
YP_560819.1	binds to and inhibits the function of flagella specific ATPase FliI
YP_560824.1	interacts with cytoplasmic MS ring of the basal body and may act to stabilize the MotAB complexes which surround the MS ring
YP_560825.1	with FliG and FliN makes up the switch complex which is involved in switching the direction of the flagella rotation
YP_560828.1	FliP, with proteins FliQ and FliR, forms the core of the central channel in the flagella export apparatus
YP_560829.1	with proteins FliP and FliR forms the core of the central channel in the flagella export apparatus
YP_560832.1	with FlgK acts as a hook filament junction protein to join the flagellar filament to the hook; Yersinia, Vibrio parahaemolyticus, Bradyrhizobium and other organisms have 2 copies of this and other flagellar genes.
YP_560833.1	with FlgL acts as a hook filament junction protein to join the flagellar filament to the hook
YP_560835.1	Flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space
YP_560836.1	part of the basal body which consists of four rings L, P, S, and M mounted on a central rod; Vibrio parahaemolyticus, Yersinia, Bradyrhizobium and other bacteria have two copies of this and other flagellar genes; the V. parahaemolyticus protein is associated with the polar flagella and the Bradyrhizobium protein is associated with the thick flagellum
YP_560837.1	part of the basal body which consists of four rings L, P, S, and M mounted on a central rod; Burkholderia thailandensis has 2 copies of this and other flagella genes
YP_560838.1	makes up the distal portion of the flagellar basal body rod
YP_560839.1	FlgF, with FlgB and C, makes up the proximal portion of the flagellar basal body rod
YP_560841.1	acts as a scaffold for the assembly of hook proteins onto the flagellar basal body rod; Yersinia, Vibrio parahaemolyticus, Bradyrhizobium and other organisms have 2 copies of some flagellar genes; in V. parahaemolyticus one set used for lateral flagella production and the other is used for the polar flagella production
YP_560842.1	with FlgF and B makes up the proximal portion of the flagellar basal body rod
YP_560843.1	with FlgF and C makes up the proximal portion of the flagellar basal body rod
YP_560849.1	sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released; this sigma factor directs late flagellar biosynthesis genes
YP_560851.1	positive regulator of class III flagellar genes
YP_560852.1	membrane protein involved in the flagellar export apparatus
YP_560853.1	membrane protein responsible for substrate specificity switching from rod/hook-type export to filament-type export
YP_560857.1	cytosolic phosphatase which functions in the chemotaxis signal transduction complex by controlling the level of phosphorylated CheY through dephosphorylation
YP_560859.1	regulates chemotaxis by demethylation of methyl-accepting chemotaxis proteins
YP_560860.1	catalyzes the conversion of glutamine residues to glutamate on methyl-accepting chemotaxis receptors
YP_560866.1	with MotA forms the ion channels that couple flagellar rotation to proton/sodium motive force across the membrane and forms the stator elements of the rotary flagellar machine
YP_560867.1	With MotB forms the ion channels that couple flagellar rotation to proton/sodium motive force across the membrane and forms the stator elements of the rotary flagellar machine
YP_560868.1	With FlhD is involved in the activation of class 2 flagellar genes and as well as a number of other genetic systems
YP_560869.1	with FlhC is involved in the activation of class 2 flagellar genes and is involved in the regulation of a number of other genetic systems
YP_560872.1	porin involved in osmoregulation allowing water to move into and out of the cell in response to osmotic pressure
YP_560878.1	a small basic protein that is one of the last in the subunit assembly; omission does not prevent assembly but the subunit is inactive; binds central domain of 16S rRNA
YP_560880.1	structural flagella protein; Vibrio contains multiple flagellin genes usually localized into two region on the chromosome, flaAC and flaCEDB in V. cholerae, flaFBA and flaCDE in V. parahemolyticus; FlaA is sigma 54 dependent and essential for motility in V.cholerae but not in V. parahaemolyticus
YP_560923.1	catalyzes the transfer of a methylene carbon from the methylamine-loaded GcvH protein to tetrahydrofolate, causing the release of ammonia and the generation of reduced GcvH protein
YP_560924.1	part of multienzyme complex composed of H, L, P, and T proteins which catalyzes oxidation of glycine to yield carbon dioxide, ammonia, 5,10-CH2-H4folate and a reduced pyridine nucleotide; protein H is involved in transfer of methylamine group from the P to T protein; covalently bound to a lipoyl cofactor
YP_560925.1	acts in conjunction with GvcH to form H-protein-S-aminomethyldihydrolipoyllysine from glycine
YP_560928.1	catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; also known as acetolactate synthase large subunit
YP_560930.1	proline utilization protein A; multifunctional protein that functions in proline catabolism in the first two enzymatic steps resulting in the conversion of proline to glutamate; in Escherichai coli this protein also self-regulates transcription via a DNA-binding domain at the N-terminus; forms dimers and is a peripherally membrane-associated protein
YP_560934.1	binding of PriA to forked DNA starts the assembly of the primosome, also possesses 3'-5' helicase activity
YP_560935.1	catalyzes the formation of coproporphyrinogen from uroporphyrinogen III
YP_560937.1	activates fatty acids by binding to coenzyme A
YP_560938.1	part of catalytic core of ATP synthase; alpha(3)beta(3)gamma(1)delta(1)epsilon(1); involved in producing ATP from ADP in the presence of the proton motive force across the membrane
YP_560939.1	Produces ATP from ADP in the presence of a proton gradient across the membrane. The beta chain is a regulatory subunit
YP_560940.1	Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is a regulatory subunit
YP_560941.1	produces ATP from ADP in the presence of a proton gradient across the membrane; the alpha chain is a catalytic subunit
YP_560942.1	Produces ATP from ADP in the presence of a proton gradient across the membrane; the delta subunit is part of the catalytic core of the ATP synthase complex
YP_560943.1	Produces ATP from ADP in the presence of a proton gradient across the membrane. Subunit B is part of the membrane proton channel.
YP_560944.1	Produces ATP from ADP in the presence of a proton gradient across the membrane. Subunit C is part of the membrane proton channel F0
YP_560945.1	Produces ATP from ADP in the presence of a proton gradient across the membrane. Subunit A is part of the membrane proton channel F0
YP_560950.1	glucose-inhibited division protein B; SAM-dependent methyltransferase; methylates the N7 position of guanosine in position 527 of 16S rRNA
YP_560951.1	GidA; glucose-inhibited cell division protein A; involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U) of the wobble uridine base in some tRNAs
YP_560968.1	phenylalanine 4-hydroxylase; phenylalanine 4-hydroxylase; catalyzes the formation of 4a-hydroxytetrahydrobiopterin and tyrosine from phenylalanine and tetrahydrobiopterin
YP_560969.1	4-alpha-hydroxytetrahydrobiopterin dehydratase activity; catalyzes the formation of (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7, 8-dihydro-6H-pterin from (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7, 8-tetrahydro-4a-hydroxypterin; functions in recycling tetrahydrobiopterin (BH4) in phenylalanine hydroxylase reaction
YP_560975.1	Catalyzes the transfer of the ammonia group from glutamine to a new carbon-nitrogen group
YP_560977.1	ATP-dependent; carboxylate-amine ligase with weak glutamate--cysteine ligase activity
YP_560979.1	catalyzes the formation of 5-methylaminomethyl-2-thiouridine in position 34 of the anticodon of tRNA molecules
YP_561000.1	involved in the first step of glutathione biosynthesis
YP_561004.1	catalyzes the formation of 3-methyl-2-oxobutanoate from 2,3,-dihydroxy-3-methylbutanoate
YP_561011.1	E1 component; part of pyruvate dehydrogenase; forms a complex with DlaT and LpdC
YP_561014.1	in Escherichia coli this protein is involved in the biosynthesis of the hypermodified nucleoside 5-methylaminomethyl-2-thiouridine, which is found in the wobble position of some tRNAs and affects ribosomal frameshifting; shows potassium-dependent dimerization and GTP hydrolysis; also involved in regulation of glutamate-dependent acid resistance and activation of gadE
YP_561017.1	functions to insert inner membrane proteins into the IM in Escherichia coli; interacts with transmembrane segments; functions in both Sec-dependent and -independent membrane insertion; similar to Oxa1p in mitochondria
YP_561020.1	in Escherichia coli transcription of this gene is enhanced by polyamines
YP_552326.1	catalyzes the formation of 2-amino-3-oxobutanoate from acetyl-CoA and glycine
YP_552327.1	converts threonine and NAD to 1,2-amino-3-oxobutanoate and NADH; functions in threonine catabolism
YP_552350.1	catalyzes the formation of propanoyl-CoA from methylmalonyl-CoA
YP_552377.1	stimulates the release of release factors 1 and 2 from the ribosome after hydrolysis of the ester bond in peptidyl-tRNA has occurred; GDP/GTP-binding protein
YP_552424.1	Putative type II/IV secretion system-relatedprotein
YP_552433.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_552434.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_552435.1	lipoprotein signal peptidase; integral membrane protein that removes signal peptides from prolipoproteins during lipoprotein biosynthesis
YP_552436.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_552442.1	catalyzes the conversion of citrate to isocitrate
YP_552443.1	functions in propionate metabolism; involved in isomerization of (2S,3S)-methylcitrate to (2R,3S)-methylisocitrate; also encodes minor aconitase or dehydratase activity; aconitase C
YP_552445.1	catalyzes the synthesis of 2-methylcitrate from propionyl-CoA and oxaloacetate; also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity
YP_552447.1	catalyzes the oxidation of malate to oxaloacetate
YP_552452.1	part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol
YP_552453.1	part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase
YP_552455.1	type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH
YP_552456.1	dehydratase component, catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate
YP_552457.1	catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate in leucine biosynthesis; forms a heterodimer of LeuC/D
YP_552458.1	catalyzes the oxidation of 3-isopropylmalate to 3-carboxy-4-methyl-2-oxopentanoate in leucine biosynthesis
YP_552460.1	catalyzes the formation of 4-aspartyl phosphate from aspartate 4-semialdehyde
YP_552462.1	mediates pseudouridylation (positions 38, 39, 40) at the tRNA anticodon region which contributes to the structural stability
YP_552463.1	catalyzes the formation of 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate from N-(5-phospho-beta-D-ribosyl)-anthranilate in tryptophan biosynthesis
YP_552464.1	catalyzes the formation of L-tryptophan from L-serine and 1-(indol-3-yl)glycerol 3-phosphate
YP_552466.2	catalyzes the formation of indole and glyceraldehyde 3-phosphate from indoleglycerol phosphate in tryptophan biosynthesis
YP_552467.1	catalyzes the carboxylation of acetyl-CoA to malonyl-CoA; forms a tetramer of AccA2D2 subunits
YP_552471.1	Catalyzes first step of the de novo purine nucleotide biosynthetic pathway
YP_552472.1	catalyzes the conversion of O-succinylhomoserine into homocysteine
YP_552482.1	catalyzes the transfer of a segment of a 1,4-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain
YP_552505.1	catalyzes the formation of O-phospho-L-homoserine from L-homoserine
YP_552507.1	Catalyzes the hydrolysis of AMP to form adenine and ribose 5-phosphate using water as the nucleophile
YP_552511.1	has 3'-5' exonuclease, 5'-3' exonuclease and 5'-3'polymerase activities, primarily functions to fill gaps during DNA replication and repair
YP_552516.1	catalyzes the bidirectional exonucleolytic cleavage of DNA
YP_552518.1	catalyzes the formation of 1-deoxy-D-xylulose 5-phosphate from pyruvate and D-glyceraldehyde 3-phosphate
YP_552519.1	similar protein in Methanocaldococcus converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate as the first step in methanopterin biosynthesis
YP_552520.1	in most organisms, only the N-terminal domain is present in a single polypeptide; in some archaea this domain is fused to a kinase domain; this gene is essential for growth in Escherichia coli and Bacillus subtilis; the secreted glycoprotease from Pasteurella haemolytica showed specificity for O-sialoglycosylated proteins; the Pyrococcus structure shows DNA-binding properties, iron-binding, ATP-binding, and AP endonuclease activity
YP_552522.1	a small basic protein that is one of the last in the subunit assembly; omission does not prevent assembly but the subunit is inactive; binds central domain of 16S rRNA
YP_552524.1	synthesizes RNA primers at the replication forks
YP_552525.1	sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released; this is the primary sigma factor of bacteria
YP_552563.1	activates fatty acids by binding to coenzyme A
YP_552569.1	Protocatechuate pathway; Citation: Biochem. Biophys. Res. Commun. 295 (4), 903-909 (2002)
YP_552570.1	Protocatechuate pathway; Citation: Biochem. Biophys. Res. Commun. 295 (4), 903-909 (2002)
YP_552572.1	Tyrosine degradation; Citation: J. Bacteriol. 186 (15), 5062-5077 (2004)
YP_552585.1	catalyzes the formation of oxalyl-CoA from oxalate and Formyl-CoA
YP_552586.1	catalyzes the formation of formyl-CoA from oxalyl-CoA
YP_552593.1	Citation: FEMS Microbiol. Lett. 220 (2), 255- 260(2003); Terephthalate degradation
YP_552594.1	Terephthalate degradation; Citation: Environ. Health Perspect. 103, 9-12(1995)
YP_552595.1	Terephthalate degradation; Citation: Environ. Health Perspect. 103, 9-12(1995)
YP_552607.1	activates fatty acids by binding to coenzyme A
YP_552610.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_552620.1	catalyzes the conversion of ferulic acid to feruloyl-CoA
YP_552634.1	Endoribonuclease L-PSP domain present
YP_552682.1	catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis
YP_552683.1	DNA-binding domain present
YP_552692.1	catalyzes the formation of S-ureidoglycolate and urea from allantoate
YP_552721.1	catalyzes the interconversion of D-xylose to D-xylulose
YP_552723.1	with XylFH is part of the high affinity xylose ABC transporter
YP_552725.1	Tetratricopeptide repeat present
YP_552734.1	Weak similarity to circadian clock proteins ofCyanobacteria
YP_552773.1	PRC-barrel domain present
YP_552784.1	in some organisms the DhaK and DhaL subunits are encoded by separate genes; in others they are fused; functions along with DhaM to phosphorylate dihydroxyacetone
YP_552787.1	catalyzes the selenophosphate-dependent transfer of selenium from selenophosphate for conversion of 2-thiouridine to 2-selenouridine at the wobble position in tRNA
YP_552788.1	catalyzes the formation of selenophosphate from selenide and ATP
YP_552794.1	catalyzes the formation of selenocysteinyl-tRNA(Sec) from seryl-tRNA(Sec) and L-selenophosphate in selenoprotein biosynthesis
YP_552813.1	Homogentisate pathway; Citation: Environ Microbiol. 2002 Dec;4(12):824- 41.J. Bacteriol. 186 (15), 5062-5077 (2004)
YP_552819.1	dehydratase component, catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate
YP_552839.1	catalyzes the oxidation of tricarballylate to cis-aconitate; FAD-dependent; required for the utilization of tricarballylate as a carbon and energy source by S. enterica
YP_552862.1	catalyzes the dephosphorylation of 2-phosphoglycolate to form glycolate and phosphate
YP_552873.1	Required in the synthesis of PPQ, but its exact function is unknown
YP_552874.1	possibly involved in transport of pyrroloquinoline quinone transport
YP_552878.1	catalyzes the transfer of a formyl group from formylmethanofuran to tetrahydromethanopterin tetrahydromethanopterin
YP_552881.1	Required for methylotrophy
YP_552888.1	type III RuBisCO; involved in carbon fixation
YP_552891.1	catalyzes the formation of D-fructose 6-phosphate from fructose-1,6-bisphosphate
YP_552894.1	class II aldolase; catalyzes the reversible aldol condensation of dihydroxyacetonephosphate and glyceraldehyde 3-phosphate in the Calvin cycle, glycolysis and gluconeogenesis
YP_552906.1	Required for methylotrophy
YP_552908.1	catalyzes the reversible formation of methenyl-H(4)methanopterin from N(5)-formyl-H(4)methanopterin
YP_552909.1	Required for methylotrophy
YP_552910.1	Function confirmed by biochemical assay & mutantanalysis; Citation: J Bacteriol, 186:2173-2178
YP_552965.1	catalyzes the formation of acetate from pyruvate
YP_552969.1	Citation: J. Bacteriol. 180 (24), 6529-6537 (1998)
YP_552970.1	Citation: J. Bacteriol. 180 (24), 6529-6537 (1998)
YP_553005.1	flavohemoprotein; catalyzes the formation of nitrate from nitric oxide; can also catalyze the reduction of dihydropteridine
YP_553006.1	Required for the expression of anaerobic nitric oxide (NO) reductase; acts as a transcriptional activator for the norVW operon
YP_553008.1	activator of 3-phenylpropionic acid catabolism
YP_553009.1	catalyzes the formation of 3-(2,3-dihydroxyphenyl)propionate from 3-(3-hydroxyphenyl)propionate
YP_553010.1	catalyzes the cleavage of 3-(2,3-dihydroxyphenyl) propionate into 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate; part of the 3-phenylpropionic acid degradation pathway; member of the protocatechuate 4,5-dioxygenase family
YP_553011.1	3-hydroxyphenyl propionate pathway; Citation: Microbiology 145 (Pt 10), 2813-2820(1999)
YP_553012.1	catalyzes the formation of acetyl-CoA from acetalaldehyde
YP_553013.1	catalyzes the formation of pyruvate and acetaldehyde from 4-hydroxy-2-ketovaleric acid; involved in the degradation of phenylpropionate
YP_553014.1	Citation: J. Bacteriol. 170, 2573-2581 (1997); 3-hydroxyphenyl propionate pathway
YP_553015.1	3-hydroxyphenyl propionate pathway; Citation: J. Bacteriol. 179 (8), 2573-2581 (1997).J. Bacteriol. 178 (17), 5249-5256 (1996)
YP_553035.1	catalyzes the synthesis of 2-methylcitrate from propionyl-CoA and oxaloacetate; also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity
YP_553036.1	Catalyzes the conversion of citrate to isocitrate
YP_553069.1	catalyzes the formation of oxalyl-CoA from oxalate and Formyl-CoA
YP_553082.1	catalyzes the oxidation of UDP-N-acetyl-D-mannosamine to UDP-N-acetylmannosaminuronic acid
YP_553126.1	catalyzes the formation of D-ribulose 5-phosphate from 6-phospho-D-gluconate
YP_553169.1	catalyzes the thiolytic cleavage of beta-ketoadipyl-CoA to succinate and acetyl-CoA
YP_553176.1	component of the membrane-bound D-lactate oxidase, FAD-binding, NADH independent
YP_553217.1	with MdtO and MdtP is involved in resistance to puromycin, acriflavine and tetraphenylarsonium chloride
YP_553228.1	catalyzes the conversion of carbamoyl phosphate and aspartate to form N-carbamoyl aspartate
YP_553250.1	upregulated by FixLJ/FixK under oxygen limitation; involved in regulation of genes involved in carbon and amino acid metabolism
YP_553289.1	catalyzes the formation of glutamate and formamide from N-formimidoyl-L-glutamate
YP_553293.1	catalyzes the hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
YP_553294.1	binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP)
YP_553301.1	Homoprotocatechuate pathway; Citation: Gene 166 (1), 73-76 (1995)
YP_553302.1	Homoprotocatechuate pathway
YP_553303.1	Homoprotocatechuate pathway; Citation: J. Bacteriol. 178 (1), 111-120 (1996)
YP_553304.1	Homoprotocatechuate pathway; Citation: J. Bacteriol. 174 (9), 2903-2912 (1992).FEBS Lett. 275 (1-2), 53-57 (1990)
YP_553305.1	Homoprotocatechuate pathway
YP_553306.1	Homoprotocatechuate pathway; Citation: Biochemistry 41 (9), 2982-2989 (2002)
YP_553307.1	Homoprotocatechuate pathway; Citation: Biochemistry 41 (9), 2982-2989 (2002)
YP_553308.1	Homoprotocatechuate pathway; Citation: Mol. Gen. Genet. 237 (1-2), 241-250(1993)
YP_553346.1	catalyzes the formation of nicotinamide adenine dinucleotide (NAD) from nicotinic acid adenine dinucleotide (NAAD) using either ammonia or glutamine as the amide donor and ATP; ammonia-utilizing enzymes include the ones from Bacillus and Escherichia coli while glutamine-utilizing enzymes include the Mycobacterial one; forms homodimers
YP_553442.1	catalyzes the formation of phosphonoacetaldehyde from 2-aminoethylphosphonate and pyruvate
YP_553469.1	Catalyzes the transfer of 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A to the apo-acyl carrier protein of malonate dehydrogenase to form holo-acyl carrier protein
YP_553471.1	The beta subunit catalyzes the decarboxylation of the malonyl moiety on coenzyme A
YP_553472.1	acyl carrier protein of malonate decarboxylase
YP_553473.1	catalyzes the reversible formation of 2'-(5''-triphosphoribosyl)-3'dephospho-CoA from 3-dephospho-CoA
YP_553516.1	catalyzes the formation of 2,5-dioxopentanoate from 5-dehydro-4-deoxy-D-glucarate
YP_553533.1	catalyzes the hydrolysis of D-alanyl-D-alanine dipeptide: Zn dependent; involved in peptidoglycan synthesis
YP_553554.1	catalyzes the formation of D-glucono-1,5-lactone 6-phosphate from D-glucose 6-phosphate
YP_553610.1	Citation: Eur. J. Biochem. 240 (2), 314-322 (1996)
YP_553661.1	catalyzes the formation of adenosylcob(III)yrinic acid a,c-diamide from cob(I)yrinic acid a,c-diamide
YP_553666.1	catalyzes 2 sequential methylations, the formation of precorrin-1 and S-adenosyl-L-homocysteine from S-adenosyl-L-methionine and uroporphyrin III, and the formation of precorrin-2 and S-adenosyl-L-homocysteine from S-adenosyl-L-methionine and precorrin-1
YP_553668.1	putative cobalamin biosynthesis-related protein
YP_553669.1	with CobST catalyzes the formation of cobyrinic acid a,c-diamide from hydrogenobyrinic acid a,c-diamide in an ATP-dependent manner; involved in porphyrin and chlorophyll metabolism; vitamin B12 metabolism
YP_553680.1	cytochrome o ubiquinol oxidase subunit III
YP_553681.1	putative cytochrome o ubiquinol oxidase
YP_553707.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_553708.1	lipoprotein signal peptidase; integral membrane protein that removes signal peptides from prolipoproteins during lipoprotein biosynthesis
YP_553709.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_553710.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_553715.1	putative sarcosine oxidase delta subunit
YP_553722.1	catalyzes the oxidation of choline to betaine aldehyde and betain aldehyde to glycine betaine
YP_553723.1	catalyzes the formation of betaine from betaine aldehyde
YP_553724.1	HTH-type; bet1; Repressor involved in choline regulation of the bet genes
YP_553725.1	Function confirmed by biochemical assay & mutantanalysis; Citation: J Bacteriol, 186:2173-2178
YP_553729.1	catalyzes the reaction of glycine with 5,10-methylenetetrahydrofolate to form L-serine and tetrahydrofolate
YP_553739.1	produces formate from formyl-tetrahydrofolate which is the major source of formate for PurT in de novo purine nucleotide biosynthesis; has a role in one-carbon metabolism; forms a homohexamer; activated by methionine and inhibited by glycine
YP_553745.1	60 kDa chaperonin; 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is not essential for growth
YP_553746.1	10 kDa chaperonin; 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring
YP_553781.1	catalyzes the conversion of citrate to isocitrate and the conversion of 2-methylaconitate to 2-methylisocitrate
YP_553790.1	catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis
YP_553796.1	catalyzes the interconversion of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate
YP_553842.1	Citation: FEMS Microbiol. Lett. 181 (1), 165- 170(1999)
YP_553843.1	functions with NifE to assemble FeMo cofactor; functions in assembly of nitrogenase MoFe
YP_553844.1	functions with NifN to assemble FeMo cofactor; functions in assembly of nitrogenase MoFe
YP_553847.1	Citation: Braz. J. Med. Biol. Res. 29 (12),1599- 1602 (1996)
YP_553848.1	Citation: Braz. J. Med. Biol. Res. 29 (12),1599- 1602 (1996)
YP_553849.1	nitrogenase iron protein; nitrogenase component 2; with component 1, an molybdenum-iron protein, catalyzes the fixation of nitrogen to ammonia; nitrogen reductase provides electrons to the nitrogenase complex; in R. etli there are three essentially identical copies of nifH which are actively expressed during symbiosis
YP_553872.1	essential respiratory protein A; may be involved in the transfer of iron-sulfur clusters; essential for growth using oxygen or alternate electron acceptors
YP_553877.1	associates with NifD and may protect the nitrogenase Fe-Mo protein from oxidative damage
YP_553892.1	catalyzes the formation of L-proline from pyrroline-5-carboxylate
YP_553947.1	catalyzes the hydrolysis of allophanate
YP_553965.1	catalyzes the oxidative deamination of D-amino acids
YP_553971.1	similar to full-length Gnd, these proteins seems to have a truncated C-terminal 6PGD domainin; in Methylobacillus flagellatus this gene is essential for NAD+-dependent oxidation of 6-phosphogluconate
YP_553997.1	catalyzes the ATP-dependent formation of a phosphodiester at the site of a single strand break in duplex DNA
YP_554030.1	catalyzes the formation of alpha-1,4-glucan chains from ADP-glucose
YP_554056.1	catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine to form methionine
YP_554058.1	CobK/CbiJ; there are 2 pathways for cobalamin (vitamin B12) production, one aerobic (ex. P. denitrificans), the other anaerobic (ex. S. typhimurium); the CobK/CbiJ perform similar reactions in both; the anaerobic pathway includes the use of a chelated cobalt ion in order for ring contraction to occur; CobK thus converts precorrin 6 into dihydro-precorrin 6 while CbiJ converts cobalt-precorrin 6 into cobalt-deihydro-precorrin 6
YP_554059.1	Catalyzes the methylation of C-1 in cobalt-precorrin-5 and the subsequent extrusion of acetic acid from the resulting intermediate to form cobalt-precorrin-6A
YP_554062.1	catalyzes the interconversion of precorrin-8X and hydrogenobyrinate
YP_554063.1	catalyzes the formation of precorrin-3 from precorrin-2
YP_554082.1	ketopantoate reductase; catalyzes the NADPH reduction of ketopantoate to pantoate; functions in pantothenate (vitamin B5) biosynthesis
YP_554084.1	catalyzes the formation of L-glutamate and an aromatic oxo acid from an aromatic amino acid and 2-oxoglutarate
YP_554091.1	Catalase HPII; monofunctional catalase that decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide
YP_554094.1	catalyzes conversion of 1-aminocyclopropane-1-carboxylate to ammonia and alpha-ketobutyrate
YP_554100.1	alkyl hydroperoxide reductase subunit
YP_554134.1	sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released; sigma 54 factor is responsible for the expression of enzymes involved in nitrogen assimilation and metabolism; the rhizobia often have 2 copies of this sigma factor; in Rhizobium etli RpoN1 shown to be involved in the assimilation of several nitrogen and carbon sources during free-living aerobic growth and RpoN2 is involved in symbiotic nitrogen fixation; in Bradyrhizobium both RpoN1 and N2 are functional in free-living and symbiotic conditions, rpoN1 gene was regulated in response to oxygen
YP_554154.1	c-di-GMP phosphodiesterase; probably degrades signalling molecule c-di-GMP
YP_554155.1	regulator of pathogenicity factor RpfF; involved in synthesis of a diffusible signal factor involved in the regulation of extracellular enzymes
YP_554171.1	type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH
YP_554178.1	catalyzes the formation of glutamate from glutamine
YP_554194.1	Citation: J. Bacteriol. 185 (19), 5871-5881 (2003)
YP_554195.1	Citation: J. Bacteriol. 183 (2), 700-708 (2001)
YP_554196.1	Citation: J. Bacteriol. 185 (19), 5871-5881 (2003)
YP_554197.1	Citation: J. Bacteriol. 185 (19), 5871-5881 (2003)
YP_554202.1	Acylates the intermediate (KDO)2-lipid IVA to form (KDO)2-(lauroyl)-lipid IVA
YP_554217.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_554238.1	stimulates the activities of the other two initiation factors, IF-2 and IF-3
YP_554246.1	catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia
YP_554253.1	Catalyzes the reversible hydrolysis of the amide bond within dihydroorotate. This metabolic intermediate is required for the biosynthesis of pyrimidine nucleotides
YP_554293.1	catalyzes the formation of indole-3-acetic acid from indole-3-acetamide
YP_554342.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_554347.1	catalyzes the formation of 3-deoxy-D-arabino-hept-2-ulosonate 7 phosphate from phosphoenolpyruvate and D-erythrose 4-phosphate, tyrosine sensitive
YP_554348.1	HupA
YP_554358.1	catalyzes the formation of putrescine from agmatine
YP_554375.1	Has polymerase, DNA-binding and 3'-5' exonuclease activities. In Aeropyrum pernix this protein is sensitive to aphidicolin and stable at 95#C
YP_554389.1	Citation: Annu Rev Microbiol. 1996;50:553-90
YP_554390.1	Citation: Annu Rev Microbiol. 1996;50:553-90
YP_554391.1	Citation: Annu Rev Microbiol. 1996;50:553-90
YP_554392.1	catalyzes the degradation of 2-hydro-1,2-dihydroxy benzoate to catechol
YP_554420.1	AroE; catalyzes the conversion of shikimate to 3-dehydroshikimate
YP_554421.1	catalyzes the formation of 3-dehydroshikimate from 3-dehydroquinate in chorismate biosynthesis
YP_554446.1	with FlhC is involved in the activation of class 2 flagellar genes and is involved in the regulation of a number of other genetic systems
YP_554447.1	with FlhD is involved in the activation of class 2 flagellar genes and as well as a number of other genetic systems
YP_554478.1	converts (S)-3-hydroxybutanoyl-CoA to 3-acetoacetyl-CoA
YP_554542.1	DNA-binding protein BpH2
YP_554608.1	Citation: Biochem J. 2003 Jan 15;369(Pt 2):275-85
YP_554609.1	Citation: Biochem J. 2003 Jan 15;369(Pt 2):275-85
YP_554610.1	Citation: Biochem J. 2003 Jan 15;369(Pt 2):275-85
YP_554611.1	Citation: Biochem J. 2003 Jan 15;369(Pt 2):275-85
YP_554612.1	catalyzes the formation of acetyl phosphate and sulfite from 2-sulfoacetaldehyde; is active when grown on taurine as a sole carbon source
YP_554613.1	Citation: Biochem J. 2003 Jan 15;369(Pt 2):275-85
YP_554614.1	Putative sulfate efflux channel; Citation: Biochem J. 2003 Jan 15;369(Pt 2):275-85
YP_554618.1	Citation: Biochem J. 2003 Jan 15;369(Pt 2):275-85
YP_554619.1	Citation: Biochem J. 2003 Jan 15;369(Pt 2):275-85
YP_554633.1	catalyzes the formation of pyruvate and beta-alanine from L-alanine and 3-oxopropanoate
YP_554656.1	Protocatechuate pathway; Citation: Nucleic Acids Res. 32 (19), 5766- 5779(2004)
YP_554658.1	Catalyzes the cycloisomerization of cis,cis-muconate
YP_554736.1	this stereospecific enzymes reduces the S isomer of methionine sulfoxide while MsrB reduces the R form; provides protection against oxidative stress
YP_554744.1	allantoate amidohydrolase and N-carbamoyl-L-amino acid amidohydrolase are very similar; the allantoate amidohydrolase from Escherichia coli forms a dimer and binds zinc ions for catalytic activity and catalyzes the conversion of allantoate to (S)-ureidoglycolate and ammonia; carbamoyl amidohydrolase from Bacillus sp. converts N-carbamoyl amino acids to amino acids, ammonia, and carbon dioxide
YP_554751.1	catalyzes the reaction of cyanate and bicarbonate to produce ammonia and carbon dioxide
YP_554776.1	part of the FhuBCD ATP-dependent iron (III) hydroxamate transporter involved in the high-affinity transport of Fe(3+)-ferrichrome
YP_554780.1	RNA polymerase sigma factor involved in the synthesis of the siderophores pyoverdine in Pseudomonas and malleobactin in Burkholderia; also involved in the synthesis of exotoxin and PrpL protease
YP_554791.1	catalyzes the oxidation of UDP-N-acetyl-D-mannosamine to UDP-N-acetylmannosaminuronic acid
YP_554837.1	catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate in leucine biosynthesis; forms a heterodimer of LeuC/D
YP_554838.1	dehydratase component, catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate
YP_554890.1	catalyzes a two-step reaction, first charging a tryptophan molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA
YP_554919.1	catalyzes the formation of beta-ketovaleryl-CoA from acetyl-CoA and propionyl-CoA
YP_554935.1	catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates
YP_554936.1	catalyzes the transamination of the branched-chain amino acids to their respective alpha-keto acids
YP_554940.1	Enables the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation
YP_554941.1	Catalyzes a key regulatory step in fatty acid biosynthesis
YP_554958.1	in Pseudomonas aeruginosa this enzyme is a trimer of dimers; essential for membrane formation; performs third step of type II fatty acid biosynthesis; catalyzes dehydration of (3R)-hydroxyacyl-ACP to trans-2-acyl-ACP
YP_554980.1	catalyzes the radical-mediated insertion of two sulfur atoms into an acyl carrier protein (ACP) bound to an octanoyl group to produce a lipoyl group
YP_555013.1	catalyzes the oxidation of tricarballylate to cis-aconitate; FAD-dependent; required for the utilization of tricarballylate as a carbon and energy source by S. enterica
YP_555014.1	catalyzes the conversion of salicylyl-CoA to gentisyl-CoA
YP_555017.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_555078.1	catalyzes the formation of D-glucono-1,5-lactone 6-phosphate from D-glucose 6-phosphate
YP_555088.1	rubredoxin
YP_555111.1	catalyzes the formation of L-aspartate to iminoaspartate in NAD(+) biosynthesis
YP_555117.1	member of a large family of NAD or NADP-dependent oxidoreductases; paralogs occur in many bacteria
YP_555151.1	catalyzes the formation of benzaldehyde from benzoylformate
YP_555152.1	Mandelate pathway; Citation: Biochemistry 29 (42), 9856-9862 (1990)
YP_555153.1	Mandelate pathway; Citation: Biochemistry 29 (42), 9856-9862 (1990)
YP_555219.1	catalyzes the degradation of histidine to urocanate and ammmonia
YP_555221.1	upregulated by FixLJ/FixK under oxygen limitation; involved in regulation of genes involved in carbon and amino acid metabolism
YP_555252.1	catalyzes the hydrolysis of acylphosphate
YP_555256.1	catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP); functions in the nonmevalonate isoprenoid biosynthesis pathway
YP_555308.1	Citation: Appl. Environ. Microbiol. 69 (12),7257- 7265 (2003)
YP_555320.1	produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a catalytic subunit
YP_555322.1	produces ATP from ADP in the presence of a proton gradient across the membrane; subunit C is part of the membrane proton channel F0
YP_555323.2	produces ATP from ADP in the presence of a proton gradient across the membrane; subunit A is part of the membrane proton channel F0
YP_555325.1	produces ATP from ADP in the presence of a proton gradient across the membrane; the epsilon subunit is part of the catalytic core of the ATP synthase complex
YP_555326.1	produces ATP from ADP in the presence of a proton gradient across the membrane; the beta chain is a regulatory subunit
YP_555327.1	Catalyzes a key regulatory step in fatty acid biosynthesis
YP_555328.1	Enables the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation
YP_555333.1	catalyzes the formation of 2-oxobutanoate from L-threonine; involved in ectoine utilization
YP_555334.1	putative cyclodeaminase
YP_555410.1	60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; the rhizobia and high GC gram-positive bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the R. leguminosarum protein in this cluster is transcribed under anaerobic conditions and is not necessary for growth
YP_555411.1	10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring
YP_555438.1	catalyzes the formation of nicotinamide adenine dinucleotide (NAD) from nicotinic acid adenine dinucleotide (NAAD) using either ammonia or glutamine as the amide donor and ATP; ammonia-utilizing enzymes include the ones from Bacillus and Escherichia coli while glutamine-utilizing enzymes include the Mycobacterial one; forms homodimers
YP_555472.1	catalyzes the hydrolysis of D-alanyl-D-alanine dipeptide: Zn dependent; involved in peptidoglycan synthesis
YP_555522.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_555548.1	NHL repeat
YP_555550.1	converts (S)-3-hydroxybutanoyl-CoA to 3-acetoacetyl-CoA
YP_555575.1	Citation: Biochem. J. 330 (Pt 3), 1375-1381 (1998)
YP_555581.1	catalyzes the oxidation of L-histidinol to L-histidinaldehyde and then to L-histidine in histidine biosynthesis; functions as a dimer
YP_555597.1	catalyzes the formation of beta-ketovaleryl-CoA from acetyl-CoA and propionyl-CoA
YP_555607.1	Potentially has regulatory function as described for AmpD on AmpC beta-lactamase expression, though other protein in LB400 has significantly higher similarity with AmpD.
YP_555622.1	Citation: Adv Microb Physiol 2001; 45:50-112
YP_555623.1	Citation: Adv Microb Physiol 2001; 45:50-112
YP_555624.1	periplasmic; catalytic subunit; with NapBC catalyzes the reduction of nitrate to nitrite; NapAB receives electrons from NapC
YP_555625.1	Citation: Adv Microb Physiol 2001; 45:50-112
YP_555626.1	Citation: Adv Microb Physiol 2001; 45:50-112
YP_555646.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_555647.1	lipoprotein signal peptidase; integral membrane protein that removes signal peptides from prolipoproteins during lipoprotein biosynthesis
YP_555648.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_555649.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_555659.1	catalyzes the oxidative deamination of D-amino acids
YP_555696.1	Citation: Mol. Plant Microbe Interact. 14 (7),887- 894 (2001)
YP_555697.1	Citation: Mol. Plant Microbe Interact. 14 (7),887- 894 (2001)
YP_555721.1	catalyzes the reaction of cyanate and bicarbonate to produce ammonia and carbon dioxide
YP_555771.1	contains CheB and CheR domains
YP_555795.1	catalyzes the interconversion of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate
YP_555827.1	Citation: J. Bacteriol. 177:676-687(1995).
YP_555829.1	Citation: J. Bacteriol. 182:3784-3793(2000)
YP_555833.1	Citation: J. Bacteriol. 182:3784-3793(2000).
YP_555834.1	Citation: J. Bacteriol. 181:2675-2682(1999).
YP_555835.1	Citation: J. Bacteriol. 181:2675-2682(1999).
YP_555839.1	Citation: J. Bacteriol. 182:3784-3793(2000).
YP_555840.1	Citation:  J. Bacteriol. 182:3784-3793(2000) J.Bacteriol. 186:3631-3639(2004), Can. J. Microbiol.48:49- 59(2002).
YP_555841.1	Citation: J. Bacteriol. 186:3631-3639(2004)
YP_555842.1	Citation: J. Bacteriol. 186:3631-3639(2004)
YP_555843.1	Citation: J. Bacteriol. 186:3631-3639(2004)
YP_555844.1	converts (S)-3-hydroxybutanoyl-CoA to 3-acetoacetyl-CoA
YP_555845.1	Citation: J. Bacteriol. 186:3631-3639(2004)
YP_555847.1	Citation: J. Bacteriol. 186:3631-3639(2004), Can.J. Microbiol. 48:49-59(2002)
YP_555851.1	Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA
YP_555853.1	Citation: J. Bacteriol. 186:3631-3639(2004)
YP_555854.1	Citation: J. Bacteriol. 186:3631-3639(2004)
YP_555855.1	Citation: J. Bacteriol. 186:3631-3639(2004)
YP_555856.1	Citation: J. Bacteriol. 186:3631-3639(2004)
YP_555862.1	catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates
YP_555879.1	Citation: J. Bacteriol. 186:3631-3639(2004), Can.J. Microbiol. 48:49-59(2002)
YP_555886.1	Citation: J. Bacteriol. 181:2675-2682(1999)
YP_555887.1	Citation: J. Bacteriol. 182:3784-3793(2000)
YP_555888.1	Citation: J. Bacteriol. 182:3784-3793(2000)
YP_555980.1	reversible synthesis of carbamate and ATP from carbamoyl phosphate and ADP
YP_555981.1	catalyzes the formation of ornithine and carbamylphosphate from citrulline in the arginine catabolic pathway
YP_555982.1	catalyzes the degradation of arginine to citruline and ammonia
YP_555994.1	catalyzes the hydrolytic cleavage of imides that range from linear to heterocyclic and that include hydantoins, dihydropyrimidines, and phthalimides
YP_556034.1	Catalyzes the deamination of cytosine to uracil and ammonia
YP_556080.1	activates fatty acids by binding to coenzyme A
YP_556108.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_556109.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_556110.1	lipoprotein signal peptidase; integral membrane protein that removes signal peptides from prolipoproteins during lipoprotein biosynthesis
YP_556111.1	ISPpu12; Citation: J Bacteriol. 2002 Dec;184(23):6572-80
YP_556113.1	Phenylacetyl-CoA pathway; Citation: Proc. Natl. Acad. Sci. U.S.A. 95 (11), 6419-6424 (1998). J. Bacteriol. 182 (2), 286-294 (2000).Environ Microbiol. 2002 Dec;4(12):824-41
YP_556115.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Mol. Microbiol. 2004 Oct;54(1):223-38. Appl EnvironMicrobiol. 2004 Aug;70(8):4961-70.
YP_556116.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Mol. Microbiol. 2004 Oct;54(1):223-38. Appl EnvironMicrobiol. 2004 Aug;70(8):4961-70.
YP_556117.1	cleaves the ring of 2,3-dihydro-2,3-dihydroxybenzoyl-CoA forming 6-hydroxy-3-hexenoyl-CoA
YP_556118.1	consists of N-terminal helix-turn-helix domain and C-terminal shikimate kinase-like domain which may bind benzoyl-CoA; controls inducible expression of the bzd catabolic operon that is involved in the anaerobic catabolism of benzoate
YP_556119.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Appl Environ Microbiol. 2004 Aug;70(8):4961-70.
YP_556120.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Appl Environ Microbiol. 2004 Aug;70(8):4961-70.
YP_556121.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Appl Environ Microbiol. 2004 Aug;70(8):4961-70.
YP_556122.1	Citation: J. Bacteriol. 2002 Nov;184(22):6301- 15.Appl Environ Microbiol. 2004 Aug;70(8):4961-70.
YP_556126.1	catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis
YP_556149.1	consists of N-terminal helix-turn-helix domain and C-terminal shikimate kinase-like domain which may bind benzoyl-CoA; controls inducible expression of the bzd catabolic operon that is involved in the anaerobic catabolism of benzoate
YP_556213.1	catalyzes the formation of 3-(2,3-dihydroxyphenyl)propionate from 3-(3-hydroxyphenyl)propionate
YP_556216.1	Putative regulator of homogentisate pathway (HmgR)
YP_556217.1	An oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanine
YP_556218.1	Homogentisate pathway; Citation: Environ Microbiol. 2002 Dec;4(12):824- 41.J. Bacteriol. 186 (15), 5062-5077 (2004)
YP_556246.1	An oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanine
YP_556251.1	converts 3-hydroxyadipyl-CoA to beta-ketoadipyl-CoA in phenylacetate degradation
YP_556280.1	paralogs to the E1 component of pyruvate dehydrogenase subunit E1
YP_556325.1	Citation: J. Bacteriol. 182 (20), 5849-5863 (2000)
YP_556334.1	Citation: J. Bacteriol. 185 (19), 5871-5881(2003).
YP_556335.1	Citation:  J. Bacteriol. 185 (19), 5871-5881(2003).
YP_556336.1	Citation:  J. Bacteriol. 185 (19), 5871-5881(2003).
YP_556337.1	Citation:  J. Bacteriol. 185 (19), 5871-5881(2003).
YP_556338.1	for anthranilate dioxygenase genes; Citation: J. Bacteriol. 185 (19), 5871-5881 (2003)
YP_556377.1	catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; also known as acetolactate synthase large subunit
YP_556387.1	Citation: Mol Microbiol. 1995 Sep;17(6):1189-200
YP_556388.1	Citation: Mol Microbiol. 1995 Sep;17(6):1189-200
YP_556389.1	Citation: Mol Microbiol. 1995 Sep;17(6):1189-200
YP_556398.1	biphenyl pathway; Citation: J. Bacteriol. 174 (9), 2903-2912 (1992). Gene 144 (1), 9-16 (1994)
YP_556399.1	catalyzes the formation of pyruvate and acetaldehyde from 4-hydroxy-2-ketovaleric acid; involved in the degradation of phenylpropionate
YP_556400.1	catalyzes the formation of acetyl-CoA from acetalaldehyde
YP_556401.1	biphenyl pathway; Citation: J. Bacteriol. 174 (9), 2903-2912 (1992). Gene 144 (1), 9-16 (1994)
YP_556402.1	biphenyl pathway; Citation: J. Bacteriol. 174 (9), 2903-2912 (1992). Gene 144 (1), 9-16 (1994)
YP_556403.1	biphenyl pathway; Citation: J. Bacteriol. 174 (9), 2903-2912 (1992)
YP_556404.1	Converts cis-3-(3-carboxyethyl)-3,5-cyclohexadiene-1,2-diol (PP-dihydrodiol) into 3-(2,3-dihydroxylphenyl)propionate
YP_556405.1	biphenyl pathway; Citation: J. Bacteriol. 174 (9), 2903-2912 (1992)
YP_556406.1	biphenyl pathway; Citation: J. Bacteriol. 174 (9), 2903-2912 (1992)
YP_556407.1	biphenyl pathway; Citation: J. Bacteriol. 174 (9), 2903-2912 (1992)
YP_556408.1	biphenyl pathway; Citation: J. Bacteriol. 174 (9), 2903-2912 (1992)
YP_556409.1	biphenyl pathway; Citation: J. Bacteriol. 174 (9), 2903-2912 (1992)
YP_556410.1	biphenyl pathway; Citation: Microbiology 147(Pt 8):2169-82 (2001)
YP_556494.1	catalyzes the formation of acetate from pyruvate
YP_556519.1	catalyzes the formation of L-ornithine from N(2)-acetyl-L-ornithine
YP_556530.1	catalyzes the formation of S-ureidoglycolate and urea from allantoate
YP_556559.1	catalyzes the formation of 3-methyl-2-oxobutanoate from 2,3,-dihydroxy-3-methylbutanoate