u_prommatches8

Gene list

Wadsworth clusters

Rajewsky clusters


Score

Strand

Gene name

Blattner ID

Description

EcoCyc link

SwissProt comment

2.928245-fimZb0535fimbrial Z protein; probable signal transducer EG11103 SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE). SIMILARITY: TO OTHER BACTERIAL REGULATORY PROTEINS INVOLVED IN SIGNAL TRANSDUCTION. SIMILARITY: BELONGS TO THE LUXR/UHPA FAMILY OF TRANSCRIPTIONAL REGULATORS.
0.989214+yjbNb4049orf, hypothetical protein EG11932 SIMILARITY: BELONGS TO THE UPF0034 (NIFR3/SMM1) FAMILY. STRONG, TO H.INFLUENZAE HI0634.
yjbOb4050orf, hypothetical protein EG11933
0.985437-ybcIb0527orf, hypothetical protein EG12708
0.874748+hisLb2018his operon leader peptide EG11269 FUNCTION: THIS PROTEIN IS INVOLVED IN THE ATTENUATION MECHANISM FOR THE CONTROL OF THE EXPRESSION OF THE HIS STRUCTURAL GENES.
hisGb2019ATP phosphoribosyltransferase EG10449 CATALYTIC ACTIVITY: 1-(5-PHOSPHO-D-RIBOSYL)-ATP + PYROPHOSPHATE = ATP + 5-PHOSPHO-ALPHA-D-RIBOSE 1-DIPHOSPHATE. PATHWAY: FIRST STEP IN HISTIDINE BIOSYNTHETIC PATHWAY. IS VERY IMPORTANT IN THE REGULATION OF HISTIDINE METABOLISM. SUBUNIT: HOMOHEXAMER. SUBCELLULAR LOCATION: CYTOPLASMIC. SIMILARITY: BELONGS TO THE ATP PHOSPHORIBOSYLTRANSFERASE FAMILY.
hisDb2020L-histidinal:NAD+ oxidoreductase; L-histidinol:NAD+ oxidoreductase EG10447 FUNCTION: THIS PROTEIN IS CONSIDERED AS A BIFUNCTIONAL ENZYME, POSSESSING TWO ACTIVE SITES, ONE AN ALCOHOL DEHYDROGENASE AND THE OTHER AN ALDEHYDE DEHYDROGENASE. CATALYTIC ACTIVITY: L-HISTIDINOL + 2 NAD(+) = L-HISTIDINE + 2 NADH. PATHWAY: TENTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY. SUBUNIT: HOMODIMER. SIMILARITY: TO OTHER PROKARYOTIC, FUNGAL AND PLANTS HDH.
hisCb2021histidinol-phosphate aminotransferase EG10446 CATALYTIC ACTIVITY: L-HISTIDINOL-PHOSPHATE + 2-OXOGLUTARATE = 3-(IMIDAZOL-4-YL)-2-OXOPROPYL PHOSPHATE + GLUTAMATE. COFACTOR: PYRIDOXAL PHOSPHATE. PATHWAY: EIGHTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY. SUBUNIT: HOMODIMER. SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT AMINOTRANSFERASES.
hisBb2022imidazoleglycerolphosphate dehydratase and histidinol-phosphate phosphatase EG10445 CATALYTIC ACTIVITY: D-ERYTHRO-1-(IMIDAZOL-4-YL)GLYCEROL 3-PHOSPHATE = 3-(IMIDAZOL-4-YL)-2-OXOPROPYL PHOSPHATE + H(2)O. CATALYTIC ACTIVITY: L-HISTIDINOL-PHOSPHATE + H(2)O = L-HISTIDINOL + ORTHOPHOSPHATE. PATHWAY: SEVENTH & NINTH STEPS IN HISTIDINE BIOSYNTHETIC PATHWAY. SUBCELLULAR LOCATION: CYTOPLASMIC. SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE FAMILY.
hisHb2023glutamine amidotransferase subunit of heterodimer with HisF = imidazole glycerol phosphate synthase holoenzyme EG10450 FUNCTION: CATALYZES AN AMIDOTRANSFERASE REACTION THAT GENERATES IMIDAZOLE-GLYCEROL PHOSPHATE AND 5-AMINOIMIDAZOL-4-CARBOXAMIDE RIBONUCLEOTIDE, WHICH IS USED FOR PURINE SYNTHESIS. PATHWAY: FIFTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY. SUBCELLULAR LOCATION: CYTOPLASMIC. SIMILARITY: BELONGS TO THE HISH FAMILY. SIMILARITY: CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN.
hisAb2024N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'- phosphoribosyl)-4-imidazolecarboxamide isomerase EG10444 CATALYTIC ACTIVITY: N-(5'-PHOSPHO-D-RIBOSYLFORMIMINO)-5-AMINO-1- (5''-PHOSPHORIBOSYL)-4-IMIDAZOLECARBOXAMIDE = N-(5'-PHOSPHO-D-1'- RIBULOSYLFORMIMINO)-5-AMINO-1-(5''-PHOSPHORIBOSYL)-4- IMIDAZOLECARBOXAMIDE. PATHWAY: FOURTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY. SUBUNIT: MONOMER. SUBCELLULAR LOCATION: CYTOPLASMIC. SIMILARITY: BELONGS TO THE HISA / HISF FAMILY.
hisFb2025imidazole glycerol phosphate synthase subunit in heterodimer with HisH = imidazole glycerol phsphate synthase holoenzyme EG10448 FUNCTION: CATALYZES THE CYCLIZATION REACTION THAT PRODUCES D-ERYTHRO-IMIDAZOLE GLYCEROL PHOSPHATE. PATHWAY: SIXTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY. SUBUNIT: MONOMER. SUBCELLULAR LOCATION: CYTOPLASMIC. SIMILARITY: BELONGS TO THE HISA / HISF FAMILY.
hisIb2026phosphoribosyl-amp cyclohydrolase; phosphoribosyl-ATP pyrophosphatase EG10451 CATALYTIC ACTIVITY: 5-PHOSPHORIBOSYL-ATP + H(2)O = 5-PHOSPHORIBOSYL-AMP + PYROPHOSPHATE. CATALYTIC ACTIVITY: 5-PHOSPHORIBOSYL-AMP + H(2)O = 5-(5-PHOSPHO-D-RIBOSYLAMINOFORMIMINO)-1-(5-PHOSPHO-RIBOSYL) IMIDAZOLE-4-CARBOXAMIDE. PATHWAY: SECOND AND THIRD STEPS IN HISTIDINE BIOSYNTHETIC PATHWAY. SUBCELLULAR LOCATION: CYTOPLASMIC.
0.738567+tsrb4355methyl-accepting chemotaxis protein I, serine sensor receptor EG11034 FUNCTION: RECEPTOR FOR THE ATTRACTANT L-SERINE AND RELATED AMINO ACIDS AND IS ALSO RESPONSIBLE FOR CHEMOTAXIS AWAY FROM A WIDE RANGE OF REPELLENTS, INCLUDING LEUCINE, INDOLE, AND WEAK ACIDS. FUNCTION: CHEMOTACTIC-SIGNAL TRANSDUCERS RESPOND TO CHANGES IN THE CONCENTRATION OF ATTRACTANTS AND REPELLENTS IN THE ENVIRONMENT, TRANSDUCE A SIGNAL FROM THE OUTSIDE TO THE INSIDE OF THE CELL, AND FACILITATE SENSORY ADAPTATION THROUGH THE VARIATION OF THE LEVEL OF METHYLATION. ATTRACTANTS INCREASE THE LEVEL OF METHYLATION WHILE REPELLENTS DECREASE THE LEVEL OF METHYLATION, THE METHYL GROUPS ARE ADDED BY THE METHYLTRANSFERASE CHER AND REMOVED BY THE METHYLESTERASE CHEB. SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE. SIMILARITY: BELONGS TO THE CHEMOTAXIS SENSORY TRANSDUCERS FAMILY.
0.706063+b1741b1741putative excinuclease subunit
0.702040+dbpAb1343ATP-dependent RNA helicase EG10210 FUNCTION: COULD PLAY A MAJOR ROLE IN RIBOSOME ASSEMBLY, SPECIFICALLY IN THE ASSEMBLY PROCESS OF THE ACTIVE CENTER OF 50S RIBOSOMAL SUBUNITS. HAS AN ATP-DEPENDENT HELICASE ACTIVITY. CAN UNWIND THE 23S RRNA AS WELL AS 16S RRNA. CAN HYDROLYSE ATP ONLY IN THE PRESENCE OF BACTERIAL 23S RRNA. SIMILARITY: BELONGS TO THE "DEAD" BOX FAMILY HELICASE.
0.584827+b1729b1729part of a kinase EG13990 SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE). SIMILARITY: BELONGS TO THE SODIUM:DICARBOXYLATE SYMPORTER FAMILY (SDF). STRONG, TO H.INFLUENZAE HI1154.
0.534804+serSb0893serine tRNA synthetase; also charges selenocystein tRNA with serine EG10947 CATALYTIC ACTIVITY: ATP + L-SERINE + TRNA(SER) = AMP + PYROPHOSPHATE + L-SERYL-TRNA(SER). SUBUNIT: HOMODIMER. SUBCELLULAR LOCATION: CYTOPLASMIC. SIMILARITY: BELONGS TO CLASS-II AMINOACYL-TRNA SYNTHETASE FAMILY.
0.531471+metFb39415,10-methylenetetrahydrofolate reductase EG10585 CATALYTIC ACTIVITY: 5-METHYLTETRAHYDROFOLATE + ACCEPTOR = 5,10-METHYLENETETRAHYDROFOLATE + REDUCED ACCEPTOR. COFACTOR: FAD. PATHWAY: METHIONINE BIOSYNTHESIS. SUBUNIT: HOMOTETRAMER. SIMILARITY: BELONGS TO THE METHYLENETETRAHYDROFOLATE REDUCTASE (EC 1.5.1.20/EC 1.7.99.5) FAMILY.
0.515222+b2710b2710putative flavodoxin
ygbDb2711putative oxidoreductase EG12450 COFACTOR: FAD (BY SIMILARITY). SIMILARITY: STRONG, TO FERREDOXINS/ADRENODOXINS REDUCTASES.
0.483741-b3975b3975orf, hypothetical protein
0.441093+b1446b1446orf, hypothetical protein EG13768
0.412777+b2389b2389orf, hypothetical protein
b2390b2390orf, hypothetical protein EG14385 SIMILARITY: TO E.COLI YAAX.
b2391b2391orf, hypothetical protein
0.389992+hdeDb3511orf, hypothetical protein EG11495
0.386763+rcsAb1951positive regulator for ctr capsule biosynthesis, positive transcription factor EG10820 FUNCTION: POSITIVE REGULATOR OF CAPSULAR POLYSACCHARIDE SYNTHESIS. RCSA AND RCSB FORM A COMPLEX TO PROMOTE TRANSCRIPTION OF THE GENES FOR CAPSULE SYNTHESIS. MISCELLANEOUS: DEGRADATION OF THE RCSA PROTEIN IN VIVO DEPENDS ON THE LON PROTEASE. ITS STABILITY IS INCREASED BY RCSB. RCSA* IS MORE STABLE THAN RCSA. SIMILARITY: BELONGS TO THE LUXR/UHPA FAMILY OF TRANSCRIPTIONAL REGULATORS.
0.379440+ybbXb0512putative hydrolase EG13619 FUNCTION: INVOLVED IN THE ANAEROBIC UTILIZATION OF ALLANTOIN. CATALYTIC ACTIVITY: ALLANTOIN + H(2)O = ALLANTOATE. COFACTOR: ZINC (BY SIMILARITY). PATHWAY: FIRST STEP IN THE DEGRADATION OF ALLANTOIN (PURINE CATABOLISM). INDUCTION: BY GLYOXYLATE. SIMILARITY: BELONGS TO THE DHOASE FAMILY.
ybbYb0513putative transport EG13620 SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). INDUCTION: BY GLYOXYLATE. SIMILARITY: BELONGS TO THE XANTHINE/URACIL PERMEASES FAMILY. STRONG, TO B.SUBTILIS YWDJ.
ybbZb0514orf, hypothetical protein EG13621 CATALYTIC ACTIVITY: ATP + (R)-GLYCERATE = ADP + 3-PHOSPHO-(R)- GLYCERATE. PATHWAY: GLYOXYLATE CATABOLISM. INDUCTION: BY GLYOXYLATE. SIMILARITY: BELONGS TO THE UPF0068 FAMILY.
0.378000-yefMb2017orf, hypothetical protein EG12844 SIMILARITY: BELONGS TO THE PHD/YEFM FAMILY.
0.365285+yafMb0228orf, hypothetical protein EG13150 SIMILARITY: STRONG, TO H.INFLUENZAE HI0217.
0.352960+ptab2297phosphotransacetylase EG20173 CATALYTIC ACTIVITY: ACETYL-COA + ORTHOPHOSPHATE = COA + ACETYL PHOSPHATE. PATHWAY: LAST OF TWO STEPS IN THE CONVERSION OF ACETATE TO ACETYL-COA. SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL). SIMILARITY: IN THE N-TERMINAL SECTION; CONTAINS A DOMAIN WITH SOME SIMILARITIES WITH COBQ/BIOD. SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE PHOSPHATE ACETYLTRANSFERASE AND BUTYRYLTRANSFERASE FAMILY.
0.347465+tauAb0365taurine transport system periplasmic protein EG13300 FUNCTION: PART OF A BINDING-PROTEIN-DEPENDENT TRANSPORT SYSTEM FOR TAURINE. SUBCELLULAR LOCATION: PERIPLASMIC (POTENTIAL). SIMILARITY: TO SYNECHOCYSTIS PCC 6803 SLL0473.
tauBb0366taurine ATP-binding component of a transport system EG13299 FUNCTION: PART OF A BINDING-PROTEIN-DEPENDENT TRANSPORT SYSTEM FOR TAURINE. PROBABLY RESPONSIBLE FOR ENERGY COUPLING TO THE TRANSPORT SYSTEM. SUBCELLULAR LOCATION: INNER MEMBRANE-ASSOCIATED (POTENTIAL). SIMILARITY: BELONGS TO THE ATP-BINDING TRANSPORT PROTEIN FAMILY (ABC TRANSPORTERS).
tauCb0367taurine transport system permease protein EG13301 FUNCTION: PART OF A BINDING-PROTEIN-DEPENDENT TRANSPORT SYSTEM FOR TAURINE. PROBABLY RESPONSIBLE FOR THE TRANSLOCATION OF THE SUBSTRATE ACROSS THE MEMBRANE. SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE (POTENTIAL). SIMILARITY: WITH INTEGRAL MEMBRANE COMPONENTS OF OTHER BINDING- PROTEIN-DEPENDENT TRANSPORT SYSTEMS. BELONGS TO THE CYSTW SUBFAMILY.
tauDb0368taurine dioxygenase, 2-oxoglutarate-dependent EG12423 FUNCTION: CONVERTS TAURINE AND ALPHA KETOGLUTARATE TO SULFITE, AMINOACETALDEHYDE AND SUCCINATE. REQUIRED FOR THE UTILIZATION OF TAURINE (2-AMINOETHANESULFONIC ACID) AS A SULFUR SOURCE. OPTIMAL PH FOR ACTIVITY IS 6.9. PENTANE-SULFONIC ACID, 3-(N- MORPHOLINO)PROPANESULFONIC ACID AND 1,3-DIOXO-2- ISOINDOLINEETHANESULFONIC ACID ARE ALSO SUBSTRATES FOR THIS ENZYME. CATALYTIC ACTIVITY: TAURINE + 2-OXOGLUTARATE + O(2) = SULFITE + AMINOACETALDEHYDE + SUCCINATE + CO(2). COFACTOR: IRON AND ASCORBATE. ENZYME REGULATION: DIVALENT METAL IONS INHIBITED. PATHWAY: CATABOLISM OF TAURINE. SUBUNIT: HOMODIMER. INDUCTION: UNDER SULFUR STARVATION. SIMILARITY: BELONGS TO THE TFDA FAMILY OF DIOXYGENASES. CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO FRAMESHIFTS.
0.346145-maoCb1387putative aldehyde dehydrogenase EG13735 PATHWAY: AEROBIC CATABOLISM OF PHENYLACETIC ACID. INDUCTION: ACTIVATED BY CAMP RECEPTOR PROTEIN (CRP) AND INTEGRATION HOST FACTOR (IHF). INHIBITED BY PAAX. SIMILARITY: BELONGS TO THE ALDEHYDE DEHYDROGENASES FAMILY.
0.316795+ygeXb2871putative dehydratase EG13054 FUNCTION: CATALYZES THE ALPHA,BETA-ELIMINATION REACTION OF BOTH L- AND D-ALPHA,BETA-DIAMINOPROPIONATE, THE MOST SUITABLE SUBSTRATES TO FORM PYRUVATE AND AMMONIA. THE L- AND D-ISOMERS OF SERINE ARE ALSO DEGRADED, THOUGH SLOWLY; IT IS THE ONLY SERINE DEHYDRATASE WHICH CAN ELIMINATE AN AMINO GROUP AT THE BETA-CARBON POSITION (BY SIMILARITY). CATALYTIC ACTIVITY: 2,3-DIAMINOPROPIONATE = PYRUVATE + 2 NH(3). COFACTOR: PYRIDOXAL PHOSPHATE. SIMILARITY: TO S.TYPHIMURIUM DIAMINOPROPIONATE AMMONIA-LYASE AND TO THREONINE DEHYDRATASES.
ygeYb2872putative deacetylase EG13055 SIMILARITY: BELONGS TO PEPTIDASE FAMILY M20A; ALSO KNOWN AS THE ARGE/DAPE/ACY1/CPG2/YSCS FAMILY.
b2873b2873orf, hypothetical protein EG13056 SIMILARITY: BELONGS TO THE DEHYDROPYRIMIDINASE FAMILY.
yqeAb2874putative kinase EG13057 SIMILARITY: BELONGS TO THE CARBAMATE KINASE FAMILY.
0.311596+gloAb1651lactoylglutathione lyase EG13421 FUNCTION: CATALYZES THE CONVERSION OF HEMIMERCAPTAL, FORMED FROM METHYLGLYOXAL AND GLUTATHIONE, TO S-LACTOYLGLUTATHIONE. CATALYTIC ACTIVITY: (R)-S-LACTOYLGLUTATHIONE = GLUTATHIONE + METHYLGLYOXAL. COFACTOR: BINDS ONE NICKEL ION PER MOLECULE. PATHWAY: GLYOXAL PATHWAY. SUBUNIT: HOMODIMER. MASS SPECTROMETRY: MW=19419; METHOD=ELECTROSPRAY. SIMILARITY: BELONGS TO THE GLYOXALASE I FAMILY.
rntb1652RNase T, degrades tRNA EG11547 FUNCTION: RESPONSIBLE FOR THE END-TURNOVER OF TRNA: SPECIFICALLY REMOVES THE TERMINAL AMP RESIDUE FROM UNCHARGED TRNA (TRNA-C-C-A). ALSO APPEARS TO BE INVOLVED IN TRNA BIOSYNTHESIS, ESPECIALLY IN STRAINS LACKING OTHER EXORIBONUCLEASES. SUBUNIT: HOMODIMER. SIMILARITY: BELONGS TO THE RNASE T FAMILY.
lhrb1653member of ATP-dependent helicase superfamily II EG11548 SIMILARITY: WITH OTHER ATP DEPENDENT HELICASES.
0.305442+ilvLb3766ilvGEDA operon leader peptide EG11270
ilvG_1b3767acetolactate synthase II, large subunit, cryptic, interrupted EG10498 CATALYTIC ACTIVITY: 2-ACETOLACTATE + CO(2) = 2-PYRUVATE (THIS ENZYME ALSO CATALYZES FORMATION OF 2-ACETO-2-HYDROXYBUTANOATE). COFACTOR: THIAMINE PYROPHOSPHATE, AND MAGNESIUM ION. PATHWAY: FIRST STEP IN VALINE AND ISOLEUCINE BIOSYNTHESIS. SUBUNIT: TETRAMER OF TWO LARGE AND TWO SMALL CHAINS. MISCELLANEOUS: E.COLI CONTAINS GENES FOR 3 AHAS ISOZYMES: ILVBN, ILVGM AND ILVIH. ONLY THE VAL-INHIBITABLE ILVBN & ILVIH ARE EXPRESSED. ILVG, VAL-RESISTANT, IS EXPRESSED IN STRAINS HAVING THE ILV0 MUTATION. THE ILV02096 MUTATION (AN INSERTION OF 2 BP) CAUSES A FRAMESHIFT IN TRANSLATION, PERMITTING THE EXPRESSION OF THIS ISOZYME. SIMILARITY: WITH OTHER ENZYMES WHICH REQUIRE TPP.
0.290934+yaaFb0030orf, hypothetical protein EG11082 SIMILARITY: BELONGS TO THE IUNH FAMILY.
0.287811+hydHb4003sensor kinase for HydG, hydrogenase 3 activity EG10008 FUNCTION: MEMBER OF THE TWO-COMPONENT REGULATORY SYSTEM HYDH/HYDG INVOLVED IN THE REGULATION OF THE LABILE HYDROGENASE ACTIVITY. HYDH MAY FUNCTION AS A MEMBRANE-ASSOCIATED PROTEIN KINASE THAT PHOSPHORYLATES HYDG IN RESPONSE TO ENVIRONMENTAL SIGNALS. SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE (PROBABLE). SIMILARITY: TO OTHER PROKARYOTIC SENSORY TRANSDUCTION HISTIDINE KINASES.
hydGb4004response regulator of hydrogenase 3 activity (sensor HydH) EG10482 FUNCTION: MEMBER OF THE TWO-COMPONENT REGULATORY SYSTEM HYDH/HYDG INVOLVED IN THE REGULATION OF THE LABILE HYDROGENASE ACTIVITY. WHEN ACTIVATED BY HYDH IT ACTS IN CONJUNCTION WITH SIGMA-54 AS A TRANSCRIPTIONAL ACTIVATOR. SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE). PTM: PHOSPHORYLATED BY HYDH (PROBABLE). SIMILARITY: THE N-TERMINAL REGION IS SIMILAR TO THAT OF OTHER REGULATORY COMPONENTS OF SENSORY TRANSDUCTION SYSTEMS. SIMILARITY: THE CENTRAL REGION CONTAINS A SIGMA-54 FACTOR INTERACTION ATP-BINDING DOMAIN.
0.268001+acrDb2470sensitivity to acriflavine, integral membrane protein, possible efflux pump EG10014 FUNCTION: PARTICIPATES IN THE EFFLUX OF AMINOGLYCOSIDES. CONFERS RESISTANCE TO A VARIETY OF THESE SUBSTANCES. SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE (BY SIMILARITY). SIMILARITY: BELONGS TO THE ACRB/ACRD/ACRF FAMILY.
0.258511-aspCb0928aspartate aminotransferase EG10096 CATALYTIC ACTIVITY: L-ASPARTATE + 2-OXOGLUTARATE = OXALOACETATE + L-GLUTAMATE. COFACTOR: PYRIDOXAL PHOSPHATE. SUBUNIT: HOMODIMER. SUBCELLULAR LOCATION: CYTOPLASMIC. SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT AMINOTRANSFERASES.
0.255496+aceEb0114pyruvate dehydrogenase (decarboxylase component) EG10024 FUNCTION: THE PYRUVATE DEHYDROGENASE COMPLEX CATALYZES THE OVERALL CONVERSION OF PYRUVATE TO ACETYL-COA & CO(2). IT CONTAINS MULTIPLE COPIES OF THREE ENZYMATIC COMPONENTS: PYRUVATE DEHYDROGENASE (E1), DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2) & LIPOAMIDE DEHYDROGENASE (E3). CATALYTIC ACTIVITY: PYRUVATE + LIPOAMIDE = S-ACETYL-DIHYDRO- LIPOAMIDE + CO(2). COFACTOR: THIAMINE PYROPHOSPHATE. SUBUNIT: HOMODIMER.
aceFb0115pyruvate dehydrogenase (dihydrolipoyltransacetylase component) EG10025 FUNCTION: THE PYRUVATE DEHYDROGENASE COMPLEX CATALYZES THE OVERALL CONVERSION OF PYRUVATE TO ACETYL-COA & CO(2). IT CONTAINS MULTIPLE COPIES OF THREE ENZYMATIC COMPONENTS: PYRUVATE DEHYDROGENASE (E1), DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2) & LIPOAMIDE DEHYDROGENASE (E3). CATALYTIC ACTIVITY: ACETYL-COA + DIHYDROLIPOAMIDE = COA + S-ACETYLDIHYDROLIPOAMIDE. COFACTOR: THE E2 COMPONENT CONTAINS THREE COVALENTLY-BOUND LIPOYL COFACTORS. SUBUNIT: FORMS A 24-POLYPEPTIDE STRUCTURAL CORE WITH OCTAHEDRAL SYMMETRY. SIMILARITY: BELONGS TO THE 2-OXOACID DEHYDROGENASE FAMILY. SIMILARITY: CONTAINS 3 LIPOYL-BINDING DOMAINS.
0.255136+mviNb1069putative virulence factor EG13880 SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL). SIMILARITY: BELONGS TO THE MVIN FAMILY.
0.245790+yjaAb4011orf, hypothetical protein EG11206
0.241873+yjdAb4109putative vimentin EG11210 FUNCTION: BELONGS TO AN OPERON INVOLVED IN ALKYLPHOSPHONATE UPTAKE AND C-P LYASE. EXACT FUNCTION NOT KNOWN. MISCELLANEOUS: THE SEQUENCE SHOWN IS THAT OF STRAIN K12.
yjcZb4110orf, hypothetical protein EG12460
0.228642-yagTb0286putative xanthine dehydrogenase (EC 1.1.1.20) EG13559 FUNCTION: YAGR, YAGS AND YAGT COULD BE THREE SUBUNITS OF A DEHYDROGENASE. SIMILARITY: TO THE N-TERMINAL OF VERTEBRATE XANTHINE DEHYDROGENASES. SIMILARITY: TO 2FE-2S FERREDOXINS IN THE N-TERMINAL DOMAIN.
yagSb0285orf, hypothetical protein EG13558 FUNCTION: YAGR, YAGS AND YAGT COULD BE THREE SUBUNITS OF A DEHYDROGENASE. SIMILARITY: TO R.PALUSTRIS 4-HYDROXYBENZOYL-COA REDUCTASE SUBUNIT HBAD.
yagRb0284orf, hypothetical protein EG13557 FUNCTION: YAGR, YAGS AND YAGT COULD BE THREE SUBUNITS OF A DEHYDROGENASE. SIMILARITY: TO VERTEBRATE XANTHINE DEHYDROGENASES AND TO R.PALUSTRIS 4-HYDROXYBENZOYL-COA REDUCTASE SUBUNIT HBAC.
yagQb0283orf, hypothetical protein EG13556
yagPb0282putative transcriptional regulator LYSR-type EG13555 SIMILARITY: SOME, TO E.COLI YAFC AND YGIP.
0.222548+deoDb4384purine-nucleoside phosphorylase EG10222 FUNCTION: CLEAVAGE OF GUANOSINE OR INOSINE TO RESPECTIVE BASES AND SUGAR-1-PHOSPHATE MOLECULES. CATALYTIC ACTIVITY: PURINE NUCLEOSIDE + ORTHOPHOSPHATE = PURINE + ALPHA-D-RIBOSE 1-PHOSPHATE. SUBUNIT: HOMOHEXAMER. SIMILARITY: BELONGS TO THE PNP/UDP FAMILY 1 OF PHOSPHORYLASES.