Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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P0A855 | TOLB_ECOLI | MKQALRVAFGFLILWASVLHAEVRIVIDSGVDSGRPIGVVPFQWAGPGAAPEDIGGIVAADLRNSGKFNPLDRARLPQQPGSAQEVQPAAWSALGIDAVVVGQVTPNPDGSYNVAYQLVDTGGAPGTVLAQNSYKVNKQWLRYAGHTASDEVFEKLTGIKGAFRTRIAYVVQTNGGQFPYELRVSDYDGYNQFVVHRSPQPLMSPAWSPDGSKLAYVTFESGRSALVIQTLANGAVRQVASFPRHNGAPAFSPDGSKLAFALSKTGSLNLYVMDLASGQIRQVTDGRSNNTEPTWFPDSQNLAFTSDQAGRPQVYKVNIN... | null | null | bacteriocin transport [GO:0043213]; cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to bacteriocin [GO:0071237]; protein import [GO:0017038]; protein transport [GO:0015031]; regulation of membrane invagination [GO:1905153] | cell division site [GO:0032153]; membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288]; periplasmic space [GO:0042597]; protein-containing complex [GO:0032991] | protein domain specific binding [GO:0019904]; protein-containing complex binding [GO:0044877] | PF07676;PF04052; | 2.120.10.30;3.40.50.10070; | TolB family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00671, ECO:0000269|PubMed:2687247, ECO:0000269|PubMed:7929011}. Note=Partially associated with the outer membrane through a specific interaction with Pal (PubMed:7744736). Accumulates at cell constriction sites. Recruitment to the division site is dependent on ... | null | null | null | null | null | FUNCTION: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity (PubMed:17233825). TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded component... | Escherichia coli (strain K12) |
P0A858 | TPIS_ECOLI | MRHPLVMGNWKLNGSRHMVHELVSNLRKELAGVAGCAVAIAPPEMYIDMAKREAEGSHIMLGAQNVDLNLSGAFTGETSAAMLKDIGAQYIIIGHSERRTYHKESDELIAKKFAVLKEQGLTPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEGAVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKVDANIAEQVIIQYGGSVNASNAAELFAQPDIDGALVGGASLKADAFAVIVKAAEAAKQA | 5.3.1.1 | null | gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096] | cytosol [GO:0005829]; membrane [GO:0016020] | identical protein binding [GO:0042802]; triose-phosphate isomerase activity [GO:0004807] | PF00121; | 3.20.20.70; | Triosephosphate isomerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:6092857, ECO:0000269|PubMed:9442062}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1030 uM for D-glyceraldehyde 3-phosphate (at 25 degrees Celsius) {ECO:0000269|PubMed:9442062}; Note=kcat is 54000 min(-1) for isomerase activity with D-glyceraldehyde 3-phosphate as substrate (at 25 degrees Celsius). {ECO:0000269|PubMed:9442062}; | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|HAMAP-Rule:MF_00147}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00147}. | null | null | FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:9442062}. | Escherichia coli (strain K12) |
P0A862 | TPX_ECOLI | MSQTVHFQGNPVTVANSIPQAGSKAQTFTLVAKDLSDVTLGQFAGKRKVLNIFPSIDTGVCAASVRKFNQLATEIDNTVVLCISADLPFAQSRFCGAEGLNNVITLSTFRNAEFLQAYGVAIADGPLKGLAARAVVVIDENDNVIFSQLVDEITTEPDYEAALAVLKA | 1.11.1.24 | null | cellular response to oxidative stress [GO:0034599] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; periplasmic space [GO:0042597] | hydroperoxide reductase activity [GO:0032843]; thioredoxin peroxidase activity [GO:0008379] | PF08534; | 3.40.30.10; | Peroxiredoxin family, Tpx subfamily | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:7499381}. Cytoplasm {ECO:0000269|PubMed:19054092}. Note=Forms a mixed disulfide with cytoplasmic thioredoxin (trx1). {ECO:0000269|PubMed:19054092}. | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000255|HAMAP-Ru... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1730 uM for H(2)O(2) {ECO:0000269|PubMed:12514184}; KM=9.1 uM for cumene hydroperoxide {ECO:0000269|PubMed:12514184}; KM=25.5 uM for Trx1 (using H(2)O(2) as substrate) {ECO:0000269|PubMed:12514184}; KM=22.5 uM for Trx1 (using cumene hydroperoxide as substrate) {ECO... | null | null | null | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Has a preference for alkyl hydroperoxides and acts as a lipid peroxidase to inhibit bac... | Escherichia coli (strain K12) |
P0A870 | TALB_ECOLI | MTDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLTIAPALLKELAESEGAIERKLSYTGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL | 2.2.1.2 | null | carbohydrate metabolic process [GO:0005975]; pentose-phosphate shunt, non-oxidative branch [GO:0009052] | cytosol [GO:0005829]; membrane [GO:0016020] | transaldolase activity [GO:0004801]; transketolase or transaldolase activity [GO:0016744] | PF00923; | 3.20.20.70; | Transaldolase family, Type 1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate; Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483, ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2; Evidence={ECO:0000269|PubMed:18687684, ECO:0000269|PubMed:7592346... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=38 uM for D,L-glyceraldehyde 3-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:7592346}; KM=90 uM for D-erythrose-4-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:7592346}; KM=... | PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8.5 and 9.5. {ECO:0000269|PubMed:7592346}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 15 and 40 degrees Celsius. At temperatures above 50 degrees Celsius, activity is lost rapidly, and at 55 degrees Celsius, the enzyme is totally inactivated. {ECO:0000269|PubMed:7592346}; | FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. {ECO:0000269|PubMed:18687684, ECO:0000269|PubMed:7592346}. | Escherichia coli (strain K12) |
P0A873 | TRMD_ECOLI | MWIGIISLFPEMFRAITDYGVTGRAVKNGLLSIQSWSPRDFTHDRHRTVDDRPYGGGPGMLMMVQPLRDAIHAAKAAAGEGAKVIYLSPQGRKLDQAGVSELATNQKLILVCGRYEGIDERVIQTEIDEEWSIGDYVLSGGELPAMTLIDSVSRFIPGVLGHEASATEDSFAEGLLDCPHYTRPEVLEGMEVPPVLLSGNHAEIRRWRLKQSLGRTWLRRPELLENLALTEEQARLLAEFKTEHAQQQHKHDGMA | 2.1.1.228 | null | tRNA methylation [GO:0030488]; tRNA N1-guanine methylation [GO:0002939] | cytosol [GO:0005829] | identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; tRNA (guanine(37)-N1)-methyltransferase activity [GO:0052906] | PF01746; | 3.40.1280.10;1.10.1270.20; | RNA methyltransferase TrmD family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.22... | null | null | null | null | FUNCTION: Specifically methylates guanosine-37 in various tRNAs. {ECO:0000269|PubMed:14583191}. | Escherichia coli (strain K12) |
P0A879 | TRPB_ECOLI | MTTLLNPYFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALTKCQNITAGTNTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGMFADFINETNVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGPQHAYLNSTG... | 4.2.1.20 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | aromatic amino acid family biosynthetic process [GO:0009073]; tryptophan biosynthetic process [GO:0000162] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; tryptophan synthase activity [GO:0004834] | PF00291; | 3.40.50.1100; | TrpB family | null | null | CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; | null | PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. | null | null | FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | Escherichia coli (strain K12) |
P0A884 | TYSY_ECOLI | MKQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRCHLRSIIHELLWFLQGDTNIAYLHENNVTIWDEWADENGDLGPVYGKQWRAWPTPDGRHIDQITTVLNQLKNDPDSRRIIVSAWNVGELDKMALAPCHAFFQFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFVWTGGDTHLYSNHMDQTHLQLSREPRPLPKLIIKRKPESIFDYRFEDFEIEGYDPHPGIKAPVAI | 2.1.1.45 | null | dTMP biosynthetic process [GO:0006231]; dTTP biosynthetic process [GO:0006235]; methylation [GO:0032259]; regulation of translation [GO:0006417]; response to radiation [GO:0009314] | cytosol [GO:0005829] | magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; thymidylate synthase activity [GO:0004799] | PF00303; | 3.30.572.10; | Thymidylate synthase family, Bacterial-type ThyA subfamily | PTM: Although not discussed in the published references, Met-1 is represented in the submitted PDB entries as being modified by either a formyl, or a carboxyl group. The N-terminal is probably N-(dihydroxymethyl)methionine, the hydrated form of N-formylmethionine. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00008}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000255|HAMAP-Rule:MF_00008, ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:3286637, ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for dUMP {ECO:0000269|PubMed:3286637}; KM=25 uM for 5,10-methylenetetrahydrofolate {ECO:0000269|PubMed:3286637}; KM=4.1 uM for dUMP {ECO:0000269|PubMed:9826509}; KM=13.6 uM for 5,10-methylenetetrahydrofolate {ECO:0000269|PubMed:9826509}; Vmax=5.47 umol/min/mg... | PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}. | null | null | FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product (PubMed:2223754, PubMed:3286637, Pub... | Escherichia coli (strain K12) |
P0A887 | UBIE_ECOLI | MVDKSQETTHFGFQTVAKEQKADMVAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRLVGETGKVVLADINESMLKMGREKLRNIGVIGNVEYVQANAEALPFPDNTFDCITISFGLRNVTDKDKALRSMYRVLKPGGRLLVLEFSKPIIEPLSKAYDAYSFHVLPRIGSLVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYKF | 2.1.1.163; 2.1.1.201 | null | aerobic respiration [GO:0009060]; menaquinone biosynthetic process [GO:0009234]; methylation [GO:0032259]; ubiquinone biosynthetic process [GO:0006744] | cytoplasm [GO:0005737]; ubiquinone biosynthesis complex [GO:0110142] | 2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity [GO:0008425]; demethylmenaquinone methyltransferase activity [GO:0043770]; methyltransferase activity [GO:0008168]; S-adenosylmethionine:2-demethylmenaquinol methyltransferase activity [GO:0102094]; S-adenosylmethionine:2-demethylmenaquinol-7 methyltran... | PF01209; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, MenG/UbiE family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30686758}. | CATALYTIC ACTIVITY: Reaction=a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42640, Rhea:RHEA-COMP:9539, Rhea:RHEA-COMP:9563, ChEBI:CHEBI:15378, ChEBI:CHEBI:18151, ChEBI:CHEBI:55437, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.163; Evidence={ECO:0000... | null | PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01813, ECO:0000269|PubMed:9045837}.; PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01813, ECO:0000269|PubMed:9045837}. | null | null | FUNCTION: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) (PubMed:9045837). In vitro, can use demethylphylloquinol, an intermediate in the bio... | Escherichia coli (strain K12) |
P0A890 | TUSA_ECOLI | MTDLFSSPDHTLDALGLRCPEPVMMVRKTVRNMQPGETLLIIADDPATTRDIPGFCTFMEHELVAKETDGLPYRYLIRKGG | null | null | L-cysteine catabolic process [GO:0019448]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; tRNA wobble position uridine thiolation [GO:0002143] | cytosol [GO:0005829]; IscS-TusA complex [GO:1990329] | sulfur carrier activity [GO:0097163] | PF01206; | 3.30.110.40; | Sulfur carrier protein TusA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00413, ECO:0000269|PubMed:10830496}. | null | null | PATHWAY: tRNA modification. {ECO:0000255|HAMAP-Rule:MF_00413, ECO:0000269|PubMed:16387657}. | null | null | FUNCTION: Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA (PubMed:16387657). Interacts with IscS and stimulates its cysteine de... | Escherichia coli (strain K12) |
P0A894 | RAPZ_ECOLI | MVLMIVSGRSGSGKSVALRALEDMGFYCVDNLPVVLLPDLARTLADREISAAVSIDVRNMPESPEIFEQAMSNLPDAFSPQLLFLDADRNTLIRRYSDTRRLHPLSSKNLSLESAIDKESDLLEPLRSRADLIVDTSEMSVHELAEMLRTRLLGKRERELTMVFESFGFKHGIPIDADYVFDVRFLPNPHWDPKLRPMTGLDKPVAAFLDRHTEVHNFIYQTRSYLELWLPMLETNNRSYLTVAIGCTGGKHRSVYIAEQLADYFRSRGKNVQSRHRTLEKRKP | null | null | protein homotetramerization [GO:0051289]; RNA destabilization [GO:0050779] | protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; carbohydrate derivative binding [GO:0097367]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; RNA binding [GO:0003723] | PF03668; | 3.40.50.300; | RapZ-like family, RapZ subfamily | null | null | null | null | null | null | null | FUNCTION: Modulates the synthesis of GlmS, by affecting the processing and stability of the regulatory small RNA GlmZ. When glucosamine-6-phosphate (GlcN6P) concentrations are high in the cell, RapZ binds GlmZ and targets it to cleavage by RNase E. Consequently, GlmZ is inactivated and unable to activate GlmS synthesis... | Escherichia coli (strain K12) |
P0A898 | YBEY_ECOLI | MSQVILDLQLACEDNSGLPEESQFQTWLNAVIPQFQEESEVTIRVVDTAESHSLNLTYRGKDKPTNVLSFPFEVPPGMEMSLLGDLVICRQVVEKEAQEQGKPLEAHWAHMVVHGSLHLLGYDHIEDDEAEEMEALETEIMLALGYEDPYIAEKE | 3.1.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00009}; Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00009}; | maturation of SSU-rRNA [GO:0030490]; response to heat [GO:0009408]; ribosomal small subunit biogenesis [GO:0042274]; ribosome biogenesis [GO:0042254]; rRNA processing [GO:0006364]; transcription antitermination [GO:0031564]; translation [GO:0006412] | cytoplasm [GO:0005737] | metalloendopeptidase activity [GO:0004222]; nickel cation binding [GO:0016151]; RNA endonuclease activity, producing 3'-phosphomonoesters [GO:0016892]; zinc ion binding [GO:0008270] | PF02130; | 3.40.390.30; | Endoribonuclease YbeY family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00009, ECO:0000269|PubMed:20639334}. | null | null | null | null | null | FUNCTION: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. Acts together with the RNase R to eliminate defective 70S ribosomes, but not properly matured 70S ribosomes or individual subunits, by a process mediated sp... | Escherichia coli (strain K12) |
P0A8D6 | YMDB_ECOLI | MKTRIHVVQGDITKLAVDVIVNAANPSLMGGGGVDGAIHRAAGPALLDACLKVRQQQGDCPTGHAVITLAGDLPAKAVVHTVGPVWRGGEQNEDQLLQDAYLNSLRLVAANSYTSVAFPAISTGVYGYPRAAAAEIAVKTVSEFITRHALPEQVYFVCYDEENAHLYERLLTQQGDE | 3.1.1.106 | null | purine nucleoside metabolic process [GO:0042278]; regulation of single-species biofilm formation on inanimate substrate [GO:1900231]; response to antibiotic [GO:0046677] | null | endoribonuclease inhibitor activity [GO:0060698]; enzyme binding [GO:0019899]; O-acetyl-ADP-ribose deacetylase activity [GO:0061463]; purine nucleoside binding [GO:0001883] | PF01661; | 3.40.220.10; | YmdB family | null | null | CATALYTIC ACTIVITY: Reaction=3''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose + H(+); Xref=Rhea:RHEA:59244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:142723; EC=3.1.1.106; Evidence={ECO:0000255|HAMAP-Rule:MF_01205, ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:264... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=270 uM for O-acetyl-ADP-ribose {ECO:0000269|PubMed:21257746}; KM=430 uM for O-acetyl-ADP-ribose {ECO:0000269|PubMed:26481419}; Note=kcat is 0.48 sec(-1) (PubMed:21257746). kcat is 1.31 sec(-1) (PubMed:26481419). {ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:2648... | null | null | null | FUNCTION: Deacetylates O-acetyl-ADP ribose to yield ADP-ribose and free acetate (PubMed:21257746, PubMed:26481419). Down-regulates ribonuclease 3 (RNase III) activity. Acts by interacting directly with the region of the ribonuclease that is required for dimerization/activation (PubMed:19141481). Overexpression inhibits... | Escherichia coli (strain K12) |
P0A8F0 | UPP_ECOLI | MKIVEVKHPLVKHKLGLMREQDISTKRFRELASEVGSLLTYEATADLETEKVTIEGWNGPVEIDQIKGKKITVVPILRAGLGMMDGVLENVPSARISVVGMYRNEETLEPVPYFQKLVSNIDERMALIVDPMLATGGSVIATIDLLKKAGCSSIKVLVLVAAPEGIAALEKAHPDVELYTASIDQGLNEHGYIIPGLGDAGDKIFGTK | 2.4.2.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.; | UMP salvage [GO:0044206]; uracil salvage [GO:0006223] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | GTP binding [GO:0005525]; guanosine tetraphosphate binding [GO:0097216]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; uracil phosphoribosyltransferase activity [GO:0004845] | PF14681; | 3.40.50.2020; | UPRTase family | null | null | CATALYTIC ACTIVITY: Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019, ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9; Evidence={ECO:0000269|PubMed:8856065}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.53 uM for uracil {ECO:0000269|PubMed:10079076}; KM=58 uM for 5-phospho-alpha-D-ribose 1-diphosphate {ECO:0000269|PubMed:10079076}; | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1. | null | null | FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | Escherichia coli (strain K12) |
P0A8F8 | UVRB_ECOLI | MSKPFKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPENAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKAMLERRDVVVVASVSAIYGLGDPDLYLKMMLHLTVGMIIDQRAILRRLAELQYARNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQIVSTIPRFTIYPKTHYVTPRERIVQAMEEIKEELAARRKVLLENNKLLEEQRLTQRTQFDLEMMNELGYCSGIENYSRFLSGRGPGE... | null | null | nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage recognition [GO:0000715]; nucleotide-excision repair, preincision complex assembly [GO:0006294]; response to radiation [GO:0009314]; SOS response [GO:0009432] | cytoplasm [GO:0005737]; excinuclease repair complex [GO:0009380] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; excinuclease ABC activity [GO:0009381]; identical protein binding [GO:0042802] | PF00271;PF04851;PF02151;PF12344;PF17757; | 3.40.50.300;4.10.860.10; | UvrB family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on... | Escherichia coli (strain K12) |
P0A8G0 | UVRC_ECOLI | MSDQFDAKAFLKTVTSQPGVYRMYDAGGTVIYVGKAKDLKKRLSSYFRSNLASRKTEALVAQIQQIDVTVTHTETEALLLEHNYIKLYQPRYNVLLRDDKSYPFIFLSGDTHPRLAMHRGAKHAKGEYFGPFPNGYAVRETLALLQKIFPIRQCENSVYRNRSRPCLQYQIGRCLGPCVEGLVSEEEYAQQVEYVRLFLSGKDDQVLTQLISRMETASQNLEFEEAARIRDQIQAVRRVTEKQFVSNTGDDLDVIGVAFDAGMACVHVLFIRQGKVLGSRSYFPKVPGGTELSEVVETFVGQFYLQGSQMRTLPGEILLD... | null | null | DNA damage response [GO:0006974]; nucleotide-excision repair [GO:0006289]; response to radiation [GO:0009314]; SOS response [GO:0009432] | cytoplasm [GO:0005737]; excinuclease repair complex [GO:0009380] | DNA binding [GO:0003677]; excinuclease ABC activity [GO:0009381] | PF01541;PF14520;PF02151;PF08459; | 1.10.150.20;3.40.1440.10;4.10.860.10;3.30.420.340; | UvrC family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: 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. {ECO:0000269|PubMed:10671556, ECO:0000269|PubMed:1387639}. | Escherichia coli (strain K12) |
P0A8G6 | NQOR_ECOLI | MAKVLVLYYSMYGHIETMARAVAEGASKVDGAEVVVKRVPETMPPQLFEKAGGKTQTAPVATPQELADYDAIIFGTPTRFGNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTGGGQEQTITSTWTTLAHHGMVIVPIGYAAQELFDVSQVRGGTPYGATTIAGGDGSRQPSQEELSIARYQGEYVAGLAVKLNG | 1.6.5.2 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_01017, ECO:0000269|PubMed:16672604, ECO:0000269|PubMed:9694845}; Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_01017, ECO:0000269|PubMed:16672604, ECO:0000269|PubMed:9694845}; | response to oxidative stress [GO:0006979] | cytosol [GO:0005829]; membrane [GO:0016020]; protein-containing complex [GO:0032991] | flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]; NADH dehydrogenase (quinone) activity [GO:0050136]; NADP binding [GO:0050661]; NADPH dehydrogenase (quinone) activity [GO:0... | PF03358; | 3.40.50.360; | WrbA family | null | null | CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01017, ECO:0000269|PubMed:16672604}; CATALYTIC ACTIVITY: Reaction=a quinone + H(... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.8 uM for benzoquinone {ECO:0000269|PubMed:16672604}; KM=14 uM for NADH {ECO:0000269|PubMed:16672604}; | null | null | null | FUNCTION: It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH. {EC... | Escherichia coli (strain K12) |
P0A8G9 | EX7S_ECOLI | MPKKNEAPASFEKALSELEQIVTRLESGDLPLEEALNEFERGVQLARQGQAKLQQAEQRVQILLSDNEDASLTPFTPDNE | 3.1.11.6 | COFACTOR: Note=Does not require a metal cofactor. {ECO:0000269|PubMed:4602029}; | DNA catabolic process [GO:0006308]; mismatch repair [GO:0006298] | cytosol [GO:0005829]; exodeoxyribonuclease VII complex [GO:0009318] | exodeoxyribonuclease VII activity [GO:0008855] | PF02609; | 1.10.287.1040; | XseB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00337, ECO:0000305|PubMed:6284744}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00337, ECO:0000269|PubMed:22718974, ECO:0000269|PubMed:4602029, ECO:0000269|PubMed:4602030}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8 to 7.9. {ECO:0000269|PubMed:4602029}; | null | FUNCTION: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. It can degrade 3' or 5' ss regions extending from the termini of duplex DNA molecules and displaced ss regions. It can also excise thymine dimers i... | Escherichia coli (strain K12) |
P0A8H3 | ZUPT_ECOLI | MSVPLILTILAGAATFIGAFLGVLGQKPSNRLLAFSLGFAAGIMLLISLMEMLPAALAAEGMSPVLGYGMFIFGLLGYFGLDRMLPHAHPQDLMQKSVQPLPKSIKRTAILLTLGISLHNFPEGIATFVTASSNLELGFGIALAVALHNIPEGLAVAGPVYAATGSKRTAILWAGISGLAEILGGVLAWLILGSMISPVVMAAIMAAVAGIMVALSVDELMPLAKEIDPNNNPSYGVLCGMSVMGFSLVLLQTAGIG | null | null | cobalt ion transport [GO:0006824]; iron ion import across plasma membrane [GO:0098711]; zinc ion import across plasma membrane [GO:0071578]; zinc ion transmembrane transport [GO:0071577]; zinc ion transport [GO:0006829] | membrane [GO:0016020]; plasma membrane [GO:0005886] | ferrous iron transmembrane transporter activity [GO:0015093]; metal ion binding [GO:0046872]; zinc ion transmembrane transporter activity [GO:0005385] | PF02535; | null | ZIP transporter (TC 2.A.5) family, ZupT subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00548, ECO:0000269|PubMed:20225068, ECO:0000269|PubMed:34793140}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00548}. | CATALYTIC ACTIVITY: Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351, ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00548, ECO:0000269|PubMed:11790762, ECO:0000269|PubMed:15716430, ECO:0000269|PubMed:20225068, ECO:0000269|PubMed:34793140}; CATALYTIC ACTIVITY: Reaction=Cd(2+)(in) = Cd(2+)(out); Xref=Rhea... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.71 uM for Zn(2+) {ECO:0000269|PubMed:20225068}; KM=1.3 uM for Zn(2+) {ECO:0000269|PubMed:34793140}; KM=7.2 uM for Cd(2+) {ECO:0000269|PubMed:34793140}; KM=0.91 uM for Co(2+) {ECO:0000269|PubMed:20225068}; KM=2.2 uM for Fe(2+) {ECO:0000269|PubMed:34793140}; KM=1.1... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is near neutral pH. {ECO:0000269|PubMed:20225068}; | null | FUNCTION: Mediates zinc uptake (PubMed:11790762, PubMed:15716430, PubMed:20225068, PubMed:34793140). Has broad metal specificity and can also mediate the uptake of cadmium, cobalt, iron, manganese and possibly copper (PubMed:11790762, PubMed:15716430, PubMed:20225068, PubMed:34793140). Has a slight preference for zinc ... | Escherichia coli (strain K12) |
P0A8H6 | YIHI_ECOLI | MKPSSSNSRSKGHAKARRKTREELDQEARDRKRQKKRRGHAPGSRAAGGNTTSGSKGQNAPKDPRIGSKTPIPLGVTEKVTKQHKPKSEKPMLSPQAELELLETDERLDALLERLEAGETLSAEEQSWVDAKLDRIDELMQKLGLSYDDDEEEEEDEKQEDMMRLLRGN | null | null | negative regulation of ribosome biogenesis [GO:0090071]; ribosome biogenesis [GO:0042254] | cytosol [GO:0005829] | GTPase activator activity [GO:0005096] | PF04220; | null | YihI family | null | null | null | null | null | null | null | FUNCTION: A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function, negatively regulating cell growth, probably via ribosome assembly. Stimulates the GTPase activity of Der; a construct missing the first 45 residues is even more stimulatory. Does not stimulate 2 other GTPases (ObgE and Era). Overexpress... | Escherichia coli (strain K12) |
P0A8I1 | YQGF_ECOLI | MSGTLLAFDFGTKSIGVAVGQRITGTARPLPAIKAQDGTPDWNIIERLLKEWQPDEIIVGLPLNMDGTEQPLTARARKFANRIHGRFGVEVKLHDERLSTVEARSGLFEQGGYRALNKGKVDSASAVIILESYFEQGY | 3.1.-.- | null | ribosome biogenesis [GO:0042254]; rRNA 5'-end processing [GO:0000967] | cytosol [GO:0005829] | 3'-5'-DNA exonuclease activity [GO:0008296] | PF03652; | 3.30.420.140; | YqgF nuclease family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00651}. | null | null | null | null | null | FUNCTION: Involved in the processing of the 5'-end of pre-16S rRNA during 70S ribosome maturation (processing does not occur on total cellular RNA off the ribosome); may be a nuclease (PubMed:25545592). A temperature-sensitive yqgF mutant no longer grows when Rho or NusA are overproduced, and has reduced transcription ... | Escherichia coli (strain K12) |
P0A8I5 | TRMB_ECOLI | MKNDVISPEFDENGRPLRRIRSFVRRQGRLTKGQEHALENYWPVMGVEFSEDMLDFPALFGREAPVTLEIGFGMGASLVAMAKDRPEQDFLGIEVHSPGVGACLASAHEEGLSNLRVMCHDAVEVLHKMIPDNSLRMVQLFFPDPWHKARHNKRRIVQVPFAELVKSKLQLGGVFHMATDWEPYAEHMLEVMSSIDGYKNLSESNDYVPRPASRPVTKFEQRGHRLGHGVWDLMFERVK | 2.1.1.33 | null | RNA (guanine-N7)-methylation [GO:0036265]; tRNA (guanine-N7)-methylation [GO:0106004]; tRNA methylation [GO:0030488] | tRNA methyltransferase complex [GO:0043527] | tRNA (guanine(46)-N7)-methyltransferase activity [GO:0008176] | PF02390; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, TrmB family | null | null | CATALYTIC ACTIVITY: Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000255|HA... | null | PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01057, ECO:0000305|PubMed:12730187}. | null | null | FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_01057, ECO:0000269|PubMed:12730187}. | Escherichia coli (strain K12) |
P0A8I8 | RLMH_ECOLI | MKLQLVAVGTKMPDWVQTGFTEYLRRFPKDMPFELIEIPAGKRGKNADIKRILDKEGEQMLAAAGKNRIVTLDIPGKPWDTPQLAAELERWKLDGRDVSLLIGGPEGLSPACKAAAEQSWSLSALTLPHPLVRVLVAESLYRAWSITTNHPYHRE | 2.1.1.177 | null | rRNA base methylation [GO:0070475]; rRNA methylation [GO:0031167] | cytoplasm [GO:0005737] | protein homodimerization activity [GO:0042803]; ribosome binding [GO:0043022]; rRNA (pseudouridine-N3-)-methyltransferase activity [GO:0070038] | PF02590; | 3.40.1280.10; | RNA methyltransferase RlmH family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00658, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42752, Rhea:RHEA-COMP:10221, Rhea:RHEA-COMP:10222, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65314, ChEBI:CHEB... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.51 uM for 70S ribosome {ECO:0000269|PubMed:20817755}; KM=0.3 uM for 70S ribosome {ECO:0000269|PubMed:28428565}; KM=27 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:20817755}; Note=kcat is 5-6 min(-1) (PubMed:20817755). kcat is 2.5 min(-1) (PubMed:28428565). ... | null | null | null | FUNCTION: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. Specific for fully assembled 70S ribosomes. {ECO:0000269|PubMed:18755835, ECO:0000269|PubMed:18755836, ECO:0000269|PubMed:20817755, ECO:0000269|PubMed:28428565}. | Escherichia coli (strain K12) |
P0A8J2 | DNAT_ECOLI | MSSRVLTPDVVGIDALVHDHQTVLAKAEGGVVAVFANNAPAFYAVTPARLAELLALEEKLARPGSDVALDDQLYQEPQAAPVAVPMGKFAMYPDWQPDADFIRLAALWGVALREPVTTEELASFIAYWQAEGKVFHHVQWQQKLARSLQIGRASNGGLPKRDVNTVSEPDSQIPPGFRG | null | null | DNA replication, synthesis of RNA primer [GO:0006269]; DNA unwinding involved in DNA replication [GO:0006268]; DNA-templated DNA replication [GO:0006261]; protein homotrimerization [GO:0070207]; replication fork processing [GO:0031297] | DnaB-DnaC-DnaT-PriA-PriB complex [GO:1990158]; DnaB-DnaC-DnaT-PriA-PriC complex [GO:1990159]; primosome complex [GO:1990077] | identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; single-stranded DNA binding [GO:0003697] | PF17948; | 1.10.8.1180; | DnaT family | null | null | null | null | null | null | null | FUNCTION: This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recog... | Escherichia coli (strain K12) |
P0A8J8 | RHLB_ECOLI | MSKTHLTEQKFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADRKVNQPRALIMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGL... | 3.6.4.13 | null | RNA catabolic process [GO:0006401]; RNA processing [GO:0006396] | bacterial degradosome [GO:1990061]; cytosol [GO:0005829]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; disordered domain specific binding [GO:0097718]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, RhlB subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00661, ECO:0000269|PubMed:18337249}. Note=Forms a cytoskeletal-like coiled structure that extends along the length of the cell. Formation of this structure does not require the presence of RNase E, MinD and/or MreB. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00661, ECO:0000269|PubMed:8610017, ECO:0000269|PubMed:9732274}; | null | null | null | null | FUNCTION: DEAD-box RNA helicase involved in RNA degradation. Has RNA-dependent ATPase activity and unwinds double-stranded RNA. {ECO:0000255|HAMAP-Rule:MF_00661, ECO:0000269|PubMed:12181321, ECO:0000269|PubMed:8610017, ECO:0000269|PubMed:9732274}. | Escherichia coli (strain K12) |
P0A8K1 | PSD_ECOLI | MLNSFKLSLQYILPKLWLTRLAGWGASKRAGWLTKLVIDLFVKYYKVDMKEAQKPDTASYRTFNEFFVRPLRDEVRPIDTDPNVLVMPADGVISQLGKIEEDKILQAKGHNYSLEALLAGNYLMADLFRNGTFVTTYLSPRDYHRVHMPCNGILREMIYVPGDLFSVNHLTAQNVPNLFARNERVICLFDTEFGPMAQILVGATIVGSIETVWAGTITPPREGIIKRWTWPAGENDGSVALLKGQEMGRFKLGSTVINLFAPGKVNLVEQLESLSVTKIGQPLAVSTETFVTPDAEPAPLPAEEIEAEHDASPLVDDKKD... | 4.1.1.65 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:3042771}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:3042771}; | phosphatidylethanolamine biosynthetic process [GO:0006646]; protein autoprocessing [GO:0016540]; zymogen activation [GO:0031638] | plasma membrane [GO:0005886] | phosphatidylserine decarboxylase activity [GO:0004609]; protein homodimerization activity [GO:0042803] | PF02666; | null | Phosphatidylserine decarboxylase family, PSD-B subfamily, Prokaryotic type I sub-subfamily | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:4598120}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:4598120}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:4598120}; | null | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:4598120}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:4598120}; | null | FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Only decarboxylates the lipid-linked form of the serine moiety, and not serine alone or derivatives like phosphoserine or glycerophosphoserine. {ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:4598120}. | Escherichia coli (strain K12) |
P0A8L1 | SYS_ECOLI | MLDPNLLRNEPDAVAEKLARRGFKLDVDKLGALEERRKVLQVKTENLQAERNSRSKSIGQAKARGEDIEPLRLEVNKLGEELDAAKAELDALQAEIRDIALTIPNLPADEVPVGKDENDNVEVSRWGTPREFDFEVRDHVTLGEMHSGLDFAAAVKLTGSRFVVMKGQIARMHRALSQFMLDLHTEQHGYSENYVPYLVNQDTLYGTGQLPKFAGDLFHTRPLEEEADTSNYALIPTAEVPLTNLVRGEIIDEDDLPIKMTAHTPCFRSEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMAALEEMTGHAEKVLQLLG... | 6.1.1.11 | null | selenocysteine biosynthetic process [GO:0016260]; seryl-tRNA aminoacylation [GO:0006434] | cytosol [GO:0005829] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; serine-tRNA ligase activity [GO:0004828] | PF02403;PF00587; | 1.10.287.40; | Class-II aminoacyl-tRNA synthetase family, Type-1 seryl-tRNA synthetase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; CATAL... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=64 uM for serine {ECO:0000269|PubMed:7537870, ECO:0000269|PubMed:8065908}; KM=0.068 uM for ATP {ECO:0000269|PubMed:7537870, ECO:0000269|PubMed:8065908}; | PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. | null | null | FUNCTION: Catalyzes the attachment of serine to tRNA(Ser) (PubMed:7537870). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). {ECO:0000269|PubMed:2963963, ECO:0000269|PubMed:7537870, ECO:0000269|PubMed:8065... | Escherichia coli (strain K12) |
P0A8M0 | SYN_ECOLI | MSVVPVADVLQGRVAVDSEVTVRGWVRTRRDSKAGISFLAVYDGSCFDPVQAVINNSLPNYNEDVLRLTTGCSVIVTGKVVASPGQGQQFEIQASKVEVAGWVEDPDTYPMAAKRHSIEYLREVAHLRPRTNLIGAVARVRHTLAQALHRFFNEQGFFWVSTPLITASDTEGAGEMFRVSTLDLENLPRNDQGKVDFDKDFFGKESFLTVSGQLNGETYACALSKIYTFGPTFRAENSNTSRHLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEERADDMKFFAERVDKDAVSRLERFIEADFAQVDYTDAVTIL... | 6.1.1.22 | null | asparaginyl-tRNA aminoacylation [GO:0006421]; tRNA aminoacylation for protein translation [GO:0006418] | cytoplasm [GO:0005737] | asparagine-tRNA ligase activity [GO:0004816]; ATP binding [GO:0005524]; nucleic acid binding [GO:0003676]; protein homodimerization activity [GO:0042803] | PF00152;PF01336; | 2.40.50.140; | Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659, Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442, ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=29 uM for asparagine {ECO:0000269|PubMed:1544480}; KM=15.3 uM for asparagine {ECO:0000269|PubMed:2009959}; KM=0.5 mM for ATP {ECO:0000269|PubMed:2009959}; | null | null | null | null | Escherichia coli (strain K12) |
P0A8M3 | SYT_ECOLI | MPVITLPDGSQRHYDHAVSPMDVALDIGPGLAKACIAGRVNGELVDACDLIENDAQLSIITAKDEEGLEIIRHSCAHLLGHAIKQLWPHTKMAIGPVIDNGFYYDVDLDRTLTQEDVEALEKRMHELAEKNYDVIKKKVSWHEARETFANRGESYKVSILDENIAHDDKPGLYFHEEYVDMCRGPHVPNMRFCHHFKLMKTAGAYWRGDSNNKMLQRIYGTAWADKKALNAYLQRLEEAAKRDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQEVKGPFMMDRVLWEKTGHWDNYKDAMFTT... | 6.1.1.3 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00184}; Note=Binds 1 zinc ion per subunit. It helps recognize and select the amino acid substrate, and thus has neither a purely catalytic or structural role (PubMed:10881191). {ECO:0000269|PubMed:10319817, ECO:0000269|PubMed:10881191, E... | negative regulation of translational initiation [GO:0045947]; regulation of translation [GO:0006417]; response to antibiotic [GO:0046677]; threonyl-tRNA aminoacylation [GO:0006435]; tRNA aminoacylation [GO:0043039]; tRNA aminoacylation for protein translation [GO:0006418] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | aminoacyl-tRNA editing activity [GO:0002161]; aminoacyl-tRNA ligase activity [GO:0004812]; ATP binding [GO:0005524]; mRNA 5'-UTR binding [GO:0048027]; mRNA regulatory element binding translation repressor activity [GO:0000900]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; threonine-tRNA lig... | PF03129;PF02824;PF00587;PF07973; | 3.10.20.30;3.30.54.20;3.40.50.800; | Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}. | CATALYTIC ACTIVITY: Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=94 uM for ATP {ECO:0000269|PubMed:15507440}; KM=110 uM for L-threonine activation {ECO:0000269|PubMed:10881191, ECO:0000269|PubMed:15507440}; KM=120 uM for L-threonine activation {ECO:0000269|PubMed:18997014}; KM=0.86 uM for L-threonine aminoacylation {ECO:0000269|... | null | null | null | FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (PubMed:10881191, PubMed:15079065, PubMed:18997014). The rate-limiting step is amino acid activation in the presence of tRNA (P... | Escherichia coli (strain K12) |
P0A8N0 | MATP_ECOLI | MKYQQLENLESGWKWKYLVKKHREGELITRYIEASAAQEAVDVLLSLENEPVLVNGWIDKHMNPELVNRMKQTIRARRKRHFNAEHQHTRKKSIDLEFIVWQRLAGLAQRRGKTLSETIVQLIEDAENKEKYANKMSSLKQDLQALLGKE | null | null | cell division [GO:0051301]; chromosome organization [GO:0051276]; chromosome segregation [GO:0007059]; protein homotetramerization [GO:0051289]; regulation of DNA-templated transcription [GO:0006355] | cytoplasm [GO:0005737]; DNA replication termination region [GO:0097047] | phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565] | PF06303;PF17414; | 1.20.1270.380;1.10.1220.10; | MatP family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01073, ECO:0000269|PubMed:18984159}. Note=Accumulates in the cell as a discrete focus that colocalizes with the Ter macrodomain. | null | null | null | null | null | FUNCTION: Required for spatial organization of the terminus region of the chromosome (Ter macrodomain) during the cell cycle. Prevents early segregation of duplicated Ter macrodomains during cell division. Binds specifically to matS, which is a 13 bp signature motif repeated within the Ter macrodomain. {ECO:0000255|HAM... | Escherichia coli (strain K12) |
P0A8N3 | SYK1_ECOLI | MSEQHAQGADAVVDLNNELKTRREKLANLREQGIAFPNDFRRDHTSDQLHAEFDGKENEELEALNIEVAVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDDLPEGVYNEQFKKWDLGDILGAKGKLFKTKTGELSIHCTELRLLTKALRPLPDKFHGLQDQEARYRQRYLDLISNDESRNTFKVRSQILSGIRQFMVNRGFMEVETPMMQVIPGGAAARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQDILGKTEVTYGDVTLDF... | 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; tRNA aminoacylation for protein translation [GO:0006418] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane [GO:0016020] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; ligase activity [GO:0016874]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; tRNA binding [GO:0000049] | PF00152;PF01336; | 2.40.50.140; | Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; | null | null | null | null | null | Escherichia coli (strain K12) |
P0A8N5 | SYK2_ECOLI | MSEQETRGANEAIDFNDELRNRREKLAALRQQGVAFPNDFRRDHTSDQLHEEFDAKDNQELESLNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVFDF... | 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 3 Mg(2+) ions per subunit. The third one is coordinated by ATP.; | cellular response to heat [GO:0034605]; diadenosine tetraphosphate biosynthetic process [GO:0015966]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; RNA capping [GO:0036260]; tRNA aminoacylation for protein translation [GO:0006418] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane [GO:0016020] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; ligase activity [GO:0016874]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; tRNA binding [GO:0000049] | PF00152;PF01336; | 2.40.50.140; | Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; | null | null | null | null | FUNCTION: Can also synthesize a number of adenyl dinucleotides (in particular AppppA). These dinucleotides have been proposed to act as modulators of the heat-shock response and stress response. | Escherichia coli (strain K12) |
P0A8N7 | EPMA_ECOLI | MSETASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLVPFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEMGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFLRYLEIDPLSADKTQLREVAAKLDLSNVADTEEDRDTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTEDHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHPIDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAF... | 6.3.1.- | null | cellular response to acidic pH [GO:0071468]; lysyl-tRNA aminoacylation [GO:0006430] | cytosol [GO:0005829] | acid-ammonia (or amide) ligase activity [GO:0016880]; ATP binding [GO:0005524]; lysine-tRNA ligase activity [GO:0004824]; protein homodimerization activity [GO:0042803]; protein-lysine lysyltransferase activity [GO:0052868]; tRNA binding [GO:0000049] | PF00152; | null | Class-II aminoacyl-tRNA synthetase family, EpmA subfamily | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=213 uM for (R)-beta-lysine {ECO:0000269|PubMed:21841797}; KM=8600 uM for L-alpha-lysine {ECO:0000269|PubMed:21841797}; KM=6950 uM for (S)-beta-lysine {ECO:0000269|PubMed:21841797}; KM=206 uM for ATP {ECO:0000269|PubMed:21841797}; Note=kcat is 36 min(-1) for the ami... | null | null | null | FUNCTION: With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the eps... | Escherichia coli (strain K12) |
P0A8P6 | XERC_ECOLI | MTDLHTDVERYLRYLSVERQLSPITLLNYQRQLEAIINFASENGLQSWQQCDVTMVRNFAVRSRRKGLGAASLALRLSALRSFFDWLVSQNELKANPAKGVSAPKAPRHLPKNIDVDDMNRLLDIDINDPLAVRDRAMLEVMYGAGLRLSELVGLDIKHLDLESGEVWVMGKGSKERRLPIGRNAVAWIEHWLDLRDLFGSEDDALFLSKLGKRISARNVQKRFAEWGIKQGLNNHVHPHKLRHSFATHMLESSGDLRGVQELLGHANLSTTQIYTHLDFQHLASVYDAAHPRAKRGK | null | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; DNA transposition [GO:0006313]; plasmid maintenance [GO:0006276]; plasmid recombination [GO:0042150]; resolution of DNA recombination intermediates [GO:0071139] | cytoplasm [GO:0005737]; Holliday junction resolvase complex [GO:0048476] | DNA binding [GO:0003677]; site-specific recombinase activity [GO:0009009]; tyrosine-based site-specific recombinase activity [GO:0009037] | PF02899;PF00589; | 1.10.150.130;1.10.443.10; | 'phage' integrase family, XerC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with DNA. | null | null | null | null | null | FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines ... | Escherichia coli (strain K12) |
P0A8P8 | XERD_ECOLI | MKQDLARIEQFLDALWLEKNLAENTLNAYRRDLSMMVEWLHHRGLTLATAQSDDLQALLAERLEGGYKATSSARLLSAVRRLFQYLYREKFREDDPSAHLASPKLPQRLPKDLSEAQVERLLQAPLIDQPLELRDKAMLEVLYATGLRVSELVGLTMSDISLRQGVVRVIGKGNKERLVPLGEEAVYWLETYLEHGRPWLLNGVSIDVLFPSQRAQQMTRQTFWHRIKHYAVLAGIDSEKLSPHVLRHAFATHLLNHGADLRVVQMLLGHSDLSTTQIYTHVATERLRQLHQQHHPRA | null | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; DNA transposition [GO:0006313]; plasmid maintenance [GO:0006276]; resolution of DNA recombination intermediates [GO:0071139]; response to radiation [GO:0009314] | cytoplasm [GO:0005737]; Holliday junction resolvase complex [GO:0048476] | DNA binding [GO:0003677]; site-specific recombinase activity [GO:0009009]; tyrosine-based site-specific recombinase activity [GO:0009037] | PF02899;PF00589; | 1.10.150.130;1.10.443.10; | 'phage' integrase family, XerD subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerC binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines ... | Escherichia coli (strain K12) |
P0A8Q0 | FRDC_ECOLI | MTTKRKPYVRPMTSTWWKKLPFYRFYMLREGTAVPAVWFSIELIFGLFALKNGPEAWAGFVDFLQNPVIVIINLITLAAALLHTKTWFELAPKAANIIVKDEKMGPEPIIKSLWAVTVVATIVILFVALYW | null | null | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; bacterial-type flagellum assembly [GO:0044780]; fermentation [GO:0006113] | membrane [GO:0016020]; plasma membrane [GO:0005886]; plasma membrane fumarate reductase complex [GO:0045284] | succinate dehydrogenase activity [GO:0000104] | PF02300; | 1.20.1300.10; | FrdC family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00708, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00708, ECO:0000269|PubMed:10373108}. | null | null | null | null | null | FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cel... | Escherichia coli (strain K12) |
P0A8Q3 | FRDD_ECOLI | MINPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGDALSYERVLAFAQSFIGRVFLFLMIVLPLWCGLHRMHHAMHDLKIHVPAGKWVFYGLAAILTVVTLIGVVTI | null | null | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; bacterial-type flagellum assembly [GO:0044780]; fermentation [GO:0006113]; fumarate metabolic process [GO:0006106] | membrane [GO:0016020]; plasma membrane [GO:0005886]; plasma membrane fumarate reductase complex [GO:0045284] | succinate dehydrogenase activity [GO:0000104] | PF02313; | 1.20.1300.10; | FrdD family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00709, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00709, ECO:0000269|PubMed:10373108}. | null | null | null | null | null | FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cel... | Escherichia coli (strain K12) |
P0A8R0 | RRAA_ECOLI | MKYDTSELCDIYQEDVNVVEPLFSNFGGRASFGGQIITVKCFEDNGLLYDLLEQNGRGRVLVVDGGGSVRRALVDAELARLAVQNEWEGLVIYGAVRQVDDLEELDIGIQAMAAIPVGAAGEGIGESDVRVNFGGVTFFSGDHLYADNTGIILSEDPLDIE | null | null | negative regulation of RNA catabolic process [GO:1902369]; protein homotrimerization [GO:0070207] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity [GO:0047443]; endoribonuclease inhibitor activity [GO:0060698]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; oxaloacetate decarboxylase activity [GO:0008948]; ribonuclease inhibitor activity [GO:0008428] | PF03737; | 3.50.30.40; | RraA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome. {ECO:0000269|PubMed:13678585, ECO:... | Escherichia coli (strain K12) |
P0A8S1 | ARGP_ECOLI | MKRPDYRTLQALDAVIRERGFERAAQKLCITQSAVSQRIKQLENMFGQPLLVRTVPPRPTEQGQKLLALLRQVELLEEEWLGDEQTGSTPLLLSLAVNADSLATWLLPALAPVLADSPIRLNLQVEDETRTQERLRRGEVVGAVSIQHQALPSCLVDKLGALDYLFVSSKPFAEKYFPNGVTRSALLKAPVVAFDHLDDMHQAFLQQNFDLPPGSVPCHIVNSSEAFVQLARQGTTCCMIPHLQIEKELASGELIDLTPGLFQRRMLYWHRFAPESRMMRKVTDALLDYGHKVLRQD | null | null | negative regulation of DNA-templated DNA replication initiation [GO:0032297]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355] | null | bent DNA binding [GO:0003681]; DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF00126;PF03466; | 3.40.190.290;1.10.10.10; | LysR transcriptional regulatory family | null | null | null | null | null | null | null | FUNCTION: Controls the transcription of genes involved in arginine and lysine metabolism. Activates transcription of several genes, including argO, lysP, lysC, asd, dapB, dapD, lysA, gdhA and argK. Acts by binding directly to their promoter or control region (PubMed:10600368, PubMed:15150242, PubMed:17504942, PubMed:21... | Escherichia coli (strain K12) |
P0A8S9 | FLHD_ECOLI | MHTSELLKHIYDINLSYLLLAQRLIVQDKASAMFRLGINEEMATTLAALTLPQMVKLAETNQLVCHFRFDSHQTITQLTQDSRVDDLQQIHTGIMLSTRLLNDVNQPEEALRKKRA | null | null | bacterial-type flagellum assembly [GO:0044780]; DNA-templated transcription [GO:0006351]; positive regulation of bacterial-type flagellum assembly [GO:1902210]; positive regulation of DNA-templated transcription [GO:0045893] | cytoplasm [GO:0005737]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677] | PF05247; | 1.10.4000.10; | FlhD family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the cl... | Escherichia coli (strain K12) |
P0A8T7 | RPOC_ECOLI | MKDLLKFLKAQTKTEEFDAIKIALASPDMIRSWSFGEVKKPETINYRTFKPERDGLFCARIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTQTKVRRERMGHIELASPTAHIWFLKSLPSRIGLLLDMPLRDIERVLYFESYVVIEGGMTNLERQQILTEEQYLDALEEFGDEFDAKMGAEAIQALLKSMDLEQECEQLREELNETNSETKRKKLTKRIKLLEAFVQSGNKPEWMILTVLPVLPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLDLAAPDIIVRNEKRMLQEAVDALLDNGRRGRAITGSN... | 2.7.7.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24843001, ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:24843001, ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY}; COFACTOR: Name=Zn(2... | bacterial-type flagellum assembly [GO:0044780]; bacterial-type flagellum-dependent cell motility [GO:0071973]; cell motility [GO:0048870]; cellular response to cell envelope stress [GO:0036460]; DNA-templated transcription initiation [GO:0006352]; intracellular iron ion homeostasis [GO:0006879]; nitrate assimilation [G... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic DNA-directed RNA polymerase complex [GO:0000345]; membrane [GO:0016020]; transcription elongation factor complex [GO:0008023] | DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; magnesium ion binding [GO:0000287]; zinc ion binding [GO:0008270] | PF04997;PF00623;PF04983;PF05000;PF04998; | 1.10.132.30;1.10.150.390;1.10.1790.20;1.10.40.90;2.40.40.20;2.40.50.100;4.10.860.120;1.10.274.100; | RNA polymerase beta' chain family | PTM: Acetylated on several lysine residues in the presence of glucose. {ECO:0000269|PubMed:18723842, ECO:0000269|PubMed:21696463}. | null | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01322}; | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. {ECO:0000255|HAMAP-Rule:MF_01322, ECO:0000269|PubMed:1646077, ECO:0000269|PubMed:24843001}.; FUNCTION: Resistance to the antibiotics salinamide A, salinamide B, rifampicin... | Escherichia coli (strain K12) |
P0A8V0 | RBN_ECOLI | MELIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSMSGIIQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEILDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQALKAAGVPPGPLFQELKAGKTITLEDGRQINGADYLAAPVPGKALAIFGDTGPCDAALDLAKGVDVMVHEATLDITMEAKANSRGHSSTRQAATLAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFTVFNV | 3.1.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12029081}; Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:12029081}; | tRNA processing [GO:0008033] | null | 3'-tRNA processing endoribonuclease activity [GO:0042781]; metal ion binding [GO:0046872]; nuclease activity [GO:0004518]; protein homodimerization activity [GO:0042803]; RNA endonuclease activity, producing 5'-phosphomonoesters [GO:0016891]; RNA exonuclease activity [GO:0004532]; RNA exonuclease activity, producing 5'... | PF12706; | 3.60.15.10; | RNase Z family, RNase BN subfamily | null | null | null | null | null | null | null | FUNCTION: Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities, depending on the nature of the substrate and of the added divalent cation, and on its 3'-terminal structure. Can process the 3' termini of both CCA-less and CCA-containing tRNA precursors. CCA-less tRNAs are cleaved endonu... | Escherichia coli (strain K12) |
P0A8V2 | RPOB_ECOLI | MVYSYTEKKRIRKDFGKRPQVLDVPYLLSIQLDSFQKFIEQDPEGQYGLEAAFRSVFPIQSYSGNSELQYVSYRLGEPVFDVQECQIRGVTYSAPLRVKLRLVIYEREAPEGTVKDIKEQEVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSSGKVLYNARIIPYRGSWLDFEFDPKDNLFVRIDRRRKLPATIILRALNYTTEQILDLFFEKVIFEIRDNKLQMELVPERLRGETASFDIEANGKVYVEKGRRITARHIRQLEKDDVKLIEVPVEYIAGKVVAKDYIDESTGELICAANMELSLD... | 2.7.7.6 | null | bacterial-type flagellum assembly [GO:0044780]; bacterial-type flagellum-dependent cell motility [GO:0071973]; cell motility [GO:0048870]; cellular response to cell envelope stress [GO:0036460]; DNA-templated transcription initiation [GO:0006352]; intracellular iron ion homeostasis [GO:0006879]; nitrate assimilation [G... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic DNA-directed RNA polymerase complex [GO:0000345]; membrane [GO:0016020]; transcription elongation factor complex [GO:0008023] | DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; ribonucleoside binding [GO:0032549] | PF04563;PF04561;PF04565;PF10385;PF00562;PF04560; | 2.40.50.100;2.40.50.150;3.90.1100.10;6.10.140.1670;2.30.150.10;2.40.270.10;3.90.1800.10;3.90.1110.10; | RNA polymerase beta chain family | PTM: Acetylated on several lysine residues in the presence of glucose. {ECO:0000269|PubMed:18723842, ECO:0000269|PubMed:21696463}. | null | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. {ECO:0000269|PubMed:1646077, ECO:0000269|PubMed:24843001}.; FUNCTION: Resistance to the antibiotics salinamide A, salinamide B, rifampicin, streptolydigin, CBR703, myxopyr... | Escherichia coli (strain K12) |
P0A8V6 | FADR_ECOLI | MVIKAQSPAGFAEEYIIESIWNNRFPPGTILPAERELSELIGVTRTTLREVLQRLARDGWLTIQHGKPTKVNNFWETSGLNILETLARLDHESVPQLIDNLLSVRTNISTIFIRTAFRQHPDKAQEVLATANEVADHADAFAELDYNIFRGLAFASGNPIYGLILNGMKGLYTRIGRHYFANPEARSLALGFYHKLSALCSEGAHDQVYETVRRYGHESGEIWHRMQKNLPGDLAIQGR | null | null | fatty acid metabolic process [GO:0006631]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fatty acid biosynthetic process [GO:0045723]; regulation of fatty acid metabolic process [GO:0019217] | cytosol [GO:0005829] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; fatty-acyl-CoA binding [GO:0000062]; protein homodimerization activity [GO:0042803] | PF07840;PF00392; | 1.20.120.530;1.10.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00696}. | null | null | null | null | null | FUNCTION: Multifunctional regulator of fatty acid metabolism (PubMed:11859088, PubMed:1569108, PubMed:19854834, PubMed:21276098, PubMed:8446033, PubMed:9388199). Represses transcription of at least eight genes required for fatty acid transport and beta-oxidation including fadA, fadB, fadD, fadL and fadE (PubMed:9388199... | Escherichia coli (strain K12) |
P0A8W0 | NANR_ECOLI | MGLMNAFDSQTEDSSPAIGRNLRSRPLARKKLSEMVEEELEQMIRRREFGEGEQLPSERELMAFFNVGRPSVREALAALKRKGLVQINNGERARVSRPSADTIIGELSGMAKDFLSHPGGIAHFEQLRLFFESSLVRYAAEHATDEQIDLLAKALEINSQSLDNNAAFIRSDVDFHRVLAEIPGNPIFMAIHVALLDWLIAARPTVTDQALHEHNNVSYQQHIAIVDAIRRHDPDEADRALQSHLNSVSATWHAFGQTTNKKK | null | null | DNA-templated transcription [GO:0006351]; negative regulation of DNA-templated transcription initiation [GO:2000143] | null | core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription repressor activity [GO:0001217]; protein homodimerization activity [GO:0042803] | PF07729;PF00392; | 1.20.120.530;1.10.10.10; | NanR family | null | null | null | null | null | null | null | FUNCTION: Transcriptional repressor that controls expression of the genes required for the catabolism of sialic acids (PubMed:12897000, PubMed:23935044, PubMed:9864311). Represses expression of the nanATEK-yhcH, nanCMS and yjhBC operons. Acts by binding directly to the Nan box, a region of approximately 30 bp covering ... | Escherichia coli (strain K12) |
P0A8Y1 | YJJG_ECOLI | MKWDWIFFDADETLFTFDSFTGLQRMFLDYSVTFTAEDFQDYQAVNKPLWVDYQNGAITSLQLQHGRFESWAERLNVEPGKLNEAFINAMAEICTPLPGAVSLLNAIRGNAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYALEQAGNPDRSRVLMVGDTAESDILGGINAGLATCWLNAHHREQPEGIAPTWTVSSLHELEQLLCKH | 3.1.3.5 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15489502}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15489502}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:15489502}; Note=Divalent metal cation. Highest activity with Mn(2+) followed by Mg(2+) and... | pyrimidine nucleobase salvage [GO:0043100]; response to xenobiotic stimulus [GO:0009410]; thymine metabolic process [GO:0019859] | cytoplasm [GO:0005737] | 5'-nucleotidase activity [GO:0008253]; manganese ion binding [GO:0030145]; nucleotide binding [GO:0000166]; phosphatase activity [GO:0016791]; thymidylate 5'-phosphatase activity [GO:0050340]; XMP 5'-nucleosidase activity [GO:0106411] | PF00702; | 3.40.50.1000; | HAD-like hydrolase superfamily, YjjG family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; Evidence={ECO:0000269|PubMed:15489502}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.51 mM for 5'-dTMP (in the presence of Mn(2+)) {ECO:0000269|PubMed:15489502}; KM=2.14 mM for 5'-dTMP (in the presence of 5 mM Mg(2+) and 0.5 mM Mn(2+)) {ECO:0000269|PubMed:17286574}; KM=0.66 mM for 5'-UMP (in the presence of Mn(2+)) {ECO:0000269|PubMed:15489502}; ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:15489502}; | null | FUNCTION: Nucleotidase that shows high phosphatase activity toward non-canonical pyrimidine nucleotides and three canonical nucleoside 5'-monophosphates (UMP, dUMP, and dTMP), and very low activity against TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6-phosphogluconate. Appears to function as a house-cleaning nucleotidase ... | Escherichia coli (strain K12) |
P0A8Y3 | YIHX_ECOLI | MLYIFDLGNVIVDIDFNRVLGAWSDLTRIPLASLKKSFHMGEAFHQHERGEISDEAFAEALCHEMALPLSYEQFSHGWQAVFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSDTVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKVLC | 3.1.3.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16990279}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16990279}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:16990279}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16990279}; No... | null | null | glucose-1-phosphatase activity [GO:0008877]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145] | PF00702; | 3.40.50.1000; | HAD-like hydrolase superfamily, YihX family | null | null | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate; Xref=Rhea:RHEA:19933, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=3.1.3.10; Evidence={ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:25484615}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.028 mM for imido-di-P (with magnesium ions as cofactor and at pH 9) {ECO:0000269|PubMed:16990279}; KM=0.24 mM for alpha-D-glucose-1-phosphate (with magnesium ions as cofactor and at pH 9) {ECO:0000269|PubMed:16990279}; KM=1.6 mM for alpha-fructose-1-phosphate (wi... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-7.0. {ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:25484615}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:25484615}; | FUNCTION: Catalyzes the dephosphorylation of alpha-D-glucose 1-phosphate (Glc1P) and, to a lesser extent, of other sugar phosphates (PubMed:16990279, PubMed:25484615). Has no activity with the beta form of Glc1P. In addition, YihX has significant phosphatase activity against pyridoxal phosphate (PLP) and low beta-phosp... | Escherichia coli (strain K12) |
P0A8Y5 | YIDA_ECOLI | MAIKLIAIDMDGTLLLPDHTISPAVKNAIAAARARGVNVVLTTGRPYAGVHNYLKELHMEQPGDYCITYNGALVQKAADGSTVAQTALSYDDYRFLEKLSREVGSHFHALDRTTLYTANRDISYYTVHESFVATIPLVFCEAEKMDPNTQFLKVMMIDEPAILDQAIARIPQEVKEKYTVLKSAPYFLEILDKRVNKGTGVKSLADVLGIKPEEIMAIGDQENDIAMIEYAGVGVAMDNAIPSVKEVANFVTKSNLEDGVAFAIEKYVLN | 3.1.3.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16990279}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16990279}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:16990279}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16990279}; No... | null | cytosol [GO:0005829] | magnesium ion binding [GO:0000287]; phosphatase activity [GO:0016791]; sugar-phosphatase activity [GO:0050308] | PF08282; | 3.30.1240.10;3.40.50.1000; | HAD-like hydrolase superfamily, Cof family | null | null | CATALYTIC ACTIVITY: Reaction=sugar phosphate + H2O = sugar + phosphate.; EC=3.1.3.23; Evidence={ECO:0000269|PubMed:16990279}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.019 mM for Ery4P (in the presence of magnesium ion as cofactor and at pH 9) {ECO:0000269|PubMed:16990279}; KM=0.033 mM for Imido-di-P (in the presence of magnesium ion as cofactor and at pH 9) {ECO:0000269|PubMed:16990279}; KM=0.21 mM for Glu1P (in the presence o... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6 and 7.5. {ECO:0000269|PubMed:16990279}; | null | FUNCTION: Catalyzes the dephosphorylation of different sugar phosphates including erythrose-4-phosphate (Ery4P), ribose-5-phosphate (Ribu5P), fructose-1-phosphate (Fru1P), fructose-6-phosphate (Fru6P), glucose-6-P (Glu6P), and also imidodiphosphate (Imido-di-P) and acetyl phosphate (Acetyl-P). Selectively hydrolyzes al... | Escherichia coli (strain K12) |
P0A8Y8 | ENTH_ECOLI | MIWKRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFMMTRDGQCVVGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVLG | 3.1.2.- | null | enterobactin biosynthetic process [GO:0009239] | cytosol [GO:0005829] | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity [GO:0061522]; acyl-CoA hydrolase activity [GO:0016289]; hydrolase activity, acting on ester bonds [GO:0016788]; identical protein binding [GO:0042802]; thiolester hydrolase activity [GO:0016790] | PF03061; | 3.10.129.10; | Thioesterase PaaI family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00907, ECO:0000269|PubMed:17675380}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for 2,3-DHB-EntB {ECO:0000269|PubMed:19119850}; KM=116 uM for 2,3-DHB-EntB {ECO:0000269|PubMed:19193103}; KM=21 uM for 4-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19119850}; KM=190 uM for 4-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103}; KM=25 uM for 2,4-DHB-E... | PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00907, ECO:0000269|PubMed:17675380}. | null | null | FUNCTION: Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs. {ECO:0000269|PubMe... | Escherichia coli (strain K12) |
P0A903 | BAMC_ECOLI | MAYSVQKSRLAKVAGVSLVLLLAACSSDSRYKRQVSGDEAYLEAAPLAELHAPAGMILPVTSGDYAIPVTNGSGAVGKALDIRPPAQPLALVSGARTQFTGDTASLLVENGRGNTLWPQVVSVLQAKNYTITQRDDAGQTLTTDWVQWNRLDEDEQYRGRYQISVKPQGYQQAVTVKLLNLEQAGKPVADAASMQRYSTEMMNVISAGLDKSATDAANAAQNRASTTMDVQSAADDTGLPMLVVRGPFNVVWQRLPAALEKVGMKVTDSTRSQGNMAVTYKPLSDSDWQELGASDPGLASGDYKLQVGDLDNRSSLQFID... | null | null | Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; protein insertion into membrane [GO:0051205] | Bam protein complex [GO:1990063]; cell surface [GO:0009986]; membrane [GO:0016020] | identical protein binding [GO:0042802] | PF06804; | 3.30.530.50;3.30.310.170; | BamC family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_00924, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00924, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:27686148}. | null | null | null | null | null | FUNCTION: Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. Efficient substrate folding and insertion int... | Escherichia coli (strain K12) |
P0A910 | OMPA_ECOLI | MKKTAIAIAVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFINNNGPTHENQLGAGAFGGYQVNPYVGFEMGYDWLGRMPYKGSVENGAYKAQGVQLTAKLGYPITDDLDIYTRLGGMVWRADTKSNVYGKNHDTGVSPVFAGGVEYAITPEIATRLEYQWTNNIGDAHTIGTRPDNGMLSLGVSYRFGQGEAAPVVAPAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGMGESNPVTGNTCDNVKQRAAL... | null | null | detection of virus [GO:0009597]; DNA damage response [GO:0006974]; monoatomic ion transport [GO:0006811]; symbiont entry into host cell [GO:0046718] | cell outer membrane [GO:0009279]; membrane [GO:0016020]; outer membrane [GO:0019867]; outer membrane protein complex [GO:0106234]; outer membrane-bounded periplasmic space [GO:0030288]; pore complex [GO:0046930] | identical protein binding [GO:0042802]; monoatomic ion transmembrane transporter activity [GO:0015075]; porin activity [GO:0015288] | PF00691;PF01389; | 2.40.160.20;3.30.1330.60; | Outer membrane OOP (TC 1.B.6) superfamily, OmpA family | PTM: Hydroxybutyrylation on Ser-184 and/or Ser-188 can add up to 10 R-3-hydroxybutyrate residues; it is not clear if one or both residues are modified in vivo. Hydrophobic residues adjacent to the modified Ser residues (i.e. Leu-183, Leu-185 and Val-187) are important for hydroxylation. Hydroxybutyrylation occurs in th... | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_00842, ECO:0000269|PubMed:10636850, ECO:0000269|PubMed:10947984, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229, ECO:0000269|PubMed:7813480, ECO:0000269|PubMed:791936, ECO:0000305|PubMed:9808047}; Multi-pass membrane protein {ECO:0000255|HAM... | null | null | null | null | null | FUNCTION: With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape (PubMed:11906175, PubMed:361695). Non-covalently binds peptidoglycan (Probable) ... | Escherichia coli (strain K12) |
P0A912 | PAL_ECOLI | MQLNKVLKGLMIALPVMAIAACSSNKNASNDGSEGMLGAGTGMDANGGNGNMSSEEQARLQMQQLQQNNIVYFDLDKYDIRSDFAQMLDAHANFLRSNPSYKVTVEGHADERGTPEYNISLGERRANAVKMYLQGKGVSADQISIVSYGKEKPAVLGHDEAAYSKNRRAVLVY | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; regulation of membrane invagination [GO:1905153] | cell division site [GO:0032153]; cell outer membrane [GO:0009279]; membrane [GO:0016020] | null | PF00691; | 3.30.1330.60; | Pal lipoprotein family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_02204, ECO:0000269|PubMed:1574003}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_02204, ECO:0000269|PubMed:1574003}. Note=Accumulates at cell constriction sites. Recruitment to the division site is dependent on FtsN activity. {ECO:0000269|PubMed:17233825}. | null | null | null | null | null | FUNCTION: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity (PubMed:11115123, PubMed:17233825). The Tol-Pal system is also required for polar localization of chemoreceptors clusters (PubMed:24720726). The system a... | Escherichia coli (strain K12) |
P0A921 | PA1_ECOLI | MRTLQGWLLPVFMLPMAVYAQEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYDTNYLIYTQTSDLNKEAIASYDWAENARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVGNTDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNWNTGYGGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF | 3.1.1.32; 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10537112}; Note=Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is bound by different amino acids with binding of each Ca(2+) shared with ligands coming from each monomer (Arg-167 and Ser-172 from 1 monomer, Ser-126 of the other)... | lipid catabolic process [GO:0016042]; phosphatidylglycerol metabolic process [GO:0046471] | cell outer membrane [GO:0009279] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; calcium ion binding [GO:0005509]; lysophospholipase activity [GO:0004622]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970]; phospholipase A2 activity [GO:0004623]; phospholipase activity [GO:0004620]; p... | PF02253; | 2.40.230.10; | Phospholipase A1 family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:6397463}; Multi-pass membrane protein {ECO:0000269|PubMed:6397463}. Note=One of the very few enzymes located there. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero... | null | null | null | null | FUNCTION: Has broad substrate specificity including hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads to outer membrane breakdown and cell death; is dormant in normal growing cells. Required for efficient secretion of bacteriocins... | Escherichia coli (strain K12) |
P0A924 | PGPB_ECOLI | MRSIARRTAVGAALLLVMPVAVWISGWRWQPGEQSWLLKAAFWVTETVTQPWGVITHLILFGWFLWCLRFRIKAAFVLFAILAAAILVGQGVKSWIKDKVQEPRPFVIWLEKTHHIPVDEFYTLKRAERGNLVKEQLAEEKNIPQYLRSHWQKETGFAFPSGHTMFAASWALLAVGLLWPRRRTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATWLAQRICGPLTPPAEENREIAQREQES | 3.1.3.27; 3.1.3.4; 3.6.1.27; 3.6.1.75 | null | glycerophospholipid biosynthetic process [GO:0046474]; peptidoglycan biosynthetic process [GO:0009252]; phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid catabolic process [GO:0009395] | cell outer membrane [GO:0009279]; plasma membrane [GO:0005886] | diacylglycerol diphosphate phosphatase activity [GO:0000810]; phosphatidate phosphatase activity [GO:0008195]; phosphatidylglycerophosphatase activity [GO:0008962]; undecaprenyl-diphosphatase activity [GO:0050380] | PF01569; | 1.20.144.10; | PA-phosphatase related phosphoesterase family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. Cell outer membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. | CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glyc... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=530 uM for undecaprenyl pyrophosphate {ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:8940025}; KM=96 uM for farnesyl pyrophosphate {ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:8940025}; KM=80 uM for diacylglycerol pyrophosphate {ECO:0000269|PubMed:18411271, E... | PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 for DGPP phosphatase activity and 6.5-7.5 for undecaprenyl pyrophosphate phosphatase activity. {ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:8940025}; | null | FUNCTION: Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate. Can also use lysop... | Escherichia coli (strain K12) |
P0A925 | PGPB_ECO57 | MRSIARRTAVGAALLLVMPVAVWISGWRWQPGEQSWLLKAAFWVTETVTQPWGVITHLILFGWFLWCLRFRIKAAFVLFAILAAAILVGQGVKSWIKDKVQEPRPFVIWLEKTHHIPVDEFYTLKRAERGNLVKEQLAEEKNIPQYLRSHWQKETGFAFPSGHTMFAASWALLAVGLLWPRRRTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATWLAQRICGPLTPPAEENREIAQREQES | 3.1.3.27; 3.1.3.4; 3.6.1.27; 3.6.1.75 | null | phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid catabolic process [GO:0009395] | cell outer membrane [GO:0009279]; plasma membrane [GO:0005886] | diacylglycerol diphosphate phosphatase activity [GO:0000810]; phosphatidate phosphatase activity [GO:0008195]; phosphatidylglycerophosphatase activity [GO:0008962]; undecaprenyl-diphosphatase activity [GO:0050380] | PF01569; | 1.20.144.10; | PA-phosphatase related phosphoesterase family | PTM: The N-terminus is blocked. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glyc... | null | PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2. | null | null | FUNCTION: Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate. Can also use lysop... | Escherichia coli O157:H7 |
P0A926 | PGPB_SHIFL | MRSIARRTAVGAALLLVMPVAVWISGWRWQPGEQSWLLKAAFWVTETVTQPWGVITHLILFGWFLWCLRFRIKAAFVLFAILAAAILVGQGVKSWIKDKVQEPRPFVIWLEKTHHIPVDEFYTLKRAERGNLVKEQLAEEKNIPQYLRSHWQKETGFAFPSGHTMFAASWALLAVGLLWPRRRTLTIAILLVWATGVMGSRLLLGMHWPRDLVVATLISWALVAVATWLAQRICGPLTPPAEENREIAQREQES | 3.1.3.27; 3.1.3.4; 3.6.1.27; 3.6.1.75 | null | phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid catabolic process [GO:0009395] | cell outer membrane [GO:0009279]; plasma membrane [GO:0005886] | diacylglycerol diphosphate phosphatase activity [GO:0000810]; phosphatidate phosphatase activity [GO:0008195]; phosphatidylglycerophosphatase activity [GO:0008962]; undecaprenyl-diphosphatase activity [GO:0050380] | PF01569; | 1.20.144.10; | PA-phosphatase related phosphoesterase family | PTM: The N-terminus is blocked. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glyc... | null | PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2. | null | null | FUNCTION: Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate. Can also use lysop... | Shigella flexneri |
P0A935 | MLTA_ECOLI | MKGRWVKYLLMGTVVAMLAACSSKPTDRGQQYKDGKFTQPFSLVNQPDAVGAPINAGDFAEQINHIRNSSPRLYGNQSNVYNAVQEWLRAGGDTRNMRQFGIDAWQMEGADNYGNVQFTGYYTPVIQARHTRQGEFQYPIYRMPPKRGRLPSRAEIYAGALSDKYILAYSNSLMDNFIMDVQGSGYIDFGDGSPLNFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHSEAEVRELLEQNPSFVFFKPQSFAPVKGASAVPLVGRASVASDRSIIPPGTTLLAEVPLLDNNGKFNGQYELRLMVALDVGG... | 4.2.2.n1 | null | cell wall organization [GO:0071555]; peptidoglycan catabolic process [GO:0009253]; peptidoglycan turnover [GO:0009254] | cell outer membrane [GO:0009279]; outer membrane-bounded periplasmic space [GO:0030288] | hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; lytic transglycosylase activity [GO:0008933] | PF06725;PF03562; | 2.40.240.50;2.40.40.10; | null | null | SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. | CATALYTIC ACTIVITY: Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the Mur... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0-4.5.; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Loses rapidly its activity at temperatures above 30 degrees Celsius.; | FUNCTION: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. | Escherichia coli (strain K12) |
P0A937 | BAME_ECOLI | MRCKTLTAAAAVLLMLTAGCSTLERVVYRPDINQGNYLTANDVSKIRVGMTQQQVAYALGTPLMSDPFGTNTWFYVFRQQPGHEGVTQQTLTLTFNSSGVLTNIDNKPALSGN | null | null | Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; protein insertion into membrane [GO:0051205]; response to antibiotic [GO:0046677] | Bam protein complex [GO:1990063]; membrane [GO:0016020] | identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674] | PF04355; | 3.30.1450.10; | BamE family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_00925, ECO:0000269|PubMed:17404237, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00925, ECO:0000269|PubMed:17404237, ECO:0000269|PubMed:27686148}. | null | null | null | null | null | FUNCTION: Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely... | Escherichia coli (strain K12) |
P0A940 | BAMA_ECOLI | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGDTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTIADIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAEIQQINIVGNHAFTTDELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYVTVNITEGDQYKLSGVEVSGNLAGHSAEIEQLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYP... | null | null | cell adhesion [GO:0007155]; Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; protein insertion into membrane [GO:0051205] | Bam protein complex [GO:1990063]; cell outer membrane [GO:0009279]; membrane [GO:0016020] | null | PF01103;PF07244; | 3.10.20.310;2.40.160.50; | BamA family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01430, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:23882017, ECO:0000269|PubMed:24619089, ECO:0000269|PubMed:24914988, ECO:0000269|PubMed:26901871, ECO:0000269|PubMed:9298646}. | null | null | null | null | null | FUNCTION: Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunit... | Escherichia coli (strain K12) |
P0A944 | RIMI_ECOLI | MNTISSLETTDLPAAYHIEQRAHAFPWSEKTFASNQGERYLNFQLTQNGKMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEATIRRNYYPTTDGREDAIIMALPISM | 2.3.1.-; 2.3.1.266 | null | protein modification process [GO:0036211] | cytoplasm [GO:0005737] | N-acetyltransferase activity [GO:0008080]; peptide-alanine-alpha-N-acetyltransferase activity [GO:0008999]; peptide-lysine-N-acetyltransferase activity [GO:0061733] | PF00583; | 3.40.630.30; | Acetyltransferase family, RimI subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]; Xref=Rhea:RHEA:43756, Rhea:RHEA-COMP:10676, Rhea:RHEA-COMP:10677, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718, ChEBI:CHEBI:83... | null | null | null | null | FUNCTION: Acetylates the N-terminal alanine of ribosomal protein bS18 (PubMed:2828880, PubMed:6991870). Also acts as a N-epsilon-lysine acetyltransferase that catalyzes acetylation of several proteins (PubMed:30352934). {ECO:0000269|PubMed:2828880, ECO:0000269|PubMed:30352934, ECO:0000269|PubMed:6991870}. | Escherichia coli (strain K12) |
P0A948 | RIMJ_ECOLI | MFGYRSNVPKVRLTTDRLVVRLVHDRDAWRLADYYAENRHFLKPWEPVRDESHCYPSGWQARLGMINEFHKQGSAFYFGLFDPDEKEIIGVANFSNVVRGSFHACYLGYSIGQKWQGKGLMFEALTAAIRYMQRTQHIHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVLTALTTPDWTPGR | 2.3.1.267 | null | maturation of SSU-rRNA [GO:0030490]; protein modification process [GO:0036211]; ribosome biogenesis [GO:0042254] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | N-acetyltransferase activity [GO:0008080]; peptide-alanine-alpha-N-acetyltransferase activity [GO:0008999]; peptide-serine-alpha-N-acetyltransferase activity [GO:1990189] | PF13302; | 3.40.630.30; | Acetyltransferase family, RimJ subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-alanyl-[ribosomal protein uS5] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein uS5]; Xref=Rhea:RHEA:43752, Rhea:RHEA-COMP:10672, Rhea:RHEA-COMP:10673, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718, ChEBI:CHEBI:8368... | null | null | null | null | FUNCTION: Acetylates the N-terminal alanine of ribosomal protein uS5 (PubMed:2828880, PubMed:385889). Also plays a role in maturation of the 30S ribosomal subunit (PubMed:18466225, PubMed:20176963). Plays a role in the temperature regulation of pap pilin transcription (PubMed:1356970). {ECO:0000269|PubMed:1356970, ECO:... | Escherichia coli (strain K12) |
P0A951 | ATDA_ECOLI | MPSAHSVKLRPLEREDLRYVHQLDNNASVMRYWFEEPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVEINHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFSVEGELMHEFFINGQYRNAIRMCIFQHQYLAEHKTPGQTLLKPTAQ | 2.3.1.57 | null | coenzyme A metabolic process [GO:0015936]; polyamine catabolic process [GO:0006598]; spermidine catabolic process [GO:0046203]; spermine catabolic process [GO:0046208] | diamine N-acetyltransferase complex [GO:1990235]; protein-containing complex [GO:0032991] | diamine N-acetyltransferase activity [GO:0004145]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287] | PF13302; | 3.40.630.30; | Acetyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an alkane-alpha,omega-diamine = an N-acetylalkane-alpha,omega-diamine + CoA + H(+); Xref=Rhea:RHEA:11116, Rhea:RHEA-COMP:9766, Rhea:RHEA-COMP:9767, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:70977, ChEBI:CHEBI:70988; EC=2.3.1.57; Evidence={ECO:0000269|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for AcCoA (in the presence of 3 mM spermidine at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:8077207}; KM=220 uM for spermine (in the presence of 10 uM AcCoA at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:8077207}; KM=183 uM for spermine {ECO:000... | PATHWAY: Amine and polyamine degradation; spermidine degradation. {ECO:0000305|PubMed:10986239, ECO:0000305|PubMed:7642535}.; PATHWAY: Amine and polyamine degradation; spermine degradation. {ECO:0000305|PubMed:10986239, ECO:0000305|PubMed:7642535}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: The level of spermidine acetyltransferase activity increases at low temperature to prevent spermidine toxicity. {ECO:0000269|PubMed:10986239}; | FUNCTION: Involved in the protection against polyamine toxicity by regulating their concentration (PubMed:10986239, PubMed:7642535). Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine to yield N(1)- and N(8)-acetylspermidine (PubMed:6297970, PubMed:7052085... | Escherichia coli (strain K12) |
P0A953 | FABB_ECOLI | MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSMEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAMRGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGTSTPVGDVKELAAIREVFGDK... | 2.3.1.41 | null | fatty acid biosynthetic process [GO:0006633]; monounsaturated fatty acid biosynthetic process [GO:1903966] | cytosol [GO:0005829] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315] | PF00109;PF02801; | 3.40.47.10; | Thiolase-like superfamily, Beta-ketoacyl-ACP synthases family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.5 uM for malonyl-[ACP] (in the presence of dodecanoyl-[ACP]) {ECO:0000269|PubMed:22017312}; KM=3.2 uM for dodecanoyl-[ACP] (in the presence of malonyl-[ACP]) {ECO:0000269|PubMed:22017312}; KM=153 uM for malonyl-CoA (in the presence of dodecanoyl-[ACP]) {ECO:0000... | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305|PubMed:19679654, ECO:0000305|PubMed:8910376}. | null | null | FUNCTION: Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor (PubMed:19679654, PubMed:22017312, PubMed:8910376, PubMed:9013860). Can also use unsaturated fatty acids (PubMed:19679654, PubMed:307637... | Escherichia coli (strain K12) |
P0A955 | ALKH_ECOLI | MKNWKTSAESILTTGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRTECAVDAIRAIAKEVPEAIVGAGTVLNPQQLAEVTEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMLGMDYGLKEFKFFPAEANGGVKALQAIAGPFSQVRFCPTGGISPANYRDYLALKSVLCIGGSWLVPADALEAGDYDRITKLAREAVEGAKL | 4.1.2.14; 4.1.3.16 | null | metabolic process [GO:0008152] | cytosol [GO:0005829]; membrane [GO:0016020] | (4S)-4-hydroxy-2-oxoglutarate aldolase activity [GO:0106009]; 2-dehydro-3-deoxy-phosphogluconate aldolase activity [GO:0008675]; 4-hydroxy-2-oxoglutarate aldolase activity [GO:0008700]; identical protein binding [GO:0042802]; oxaloacetate decarboxylase activity [GO:0008948]; oxo-acid-lyase activity [GO:0016833] | PF01081; | 3.20.20.70; | KHG/KDPG aldolase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate; Xref=Rhea:RHEA:35639, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655, ChEBI:CHEBI:71685; EC=4.1.3.16; Evidence={ECO:0000269|PubMed:17981470}; CATALYTIC ACTIVITY: Reaction=(4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate; Xref=Rhea:RHEA:30687... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for KDPG {ECO:0000269|PubMed:11342129, ECO:0000269|PubMed:17981470}; KM=9 mM for 2-oxobutyrate {ECO:0000269|PubMed:11342129, ECO:0000269|PubMed:17981470}; KM=10 mM for pyruvate {ECO:0000269|PubMed:11342129, ECO:0000269|PubMed:17981470}; Note=kcat is 80 sec(-... | PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate: step 2/2.; PATHWAY: Carbohydrate metabolism; glyoxylate and dicarboxylate metabolism. | null | null | FUNCTION: Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-Keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic al... | Escherichia coli (strain K12) |
P0A959 | ALAA_ECOLI | MSPIEKSSKLENVCYDIRGPVLKEAKRLEEEGNKVLKLNIGNPAPFGFDAPDEILVDVIRNLPTAQGYCDSKGLYSARKAIMQHYQARGMRDVTVEDIYIGNGVSELIVQAMQALLNSGDEMLVPAPDYPLWTAAVSLSSGKAVHYLCDESSDWFPDLDDIRAKITPRTRGIVIINPNNPTGAVYSKELLMEIVEIARQHNLIIFADEIYDKILYDDAEHHSIAPLAPDLLTITFNGLSKTYRVAGFRQGWMVLNGPKKHAKGYIEGLEMLASMRLCANVPAQHAIQTALGGYQSISEFITPGGRLYEQRNRAWELINDI... | 2.6.1.2 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:25014014, ECO:0000305|PubMed:20729367}; | alanine biosynthetic process [GO:0006523]; D-alanine biosynthetic process [GO:0030632]; DNA damage response [GO:0006974]; L-alanine biosynthetic process from pyruvate [GO:0019272]; response to antibiotic [GO:0046677] | cytoplasm [GO:0005737] | L-alanine:2-oxoglutarate aminotransferase activity [GO:0004021]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; transaminase activity [GO:0008483] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate; Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2; Evidence={ECO:0000269|PubMed:20729367}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19455; Evidence={ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.55 mM for pyruvate (at 37 degrees Celsius and pH 8.5) {ECO:0000269|PubMed:20729367}; KM=4.9 mM for alanine (at 37 degrees Celsius and pH 8.5) {ECO:0000269|PubMed:20729367}; | PATHWAY: Amino-acid biosynthesis; L-alanine biosynthesis. {ECO:0000269|PubMed:20729367}. | null | null | FUNCTION: Involved in the biosynthesis of alanine. Catalyzes the transamination of pyruvate by glutamate, leading to the formation of L-alanine and 2-oxoglutarate. Is also able to catalyze the reverse reaction. {ECO:0000269|PubMed:20729367}. | Escherichia coli (strain K12) |
P0A962 | ASPG1_ECOLI | MQKKSIYVAYTGGTIGMQRSEQGYIPVSGHLQRQLALMPEFHRPEMPDFTIHEYTPLMDSSDMTPEDWQHIAEDIKAHYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQNKAFLQELQEASDRGIVVVNLTQCMSGKVNMGGYATGNALAHAGVIGGADMTVEATLTKLHYLLSQELDTE... | 3.5.1.1 | null | asparagine catabolic process via L-aspartate [GO:0033345]; protein homotetramerization [GO:0051289] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | asparaginase activity [GO:0004067]; identical protein binding [GO:0042802] | PF00710;PF17763; | 3.40.50.40;3.40.50.1170; | Asparaginase 1 family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; Evidence={ECO:0000269|PubMed:17451745}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.5 mM for L-asparagine; | null | null | null | null | Escherichia coli (strain K12) |
P0A964 | CHEW_ECOLI | MTGMTNVTKLASEPSGQEFLVFTLGDEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVDLRIKFSQVDVDYNDNTVVIVLNLGQRVVGIVVDGVSDVLSLTAEQIRPAPEFAVTLSTEYLTGLGALGDRMLILVNIEKLLNSEEMALLDSAASEVA | null | null | aerotaxis [GO:0009454]; chemotaxis [GO:0006935]; establishment of localization in cell [GO:0051649]; positive regulation of post-translational protein modification [GO:1901875]; signal transduction [GO:0007165] | cell tip [GO:0051286]; cytosol [GO:0005829]; methyl accepting chemotaxis protein complex [GO:0098561]; plasma membrane [GO:0005886] | protein domain specific binding [GO:0019904] | PF01584; | 2.40.50.180;2.30.30.40; | null | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. It physically bridges CheA to the MCPs (methyl-accepting chemotaxis proteins) to allow regulated phosphotransfer to CheY and CheB. | Escherichia coli (strain K12) |
P0A968 | CSPD_ECOLI | MEKGTVKWFNNAKGFGFICPEGGGEDIFAHYSTIQMDGYRTLKAGQSVQFDVHQGPKGNHASVIVPVEVEAAVA | null | null | negative regulation of DNA replication [GO:0008156]; regulation of DNA-templated transcription [GO:0006355]; regulation of gene expression [GO:0010468]; response to starvation [GO:0042594] | cytosol [GO:0005829] | nucleic acid binding [GO:0003676]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]; toxin activity [GO:0090729] | PF00313; | 2.40.50.140; | null | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Inhibits DNA replication at both initiation and elongation steps, most probably by binding to the opened, single-stranded regions at replication forks. Plays a regulatory role in chromosomal replication in nutrient-depleted cells.; FUNCTION: Involved in persister cell formation, acting downstream of mRNA inte... | Escherichia coli (strain K12) |
P0A972 | CSPE_ECOLI | MSKIKGNVKWFNESKGFGFITPEDGSKDVFVHFSAIQTNGFKTLAEGQRVEFEITNGAKGPSAANVIAL | null | null | negative regulation of termination of DNA-templated transcription [GO:0060567]; regulation of gene expression [GO:0010468]; transcription antitermination [GO:0031564] | cytosol [GO:0005829] | nucleic acid binding [GO:0003676]; poly(A) binding [GO:0008143]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]; transcription antitermination factor activity, RNA binding [GO:0001072] | PF00313; | 6.20.370.130;2.40.50.140; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | null | Escherichia coli (strain K12) |
P0A988 | DPO3B_ECOLI | MKFTVEREHLLKPLQQVSGPLGGRPTLPILGNLLLQVADGTLSLTGTDLEMEMVARVALVQPHEPGATTVPARKFFDICRGLPEGAEIAVQLEGERMLVRSGRSRFSLSTLPAADFPNLDDWQSEVEFTLPQATMKRLIEATQFSMAHQDVRYYLNGMLFETEGEELRTVATDGHRLAVCSMPIGQSLPSHSVIVPRKGVIELMRMLDGGDNPLRVQIGSNNIRAHVGDFIFTSKLVDGRFPDYRRVLPKNPDKHLEAGCDLLKQAFARAAILSNEKFRGVRLYVSENQLKITANNPEQEEAEEILDVTYSGAEMEIGFN... | null | null | bacterial-type DNA replication [GO:0044787]; DNA damage response [GO:0006974]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA-templated DNA replication [GO:0006261]; error-prone translesion synthesis [GO:0042276]; negative regulation of DNA-templated DNA replication initiation [GO:0032297]; regulat... | cytosol [GO:0005829]; DNA polymerase III complex [GO:0009360]; Hda-beta clamp complex [GO:1990085]; replication inhibiting complex [GO:1990078]; replisome [GO:0030894] | 3'-5' exonuclease activity [GO:0008408]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF00712;PF02767;PF02768; | 3.10.150.10; | Beta sliding clamp family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23994470}. Note=Localizes to midcell position when chromosomes are condensed during DNA replication (PubMed:23994470). {ECO:0000269|PubMed:23994470}. | null | null | null | null | null | FUNCTION: Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA (PubMed:2040637). DNA bound in the ring is bent 22 deg... | Escherichia coli (strain K12) |
P0A991 | ALF1_ECOLI | MTDIAQLLGKDADNLLQHRCMTIPSDQLYLPGHDYVDRVMIDNNRPPAVLRNMQTLYNTGRLAGTGYLSILPVDQGVEHSAGASFAANPLYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSYPNTYDQTLYASVEQAFNMGAVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFKKDGVDYHVSADLTGQANHLAATIGADIVKQKMAENNGGYKAINYGYTDDRVYSKLTSENPIDLVRYQLANCYMGRAGLINSGGAAGGETDLSDAVRTAVINKRAGGMGLILG... | 4.1.2.13 | null | glycolytic process [GO:0006096] | cytosol [GO:0005829]; membrane [GO:0016020] | fructose-bisphosphate aldolase activity [GO:0004332]; identical protein binding [GO:0042802] | PF01791; | 3.20.20.70; | DeoC/FbaB aldolase family, FbaB subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:9531482}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730; Eviden... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for FBP {ECO:0000269|PubMed:9531482}; | null | null | null | FUNCTION: Catalyzes the reversible aldol condensation/cleavage reaction between glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP) to yield fructose-bisphosphate (FBP). {ECO:0000269|PubMed:9531482}. | Escherichia coli (strain K12) |
P0A993 | F16PA_ECOLI | MKTLGEFIVEKQHEFSHATGELTALLSAIKLGAKIIHRDINKAGLVDILGASGAENVQGEVQQKLDLFANEKLKAALKARDIVAGIASEEEDEIVVFEGCEHAKYVVLMDPLDGSSNIDVNVSVGTIFSIYRRVTPVGTPVTEEDFLQPGNKQVAAGYVVYGSSTMLVYTTGCGVHAFTYDPSLGVFCLCQERMRFPEKGKTYSINEGNYIKFPNGVKKYIKFCQEEDKSTNRPYTSRYIGSLVADFHRNLLKGGIYLYPSTASHPDGKLRLLYECNPMAFLAEQAGGKASDGKERILDIIPETLHQRRSFFVGNDHMVE... | 3.1.3.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000269|PubMed:16670087, ECO:0000269|PubMed:17567577}; Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000269|PubMed:16670087, ECO:0000269|PubMed:17567577}; | fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; sucrose biosynthetic process [GO:0005986] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; protein-containing complex [GO:0032991] | fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; nucleotide binding [GO:0000166] | PF00316;PF18913; | 3.40.190.80;3.30.540.10; | FBPase class 1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000269|PubMed:16670087, ECO:0000269|PubMed:6327623... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.7 uM for fructose 1,6-biphosphate {ECO:0000269|PubMed:16670087}; | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|HAMAP-Rule:MF_01855}. | null | null | null | Escherichia coli (strain K12) |
P0A998 | FTNA_ECOLI | MLKPEMIEKLNEQMNLELYSSLLYQQMSAWCSYHTFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESPFAEYSSLDELFQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQWYVSEQHEEEKLFKSIIDKLSLAGKSGEGLYFIDKELSTLDTQN | 1.16.3.2 | null | cellular response to iron ion [GO:0071281]; DNA damage response [GO:0006974]; intracellular sequestering of iron ion [GO:0006880]; iron ion transport [GO:0006826]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; ferroxidase activity [GO:0004322]; identical protein binding [GO:0042802] | PF00210; | 1.20.1260.10; | Ferritin family, Prokaryotic subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide; Xref=Rhea:RHEA:11972, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:78619; EC=1.16.3.2; Evidence={ECO:0000269|PubMed:24380371}; | null | null | null | null | FUNCTION: Iron-storage protein. {ECO:0000269|PubMed:11254384}. | Escherichia coli (strain K12) |
P0A9A6 | FTSZ_ECOLI | MFEPMELTNDAVIKVIGVGGGGGNAVEHMVRERIEGVEFFAVNTDAQALRKTAVGQTIQIGSGITKGLGAGANPEVGRNAADEDRDALRAALEGADMVFIAAGMGGGTGTGAAPVVAEVAKDLGILTVAVVTKPFNFEGKKRMAFAEQGITELSKHVDSLITIPNDKLLKVLGRGISLLDAFGAANDVLKGAVQGIAELITRPGLMNVDFADVRTVMSEMGYAMMGSGVASGEDRAEEAAEMAISSPLLEDIDLSGARGVLVNITAGFDLRLDEFETVGNTIRAFASDNATVVIGTSLDPDMNDELRVTVVATGIGMDKR... | null | null | cell division [GO:0051301]; chloroplast fission [GO:0010020]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093]; protein polymerization [GO:0051258] | cell division site [GO:0032153]; cytoplasm [GO:0005737]; divisome complex [GO:1990586]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802] | PF12327;PF00091; | 3.30.1330.20;3.40.50.1440; | FtsZ family | PTM: (Microbial infection) ADP-ribosylated on Arg-174 and sometimes Arg-338 by Tre1 when infected by S.proteamaculans strain 568. This prevents the formation of Z rings, inhibiting cell division, leading to cell elongation and disadvantaging E.coli over S.proteamaculans during competition for nutrients. In vitro it can... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:1944597, ECO:0000269|PubMed:8917533}. Note=Assembles in a ring-like structure at midcell at the inner surface of the cytoplasmic membrane. {ECO:0000269|PubMed:14731269, ECO:0000269|PubMed:1944597, ECO:0000269|PubMed:30343895, ECO:00002... | null | null | null | null | null | FUNCTION: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produc... | Escherichia coli (strain K12) |
P0A9A9 | FUR_ECOLI | MTDNNTALKKAGLKVTLPRLKILEVLQEPDNHHVSAEDLYKRLIDMGEEIGLATVYRVLNQFDDAGIVTRHNFEGGKSVFELTQQHHHDHLICLDCGKVIEFSDDSIEARQREIAAKHGIRLTNHSLYLYGHCAEGDCREDEHAHEGK | null | null | negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of siderophore biosynthetic process [GO:1900705]; positive regulation of DNA-templated transcription [GO:0045893] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity [GO:0001217]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270] | PF01475; | 3.30.1490.190;1.10.10.10; | Fur family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. Regulates the expression of several outer-membrane proteins including the iron transport operon. {ECO:0000269|PubMed:2823881}. | Escherichia coli (strain K12) |
P0A9B2 | G3P1_ECOLI | MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN... | 1.2.1.12 | null | glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096] | cytosol [GO:0005829]; membrane [GO:0016020] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NADP binding [GO:0050661] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000269|PubMed:2659073}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 uM for BPG {ECO:0000269|PubMed:2659073}; KM=42 uM for NAD {ECO:0000269|PubMed:2659073}; KM=1500 uM for G3P {ECO:0000269|PubMed:2659073}; Note=kcat is 1056 sec(-1) for dehydrogenase activity.; | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester,... | Escherichia coli (strain K12) |
P0A9B6 | E4PD_ECOLI | MTVRVAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHERSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNQDQLRAEHRIVSNASCTTNCIIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEW... | 1.2.1.72 | null | glucose metabolic process [GO:0006006]; pyridoxal phosphate biosynthetic process [GO:0042823]; pyridoxine biosynthetic process [GO:0008615] | cytosol [GO:0005829] | erythrose-4-phosphate dehydrogenase activity [GO:0048001]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family, Epd subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + NAD(+) = 4-phospho-D-erythronate + 2 H(+) + NADH; Xref=Rhea:RHEA:12056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16897, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58766; EC=1.2.1.72; Evidence={ECO:0000269|PubMed:7751290}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=74 uM for NAD (at 37 degrees Celsius and pH 8.6) {ECO:0000269|PubMed:7751290, ECO:0000269|PubMed:9182530}; KM=510 uM for D-erythrose 4-phosphate (at 25 degrees Celsius and pH 8.9) {ECO:0000269|PubMed:7751290, ECO:0000269|PubMed:9182530}; KM=960 uM for D-erythrose 4... | PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 1/5. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 8.6. {ECO:0000269|PubMed:7751290, ECO:0000269|PubMed:9182530}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius at pH 8.6. Relatively thermostable. Activity begins to decrease significantly when E4PDH is incubated at 50 degrees Celsius for 5 minutes. {ECO:0000269|PubMed:7751290, ECO:0000269|PubMed:9182530}; | FUNCTION: Catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate. {ECO:0000269|PubMed:9182530, ECO:0000269|PubMed:9696782}. | Escherichia coli (strain K12) |
P0A9C0 | GLPA_ECOLI | MKTRDSQSSDVIIIGGGATGAGIARDCALRGLRVILVERHDIATGATGRNHGLLHSGARYAVTDAESARECISENQILKRIARHCVEPTNGLFITLPEDDLSFQATFIRACEEAGISAEAIDPQQARIIEPAVNPALIGAVKVPDGTVDPFRLTAANMLDAKEHGAVILTAHEVTGLIREGATVCGVRVRNHLTGETQALHAPVVVNAAGIWGQHIAEYADLRIRMFPAKGSLLIMDHRINQHVINRCRKPSDADILVPGDTISLIGTTSLRIDYNEIDDNRVTAEEVDILLREGEKLAPVMAKTRILRAYSGVRPLVAS... | 1.1.5.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; | anaerobic respiration [GO:0009061]; glycerol catabolic process [GO:0019563]; glycerol-3-phosphate catabolic process [GO:0046168] | cytosol [GO:0005829]; glycerol-3-phosphate dehydrogenase complex [GO:0009331]; plasma membrane [GO:0005886] | flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; glycerol-3-phosphate dehydrogenase (quinone) activity [GO:0004368] | PF01266;PF04324; | 1.10.10.1100;3.50.50.60; | FAD-dependent glycerol-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. Note=Loosely bound to the cytoplasmic membrane often occurring in vesicles associated with fumarate reductase. | CATALYTIC ACTIVITY: Reaction=a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3; | null | PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1. | null | null | FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor. | Escherichia coli (strain K12) |
P0A9C5 | GLN1B_ECOLI | MSAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFDGSSIGGWKGINESDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGYDRDPRSIAKRAEDYLRSTGIADTVLFGPEPEFFLFDDIRFGSSISGSHVAIDDIEGAWNSSTQYEGGNKGHRPAVKGGYFPVPPVDSAQDIRSEMCLVMEQMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFGKTATFMPKPMFGDNGSGMHCHMSLSKNGVNLFAGDKYAGLSEQALYYIGGVIKHAKAINALANPTTNSY... | 6.3.1.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P9WN39}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P9WN39}; | ammonia assimilation cycle [GO:0019676]; glutamine biosynthetic process [GO:0006542]; nitrogen utilization [GO:0019740]; response to radiation [GO:0009314] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF00120;PF03951; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000250|UniProtKB:P0A1P6}; | null | null | null | null | FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. {ECO:0000250|UniProtKB:P0A1P6}. | Escherichia coli (strain K12) |
P0A9C9 | GLPX_ECOLI | MRRELAIEFSRVTESAALAGYKWLGRGDKNTADGAAVNAMRIMLNQVNIDGTIVIGEGEIDEAPMLYIGEKVGTGRGDAVDIAVDPIEGTRMTAMGQANALAVLAVGDKGCFLNAPDMYMEKLIVGPGAKGTIDLNLPLADNLRNVAAALGKPLSELTVTILAKPRHDAVIAEMQQLGVRVFAIPDGDVAASILTCMPDSEVDVLYGIGGAPEGVVSAAVIRALDGDMNGRLLARHDVKGDNEENRRIGEQELARCKAMGIEAGKVLRLGDMARSDNVIFSATGITKGDLLEGISRKGNIATTETLLIRGKSRTIRRIQS... | 3.1.3.11 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594}; Note=Manganese. Mg(2+), Co(2+), Ni(2+), Ca(2+), Cu(2+) and Zn(2+) cannot support activity. {ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594}; | fructose 1,6-bisphosphate metabolic process [GO:0030388]; gluconeogenesis [GO:0006094]; glycerol metabolic process [GO:0006071] | cytosol [GO:0005829] | fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; manganese ion binding [GO:0030145]; protein homodimerization activity [GO:0042803] | PF03320; | 3.40.190.90;3.30.540.10; | FBPase class 2 family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=35 uM for fructose 1,6-bisphosphate (at pH 7.7 and room temperature) {ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594}; KM=70 uM for fructose 1,6-bisphosphate (at pH 9.0 and 37 degrees Celsius) {ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594}; KM... | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8. {ECO:0000269|PubMed:19073594}; | null | FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Is likely to be involved in gluconeogenesis during growth on glycerol. Also displays a low activity toward glucose 1,6-bisphosphate, and no activity against ribulose 1,5-bisphosphate, fructose 2,6-bisphosphate, or fructose 1-phosph... | Escherichia coli (strain K12) |
P0A9D2 | GSTA_ECOLI | MKLFYKPGACSLASHITLRESGKDFTLVSVDLMKKRLENGDDYFAVNPKGQVPALLLDDGTLLTEGVAIMQYLADSVPDRQLLAPVNSISRYKTIEWLNYIATELHKGFTPLFRPDTPEEYKPTVRAQLEKKLQYVNEALKDEHWICGQRFTIADAYLFTVLRWAYAVKLNLEGLEHIAAFMQRMAERPEVQDALSAEGLK | 2.5.1.18 | null | response to hydrogen peroxide [GO:0042542] | cytoplasm [GO:0005737] | glutathione transferase activity [GO:0004364]; protein homodimerization activity [GO:0042803] | PF00043;PF13409; | 1.20.1050.10;3.40.30.10; | GST superfamily, Beta family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:77... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.041 mM for glutathione {ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}; KM=0.3 mM for glutathione {ECO:0000269|PubMed:18778244, ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}; KM=0.99 mM for 1-chloro-2,4-dinitrobenze... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:2185038, ECO:0000269|PubMed:7798255}; | FUNCTION: Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfid... | Escherichia coli (strain K12) |
P0A9D8 | DAPD_ECOLI | MQQLQNIIETAFERRAEITPANADTVTREAVNQVIALLDSGALRVAEKIDGQWVTHQWLKKAVLLSFRINDNQVIEGAESRYFDKVPMKFADYDEARFQKEGFRVVPPAAVRQGAFIARNTVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYIGQSTRIYDRETGEIHYGRVPAGSVVVSGNLPSKDGKYSLYCAVIVKKVDAKTRGKVGINELLRTID | 2.3.1.117 | null | diaminopimelate biosynthetic process [GO:0019877]; lysine biosynthetic process [GO:0009085]; lysine biosynthetic process via diaminopimelate [GO:0009089] | cytosol [GO:0005829] | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity [GO:0008666]; nucleotidyltransferase activity [GO:0016779] | PF14602;PF14805; | 2.160.10.10;1.10.166.10; | Transferase hexapeptide repeat family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA; Xref=Rhea:RHEA:17325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117; Evidence={ECO:0000269|PubMed:6365916}; PhysiologicalDire... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 uM for succinyl-CoA (at pH 7.4) {ECO:0000269|PubMed:6365916}; KM=22 uM for tetrahydrodipicolinate (THDPA) (at pH 7.4) {ECO:0000269|PubMed:6365916}; Note=kcat is 2600 min(-1). {ECO:0000269|PubMed:6365916}; | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. {ECO:0000305|PubMed:6365916}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2. {ECO:0000269|PubMed:6365916}; | null | FUNCTION: Catalyzes the formation of N-succinyl-2-amino-6-oxo-L-pimelate from succinyl-CoA and tetrahydrodipicolinate, a key step in lysine biosynthesis via diaminopimelate pathway. {ECO:0000269|PubMed:6365916}. | Escherichia coli (strain K12) |
P0A9E0 | ARAC_ECOLI | MAEAQNDPLLPGYSFNAHLVAGLTPIEANGYLDFFIDRPLGMKGYILNLTIRGQGVVKNQGREFVCRPGDILLFPPGEIHHYGRHPEAREWYHQWVYFRPRAYWHEWLNWPSIFANTGFFRPDEAHQPHFSDLFGQIINAGQGEGRYSELLAINLLEQLLLRRMEAINESLHPPMDNRVREACQYISDHLADSNFDIASVAQHVCLSPSRLSHLFRQQLGISVLSWREDQRISQAKLLLSTTRMPIATVGRNVGFDDQLYFSRVFKKCTGASPSEFRAGCEEKVNDVAVKLS | null | null | arabinose catabolic process [GO:0019568] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | DNA-binding transcription repressor activity [GO:0001217]; identical protein binding [GO:0042802]; transcription cis-regulatory region binding [GO:0000976] | PF02311;PF12833; | 1.10.10.60;2.60.120.280; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcription factor that regulates the expression of several genes involved in the transport and metabolism of L-arabinose (PubMed:1447222, PubMed:2231717, PubMed:2962192, PubMed:328165, PubMed:4362626, PubMed:6251457, PubMed:6319708). Functions both as a positive and a negative regulator (PubMed:328165, Pub... | Escherichia coli (strain K12) |
P0A9E5 | FNR_ECOLI | MIPEKRIIRRIQSGGCAIHCQDCSISQLCIPFTLNEHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAIGSGHHPSFAQALETSMVCEIPFETLDDLSGKMPNLRQQMMRLMSGEIKGDQDMILLLSKKNAEERLAAFIYNLSRRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLAVKGKYITIENNDALAQLAGHTRNVA | null | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster per subunit.; | anaerobic respiration [GO:0009061]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]; response to nitric oxide [GO:0071731] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | 4 iron, 4 sulfur cluster binding [GO:0051539]; DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity [GO:0003700]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; transcription cis-regulatory region binding [GO:0000976] | PF00027;PF13545; | 2.60.120.10;1.10.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Global transcription factor that controls the expression of over 100 target genes in response to anoxia. It facilitates the adaptation to anaerobic growth conditions by regulating the expression of gene products that are involved in anaerobic energy metabolism. When the terminal electron acceptor, O(2), is no... | Escherichia coli (strain K12) |
P0A9G4 | CUER_ECOLI | MNISDVAKITGLTSKAIRFYEEKGLVTPPMRSENGYRTYTQQHLNELTLLRQARQVGFNLEESGELVNLFNDPQRHSADVKRRTLEKVAEIERHIEELQSMRDQLLALANACPGDDSADCPIIENLSGCCHHRAG | null | null | DNA-templated transcription [GO:0006351]; positive regulation of DNA-templated transcription [GO:0045893] | cytoplasm [GO:0005737]; protein-DNA complex [GO:0032993] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; copper ion binding [GO:0005507]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; transcription cis-regulatory region binding [GO:0000976] | PF13411; | 1.10.1660.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations. {ECO:0000269|PubMed:10915804, ECO:0000269|PubMed:11167016, ECO:0000269|PubMed:11399769}. | Escherichia coli (strain K12) |
P0A9G6 | ACEA_ECOLI | MKTRTQQIEELQKEWTQPRWEGITRPYSAEDVVKLRGSVNPECTLAQLGAAKMWRLLHGESKKGYINSLGALTGGQALQQAKAGIEAVYLSGWQVAADANLAASMYPDQSLYPANSVPAVVERINNTFRRADQIQWSAGIEPGDPRYVDYFLPIVADAEAGFGGVLNAFELMKAMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAIQKLVAARLAADVTGVPTLLVARTDADAADLITSDCDPYDSEFITGERTSEGFFRTHAGIEQAISRGLAYAPYADLVWCETSTPDLELARRFAQAIHAKYPGKLLAYNCSP... | 4.1.3.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:3291954}; Note=Divalent metal cations. Can also use Mn(2+) ion. {ECO:0000269|PubMed:3291954}; | glyoxylate cycle [GO:0006097]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; glyoxysome [GO:0009514] | cation binding [GO:0043169]; isocitrate lyase activity [GO:0004451]; metal ion binding [GO:0046872] | PF00463; | 3.20.20.60; | Isocitrate lyase/PEP mutase superfamily, Isocitrate lyase family | null | null | CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate = glyoxylate + succinate; Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031, ChEBI:CHEBI:36655; EC=4.1.3.1; Evidence={ECO:0000269|PubMed:3281659, ECO:0000269|PubMed:7826335, ECO:0000269|Ref.9}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.076 uM for threo-D-isocitrate (at pH 7.3) {ECO:0000269|PubMed:7826335}; KM=8 uM for threo-D-isocitrate (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|Ref.9}; KM=32 uM for isocitrate (at pH 6.8) {ECO:0000269|PubMed:3281659}; KM=63 uM for isocitrate (at pH 7.3) {E... | PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2. {ECO:0000305|PubMed:15748982}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.3. {ECO:0000269|Ref.9}; | null | FUNCTION: Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substr... | Escherichia coli (strain K12) |
P0A9G8 | MODE_ECOLI | MQAEILLTLKLQQKLFADPRRISLLKHIALSGSISQGAKDAGISYKSAWDAINEMNQLSEHILVERATGGKGGGGAVLTRYGQRLIQLYDLLAQIQQKAFDVLSDDDALPLNSLLAAISRFSLQTSARNQWFGTITARDHDDVQQHVDVLLADGKTRLKVAITAQSGARLGLDEGKEVLILLKAPWVGITQDEAVAQNADNQLPGIISHIERGAEQCEVLMALPDGQTLCATVPVNEATSLQQGQNVTAYFNADSVIIATLC | null | null | molybdate ion transport [GO:0015689]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of DNA-templated transcription initiation [GO:2000143]; positive regulation of DNA-templated transcription [GO:0045893] | cytosol [GO:0005829]; ModE complex [GO:1990198] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; molybdenum ion binding [GO:0030151] | PF03459; | 2.40.50.100;1.10.10.10; | ModE family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9210473}. | null | null | null | null | null | FUNCTION: Functions as an intracellular molybdate sensor. The ModE-Mo complex acts as a repressor of the modABC operon, which is involved in the transport of molybdate (PubMed:8550508). Binds modA promoter DNA in the absence of molybdate, however molybdate binding confers increased DNA affinity (PubMed:9044285, PubMed:... | Escherichia coli (strain K12) |
P0A9H3 | LDCI_ECOLI | MNVIAILNHMGVYFKEEPIRELHRALERLNFQIVYPNDRDDLLKLIENNARLCGVIFDWDKYNLELCEEISKMNENLPLYAFANTYSTLDVSLNDLRLQISFFEYALGAAEDIANKIKQTTDEYINTILPPLTKALFKYVREGKYTFCTPGHMGGTAFQKSPVGSLFYDFFGPNTMKSDISISVSELGSLLDHSGPHKEAEQYIARVFNADRSYMVTNGTSTANKIVGMYSAPAGSTILIDRNCHKSLTHLMMMSDVTPIYFRPTRNAYGILGGIPQSEFQHATIAKRVKETPNATWPVHAVITNSTYDGLLYNTDFIKK... | 4.1.1.18 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | arginine catabolic process [GO:0006527]; lysine catabolic process [GO:0006554] | cytosol [GO:0005829] | arginine decarboxylase activity [GO:0008792]; guanosine tetraphosphate binding [GO:0097216]; identical protein binding [GO:0042802]; lysine decarboxylase activity [GO:0008923]; pyridoxal phosphate binding [GO:0030170] | PF01276;PF03711;PF03709; | 3.40.50.2300;3.90.1150.10;3.90.100.10;3.40.640.10; | Orn/Lys/Arg decarboxylase class-I family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-lysine = cadaverine + CO2; Xref=Rhea:RHEA:22352, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:58384; EC=4.1.1.18; Evidence={ECO:0000269|PubMed:4590109}; | null | null | null | null | FUNCTION: Inducible lysine decarboxylase that catalyzes the proton-dependent decarboxylation of L-lysine to produce the polyamine cadaverine and carbon dioxide (PubMed:4590109). Plays a role in pH homeostasis by consuming protons and neutralizing the acidic by-products of carbohydrate fermentation (PubMed:17209032). {E... | Escherichia coli (strain K12) |
P0A9H7 | CFA_ECOLI | MSSSCIEEVSVPDDNWYRIANELLSRAGIAINGSAPADIRVKNPDFFKRVLQEGSLGLGESYMDGWWECDRLDMFFSKVLRAGLENQLPHHFKDTLRIAGARLFNLQSKKRAWIVGKEHYDLGNDLFSRMLDPFMQYSCAYWKDADNLESAQQAKLKMICEKLQLKPGMRVLDIGCGWGGLAHYMASNYDVSVVGVTISAEQQKMAQERCEGLDVTILLQDYRDLNDQFDRIVSVGMFEHVGPKNYDTYFAVVDRNLKPEGIFLLHTIGSKKTDLNVDPWINKYIFPNGCLPSVRQIAQSSEPHFVMEDWHNFGADYDTT... | 2.1.1.79 | null | fatty acid biosynthetic process [GO:0006633]; lipid modification [GO:0030258]; methylation [GO:0032259] | cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | bicarbonate binding [GO:0071890]; cyclopropane-fatty-acyl-phospholipid synthase activity [GO:0008825]; protein homodimerization activity [GO:0042803] | PF02353; | 3.40.50.150; | CFA/CMAS family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.... | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. | null | null | FUNCTION: Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge. {ECO:0000250}. | Escherichia coli (strain K12) |
P0A9H9 | CHEZ_ECOLI | MMQPSIKPADEHSAGDIIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLYYVVQMTAQAAERALNSVEASQPHQDQMEKSAKALTQRWDDWFADPIDLADARELVTDTRQFLADVPAHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQESRPKRENQSLLNGPQVDTSKAGVVASQDQVDDLLDSLGF | 3.1.3.- | null | bacterial-type flagellum-dependent swarming motility [GO:0071978]; chemotaxis [GO:0006935]; regulation of bacterial-type flagellum-dependent cell motility [GO:1902021]; regulation of chemotaxis [GO:0050920] | bacterial-type flagellum [GO:0009288]; cytosol [GO:0005829]; methyl accepting chemotaxis protein complex [GO:0098561]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; phosphoprotein phosphatase activity [GO:0004721] | PF04344; | 1.10.287.500;1.20.5.590; | CheZ family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12644507}. Note=Colocalizes with CheA chemoreceptor patches near the cell poles, which requires CheA(short). | null | null | null | null | null | FUNCTION: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). {ECO:0000269|PubMed:10852888, ECO:0000269|PubMed:8820640}. | Escherichia coli (strain K12) |
P0A9J0 | RNG_ECOLI | MTAELLVNVTPSETRVAYIDGGILQEIHIEREARRGIVGNIYKGRVSRVLPGMQAAFVDIGLDKAAFLHASDIMPHTECVAGEEQKQFTVRDISELVRQGQDLMVQVVKDPLGTKGARLTTDITLPSRYLVFMPGASHVGVSQRIESESERERLKKVVAEYCDEQGGFIIRTAAEGVGEAELASDAAYLKRVWTKVMERKKRPQTRYQLYGELALAQRVLRDFADAELDRIRVDSRLTYEALLEFTSEYIPEMTSKLEHYTGRQPIFDLFDVENEIQRALERKVELKSGGYLIIDQTEAMTTVDINTGAFVGHRNLDDTI... | 3.1.26.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P21513}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P21513}; | cell cycle [GO:0007049]; cell division [GO:0051301]; maturation of SSU-rRNA [GO:0030490]; rRNA processing [GO:0006364]; tRNA processing [GO:0008033] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886] | endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; ribonuclease G activity [GO:0008996]; RNA nuclease activity [GO:0004540]; rRNA binding [GO:0019843]; tRNA binding [GO:0000049] | PF10150;PF20833;PF00575; | 2.40.50.140;3.40.1260.20; | RNase E/G family, RNase G subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22509045, ECO:0000305|PubMed:14622423}. Cell inner membrane {ECO:0000269|PubMed:22509045}; Peripheral membrane protein {ECO:0000305|PubMed:22509045}. Cytoplasm, cytoskeleton {ECO:0000303|PubMed:8300545}. Note=Possible cytoskeletal location is upon overproduction. {ECO... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 uM for 5'-phosphorylated 14 base fluorogenic substrate {ECO:0000269|PubMed:15197283}; KM=0.33 uM for 5'-OH 14 base fluorogenic substrate {ECO:0000269|PubMed:15197283}; KM=0.12 uM for 5'-phosphorylated 13 base fluorogenic substrate {ECO:0000269|PubMed:18078441}... | null | null | null | FUNCTION: An endonuclease that acts in the processing of the 5'-end of precursors of 16S rRNA, generates a precursor with 3 extra nucleotides at its 5'-end (which is matured by Rnm) (PubMed:10329633, PubMed:10362534, PubMed:10722715, PubMed:20176963, PubMed:24489121, PubMed:26694614, PubMed:32343306). It prefers 5'-mon... | Escherichia coli (strain K12) |
P0A9J4 | PANE_ECOLI | MKITVLGCGALGQLWLTALCKQGHEVQGWLRVPQPYCSVNLVETDGSIFNESLTANDPDFLATSDLLLVTLKAWQVSDAVKSLASTLPVTTPILLIHNGMGTIEELQNIQQPLLMGTTTHAARRDGNVIIHVANGITHIGPARQQDGDYSYLADILQTVLPDVAWHNNIRAELWRKLAVNCVINPLTAIWNCPNGELRHHPQEIMQICEEVAAVIEREGHHTSAEDLRDYVMQVIDATAENISSMLQDIRALRHTEIDYINGFLLRRARAHGIAVPENTRLFEMVKRKESEYERIGTGLPRPW | 1.1.1.169 | null | pantothenate biosynthetic process [GO:0015940] | cytoplasm [GO:0005737] | 2-dehydropantoate 2-reductase activity [GO:0008677]; NADP binding [GO:0050661] | PF02558;PF08546; | 3.40.50.720; | Ketopantoate reductase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH; Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.169; Evidence={ECO:0000269|PubMed:10736170, ECO:0000269|PubMed:11123955}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 uM for ketopantoate {ECO:0000269|PubMed:11724562, ECO:0000269|PubMed:17229734}; KM=120 uM for ketopantoate {ECO:0000269|PubMed:10736170, ECO:0000269|PubMed:11123955}; KM=7.3 uM for NADPH {ECO:0000269|PubMed:11724562, ECO:0000269|PubMed:17229734}; KM=4 uM for NAD... | PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2. {ECO:0000305|PubMed:10736170}. | null | null | FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. {ECO:0000269|PubMed:10736170, ECO:0000269|PubMed:11123955}. | Escherichia coli (strain K12) |
P0A9J6 | RBSK_ECOLI | MQNAGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNIDITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPALVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIVALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGFRVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAAIAVTRKGAQPSVPWREEIDAFLDRQR | 2.7.1.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:16784868, ECO:0000305|PubMed:11786021}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16784868}; Note=Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst t... | D-ribose catabolic process [GO:0019303] | cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; ribokinase activity [GO:0004747] | PF00294; | 3.40.1190.20; | Carbohydrate kinase PfkB family, Ribokinase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+); Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216; EC=2.7.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:11563694, ECO:0000269|PubMed:16784868, ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.213 mM for ATP {ECO:0000269|PubMed:16784868}; KM=0.279 mM for D-ribose {ECO:0000269|PubMed:16784868}; KM=1.41 mM for 2-deoxy-D-ribose {ECO:0000269|PubMed:16784868}; KM=32 mM for D-arabinose {ECO:0000269|PubMed:16784868}; KM=31.6 mM for D-xylose {ECO:0000269|PubMe... | PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:3011794}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:16784868}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-50 degrees Celsius. {ECO:0000269|PubMed:16784868}; | FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:... | Escherichia coli (strain K12) |
P0A9J8 | CMPDT_ECOLI | MTSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVLTQQALLQQHLNKINPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRYPHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLYGLQVLERIEANQRQNFTRFVVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRN... | 4.2.1.51; 5.4.99.5 | null | chorismate metabolic process [GO:0046417]; L-phenylalanine biosynthetic process [GO:0009094]; tyrosine biosynthetic process [GO:0006571] | cytoplasm [GO:0005737] | arogenate dehydratase activity [GO:0047769]; chorismate mutase activity [GO:0004106]; prephenate dehydratase activity [GO:0004664]; protein homodimerization activity [GO:0042803] | PF01817;PF00800; | 3.30.70.260;1.20.59.10;3.40.190.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000269|PubMed:4261395}; CATALYTIC ACTIVITY: Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O; Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:165... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=45 uM for chorismate (at pH 7.8 and at 37 degrees Celsius) {ECO:0000269|PubMed:4261395}; KM=1 mM for prephenate (at pH 7.8 and at 37 degrees Celsius) {ECO:0000269|PubMed:4261395}; KM=147 uM for chorismate (at pH 4.9) {ECO:0000269|Ref.8}; KM=296 uM for chorismate (a... | PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1. {ECO:0000305}.; PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.3 for chorismate mutase activity. {ECO:0000269|PubMed:4261395}; | null | FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. {ECO:0000269|PubMed:4261395}. | Escherichia coli (strain K12) |
P0A9K7 | PHOU_ECOLI | MDSLNLNKHISGQFNAELESIRTQVMTMGGMVEQQLSDAITAMHNQDSDLAKRVIEGDKNVNMMEVAIDEACVRIIAKRQPTASDLRLVMVISKTIAELERIGDVADKICRTALEKFSQQHQPLLVSLESLGRHTIQMLHDVLDAFARMDIDEAVRIYREDKKVDQEYEGIVRQLMTYMMEDSRTIPSVLTALFCARSIERIGDRCQNICEFIFYYVKGQDFRHVGGDELDKLLAGKDSDK | null | null | cellular response to antibiotic [GO:0071236]; cellular response to heat [GO:0034605]; cellular response to pH [GO:0071467]; cellular response to phosphate starvation [GO:0016036]; cellular response to starvation [GO:0009267]; intracellular phosphate ion homeostasis [GO:0030643]; negative regulation of gene expression [... | cytoplasm [GO:0005737] | magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; protein homodimerization activity [GO:0042803] | PF01895; | null | PhoU family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3536855}. | null | null | null | null | null | FUNCTION: Part of the phosphate (Pho) regulon, which plays a key role in phosphate homeostasis. Encoded together with proteins of the phosphate-specific transport (Pst) system in the polycistronic pstSCAB-phoU operon. PhoU is essential for the repression of the Pho regulon at high phosphate conditions. In this role, it... | Escherichia coli (strain K12) |
P0A9K9 | SLYD_ECOLI | MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVPKDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHDHHHDHDHDGCCGGHGHDHGHEHGGEGCCGGKGNGGCGCH | 5.2.1.8 | null | protein maturation [GO:0051604]; protein maturation by protein folding [GO:0022417]; protein refolding [GO:0042026]; protein stabilization [GO:0050821]; response to heat [GO:0009408] | cytosol [GO:0005829] | cobalt ion binding [GO:0050897]; copper ion binding [GO:0005507]; nickel cation binding [GO:0016151]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; unfolded protein binding [GO:0051082]; zinc ion binding [GO:0008270] | PF00254; | 2.40.10.330;3.10.50.40; | FKBP-type PPIase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:16388577}; | null | null | null | null | FUNCTION: Folding helper with both chaperone and peptidyl-prolyl cis-trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa-Pro bonds of peptides, which accelerates slow... | Escherichia coli (strain K12) |
P0A9L3 | FKBB_ECOLI | MTTPTFDTIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGIADALEGKHPAVPVDVVHRALREIHERADAVRRQRFQAMAAEGVKYLEENAKKEGVNSTESGLQFRVINQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGSKWELTIPQELAYGERGAGASIPPFSTLVFEVELLEIL | 5.2.1.8 | null | chaperone-mediated protein folding [GO:0061077] | cytosol [GO:0005829]; periplasmic space [GO:0042597] | FK506 binding [GO:0005528]; identical protein binding [GO:0042802]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; protein homodimerization activity [GO:0042803] | PF00254;PF01346; | 3.10.50.40;1.10.287.460; | FKBP-type PPIase family | null | SUBCELLULAR LOCATION: Cytoplasm. Periplasm {ECO:0000269|PubMed:7610040, ECO:0000269|PubMed:8703024}. | CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; | null | null | null | null | FUNCTION: PPIases accelerate the folding of proteins (Probable). Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:8703024). Displays a preference for substrates with a lysyl residue in the P1 position (PubMed:8703024). {ECO:0000269|PubMed:8703024, ECO:0000305}. | Escherichia coli (strain K12) |
P0A9M0 | LON_ECOLI | MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEIL... | 3.4.21.53 | null | cellular response to heat [GO:0034605]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; proteolysis [GO:0006508]; response to heat [GO:0009408]; response to X-ray [GO:0010165] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; DNA binding [GO:0003677]; peptidase activity [GO:0008233]; sequence-specific DNA binding [GO:0043565]; serine-type endopeptidase activity [GO:0004252] | PF00004;PF05362;PF02190; | 1.10.8.60;1.20.5.5270;1.20.58.1480;3.30.230.10;2.30.130.40;3.40.50.300; | Peptidase S16 family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; Evidence={ECO:0000255|HAMAP-Rule:MF_01973}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.201 mM for ATP for ATPase activity {ECO:0000269|PubMed:15560777}; | null | null | null | FUNCTION: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins, including some antitoxins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypept... | Escherichia coli (strain K12) |
P0A9M2 | HPRT_ECOLI | MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYRHLPYIGKVILLDE | 2.4.2.8 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:12070315}; | GMP salvage [GO:0032263]; guanine salvage [GO:0006178]; hypoxanthine metabolic process [GO:0046100]; IMP salvage [GO:0032264]; protein homotetramerization [GO:0051289]; purine ribonucleoside salvage [GO:0006166] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | guanine phosphoribosyltransferase activity [GO:0052657]; guanosine tetraphosphate binding [GO:0097216]; hypoxanthine phosphoribosyltransferase activity [GO:0004422]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287] | PF00156; | 3.40.50.2020; | Purine/pyrimidine phosphoribosyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8; Evidence={ECO:0000269|PubMed:12070315}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975; Eviden... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.5 uM for hypoxanthine (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12070315}; KM=294 uM for guanine (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12070315}; KM=25 uM for xanthine (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12070315}... | PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1. {ECO:0000305|PubMed:12070315}. | null | null | FUNCTION: Purine salvage pathway enzyme which catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP (inosine 5'-monophosphate). To a lesser extent, can also act on guanine leading to GMP, but shows a highly less efficie... | Escherichia coli (strain K12) |
P0A9M5 | XGPT_ECOLI | MSEKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGEGFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPWDMGVVFVPPISGR | 2.4.2.-; 2.4.2.22 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9100006}; | GMP salvage [GO:0032263]; IMP salvage [GO:0032264]; protein homotetramerization [GO:0051289]; purine ribonucleoside salvage [GO:0006166]; XMP salvage [GO:0032265] | cytosol [GO:0005829]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | guanine phosphoribosyltransferase activity [GO:0052657]; guanosine tetraphosphate binding [GO:0097216]; hypoxanthine phosphoribosyltransferase activity [GO:0004422]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; xanthine phosphoribosyltransferase activity [GO:0000310] | PF00156; | 3.40.50.2020; | Purine/pyrimidine phosphoribosyltransferase family, XGPT subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate + guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:3886014, ECO:0000269|PubMed:9100006}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:254... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.3 uM for guanine (at pH 8.5) {ECO:0000269|PubMed:9100006}; KM=30.5 uM for xanthine (at pH 8.5) {ECO:0000269|PubMed:9100006}; KM=90.8 uM for hypoxanthine (at pH 8.5) {ECO:0000269|PubMed:9100006}; KM=139 uM for 5-phospho-alpha-D-ribose 1-diphosphate (at pH 8.5) {EC... | PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP from guanine: step 1/1. {ECO:0000305|PubMed:9100006}.; PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP from xanthine: step 1/1. {ECO:0000305|PubMed:9100006}. | null | null | FUNCTION: Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosph... | Escherichia coli (strain K12) |
P0A9M8 | PTA_ECOLI | MSRIIMLIPTGTSVGLTSVSLGVIRAMERKGVRLSVFKPIAQPRTGGDAPDQTTTIVRANSSTTTAAEPLKMSYVEGLLSSNQKDVLMEEIVANYHANTKDAEVVLVEGLVPTRKHQFAQSLNYEIAKTLNAEIVFVMSQGTDTPEQLKERIELTRNSFGGAKNTNITGVIVNKLNAPVDEQGRTRPDLSEIFDDSSKAKVNNVDPAKLQESSPLPVLGAVPWSFDLIATRAIDMARHLNATIINEGDINTRRVKSVTFCARSIPHMLEHFRAGSLLVTSADRPDVLVAACLAAMNGVEIGALLLTGGYEMDARISKLCE... | 2.3.1.8 | null | acetate biosynthetic process [GO:0019413]; acetate catabolic process [GO:0045733]; acetate metabolic process [GO:0006083]; acetyl-CoA biosynthetic process from acetate [GO:0019427]; L-threonine catabolic process to propionate [GO:0070689] | cytosol [GO:0005829] | phosphate acetyltransferase activity [GO:0008959]; zinc ion binding [GO:0008270] | PF13500;PF07085;PF01515; | 3.40.50.10950;3.40.1390.20;3.40.50.10750;3.40.50.300; | CobB/CobQ family; Phosphate acetyltransferase and butyryltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + phosphate = acetyl phosphate + CoA; Xref=Rhea:RHEA:19521, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.8; Evidence={ECO:0000269|PubMed:20236319}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19522; Evidence={ECO:0000269|PubMed:202... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=67.2 uM for acetyl-CoA {ECO:0000269|PubMed:20236319}; KM=44.9 uM for acetyl phosphate {ECO:0000269|PubMed:20236319}; Vmax=177.4 uM/h/mg enzyme for acetyl-CoA-forming reaction {ECO:0000269|PubMed:20236319}; Vmax=23.1 uM/h/mg enzyme for acetyl phosphate-forming react... | PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2. | null | null | FUNCTION: Involved in acetate metabolism (PubMed:16080684). Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate (PubMed:16080684). The direction of the overall reaction changes depending on growth conditions (PubMed:16080684). On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA ... | Escherichia coli (strain K12) |
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