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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P0A6X7 | IHFA_ECOLI | MALTKAEMSEYLFDKLGLSKRDAKELVELFFEEIRRALENGEQVKLSGFGNFDLRDKNQRPGRNPKTGEDIPITARRVVTFRPGQKLKSRVENASPKDE | null | null | DNA recombination [GO:0006310]; DNA-templated transcription [GO:0006351]; regulation of translation [GO:0006417] | cytosol [GO:0005829]; IHF-DNA complex [GO:1990177]; protein-DNA complex [GO:0032993] | DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; structural constituent of chromatin [GO:0030527]; transcription cis-regulatory region binding [GO:0000976] | PF00216; | 4.10.520.10; | Bacterial histone-like protein family | null | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:21903814}. Note=Scattered throughout the nucleoid (PubMed:21903814). {ECO:0000269|PubMed:21903814}. | null | null | null | null | null | FUNCTION: One of the 2 subunits of integration host factor (IHF), a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. Binds to hundreds of transcriptionally inactive, AT-rich DNA sites, approximately half its binding sites are in non-coding DNA... | Escherichia coli (strain K12) |
P0A6Y1 | IHFB_ECOLI | MTKSELIERLATQQSHIPAKTVEDAVKEMLEHMASTLAQGERIEIRGFGSFSLHYRAPRTGRNPKTGDKVELEGKYVPHFKPGKELRDRANIYG | null | null | DNA recombination [GO:0006310]; DNA-templated transcription [GO:0006351]; regulation of DNA-templated transcription [GO:0006355]; regulation of translation [GO:0006417] | chromosome [GO:0005694]; cytosol [GO:0005829]; IHF-DNA complex [GO:1990177] | DNA binding [GO:0003677]; structural constituent of chromatin [GO:0030527] | PF00216; | 4.10.520.10; | Bacterial histone-like protein family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: One of the 2 subunits of integration host factor (IHF), a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.; FUNCTION: Plays a crucial role in the lysogenic life cycle of bacteriophage lambda, as it is required not only in the recombi... | Escherichia coli (strain K12) |
P0A6Y5 | HSLO_ECOLI | MPQHDQLHRYLFENFAVRGELVTVSETLQQILENHDYPQPVKNVLAELLVATSLLTATLKFDGDITVQLQGDGPMNLAVINGNNNQQMRGVARVQGEIPENADLKTLVGNGYVVITITPSEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIRTGDVDGKPAAGGMLLQVMPAQNAQQDDFDHLATLTETIKTEELLTLPANEVLWRLYHEEEVTVYDPQDVEFKCTCSRERCADALKTLPDEEVDSILAEDGEIDMHCDYCGNHYLFNAMDIAEIRNNASPADPQVH | null | null | maintenance of unfolded protein [GO:0036506]; protein refolding [GO:0042026]; response to heat [GO:0009408]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | identical protein binding [GO:0042802]; protein folding chaperone [GO:0044183]; unfolded protein binding [GO:0051082]; zinc ion binding [GO:0008270] | PF01430; | 1.10.287.480;3.55.30.10;3.90.1280.10; | HSP33 family | PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive. | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | Escherichia coli (strain K12) |
P0A6Y8 | DNAK_ECOLI | MGKIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQRDVSIMPFKIIAADNGDAWVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKGTGNRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVLATNGDTHLGGEDFDSRLINYLVEEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPL... | null | null | cellular response to unfolded protein [GO:0034620]; chaperone cofactor-dependent protein refolding [GO:0051085]; DNA replication [GO:0006260]; protein refolding [GO:0042026]; protein unfolding [GO:0043335]; protein-containing complex assembly [GO:0065003]; response to heat [GO:0009408]; stress response to copper ion [G... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; inclusion body [GO:0016234]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; protein-folding chaperone binding [GO:0051087]; sigma factor antagonist activity [GO:0016989]; ... | PF00012; | 1.20.1270.10;3.30.420.40; | Heat shock protein 70 family | PTM: Autophosphorylated; GrpE inhibits the autophosphorylation. {ECO:0000269|PubMed:1835085, ECO:0000269|PubMed:7783627, ECO:0000269|PubMed:8206983}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}. | null | null | null | null | null | FUNCTION: Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the... | Escherichia coli (strain K12) |
P0A6Z1 | HSCA_ECOLI | MALLQISEPGLSAAPHQRRLAAGIDLGTTNSLVATVRSGQAETLADHEGRHLLPSVVHYQQQGHSVGYDARTNAALDTANTISSVKRLMGRSLADIQQRYPHLPYQFQASENGLPMIETAAGLLNPVRVSADILKALAARATEALAGELDGVVITVPAYFDDAQRQGTKDAARLAGLHVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSRGVFEVLATGGDSALGGDDFDHLLADYIREQAGIPDRSDNRVQRELLDAAIAAKIALSDADSVTVNVAGWQGEISREQFNELIAPLVKRTLLACRRALK... | null | null | cellular response to cold [GO:0070417]; chaperone cofactor-dependent protein refolding [GO:0051085]; iron-sulfur cluster assembly [GO:0016226]; protein maturation by iron-sulfur cluster transfer [GO:0097428]; protein refolding [GO:0042026] | cytosol [GO:0005829]; iron-sulfur cluster transfer complex [GO:1990230] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; unfolded protein binding [GO:0051082] | PF00012; | 1.20.1270.10;3.30.420.40; | Heat shock protein 70 family | null | null | null | null | null | null | null | FUNCTION: Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. | Escherichia coli (strain K12) |
P0A6Z3 | HTPG_ECOLI | MKGQETRGFQSEVKQLLHLMIHSLYSNKEIFLRELISNASDAADKLRFRALSNPDLYEGDGELRVRVSFDKDKRTLTISDNGVGMTRDEVIDHLGTIAKSGTKSFLESLGSDQAKDSQLIGQFGVGFYSAFIVADKVTVRTRAAGEKPENGVFWESAGEGEYTVADITKEDRGTEITLHLREGEDEFLDDWRVRSIISKYSDHIALPVEIEKREEKDGETVISWEKINKAQALWTRNKSEITDEEYKEFYKHIAHDFNDPLTWSHNRVEGKQEYTSLLYIPSQAPWDMWNRDHKHGLKLYVQRVFIMDDAEQFMPNYLRF... | null | null | DNA damage response [GO:0006974]; FtsZ-dependent cytokinesis [GO:0043093]; protein folding [GO:0006457]; response to heat [GO:0009408] | cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; identical protein binding [GO:0042802]; protein folding chaperone [GO:0044183]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [... | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | PTM: Phosphorylated. {ECO:0000269|PubMed:2647735}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}. | null | null | null | null | null | FUNCTION: Molecular chaperone. Has ATPase activity. | Escherichia coli (strain K12) |
P0A6Z6 | NIKR_ECOLI | MQRVTITLDDDLLETLDSLSQRRGYNNRSEAIRDILRSALAQEATQQHGTQGFAVLSYVYEHEKRDLASRIVSTQHHHHDLSVATLHVHINHDDCLEIAVLKGDMGDVQHFADDVIAQRGVRHGHLQCLPKED | null | COFACTOR: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Note=Binds 1 nickel ion per subunit.; | negative regulation of DNA-templated transcription initiation [GO:2000143]; regulation of DNA-templated transcription [GO:0006355]; response to nickel cation [GO:0010045] | protein-DNA complex [GO:0032993]; transcription regulator complex [GO:0005667] | core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription repressor activity [GO:0001217]; identical protein binding [GO:0042802]; nickel cation binding [GO:0016151]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976] | PF08753;PF01402; | 3.30.70.1150;1.10.1220.10; | Transcriptional regulatory CopG/NikR family | null | null | null | null | null | null | null | FUNCTION: Transcriptional repressor of the nikABCDE operon. Is active in the presence of excessive concentrations of intracellular nickel. | Escherichia coli (strain K12) |
P0A700 | HYPA_ECOLI | MHEITLCQRALELIEQQAAKHGAKRVTGVWLKIGAFSCVETSSLAFCFDLVCRGSVAEGCKLHLEEQEAECWCETCQQYVTLLTQRVRRCPQCHGDMLQIVADDGLQIRRIEIDQE | null | null | protein maturation [GO:0051604]; protein maturation by nickel ion transfer [GO:0110147]; protein modification process [GO:0036211]; protein-containing complex assembly [GO:0065003] | GTPase complex [GO:1905360]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; metallochaperone activity [GO:0016530]; nickel cation binding [GO:0016151]; zinc ion binding [GO:0008270] | PF01155; | 3.30.2320.80; | HypA/HybF family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:22016389}. | null | null | null | null | null | FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase (PubMed:12081959, PubMed:15995183). Mediates transfer of nickel, but not zinc, from the low-affinity metal-binding site in the GTPase domain of HypB to HypA (PubMed:23899293, PubMed:279516... | Escherichia coli (strain K12) |
P0A703 | HYBF_ECOLI | MHELSLCQSAVEIIQRQAEQHDVKRVTAVWLEIGALSCVEESAVRFSFEIVCHGTVAQGCDLHIVYKPAQAWCWDCSQVVEIHQHDAQCPLCHGERLRVDTGDSLIVKSIEVE | null | null | protein maturation [GO:0051604]; protein modification process [GO:0036211] | null | metallochaperone activity [GO:0016530]; nickel cation binding [GO:0016151]; zinc ion binding [GO:0008270] | PF01155; | 3.30.2320.80; | HypA/HybF family, HybF subfamily | null | null | null | null | null | null | null | FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. HybF is involved in maturation of hydrogenases 1 and 2. It may partially substitute for the function of HypA and vice versa. {ECO:0000269|PubMed:12081959}. | Escherichia coli (strain K12) |
P0A705 | IF2_ECOLI | MTDVTIKTLAAERQTSVERLVQQFADAGIRKSADDSVSAQEKQTLIDHLNQKNSGPDKLTLQRKTRSTLNIPGTGGKSKSVQIEVRKKRTFVKRDPQEAERLAAEEQAQREAEEQARREAEESAKREAQQKAEREAAEQAKREAAEQAKREAAEKDKVSNQQDDMTKNAQAEKARREQEAAELKRKAEEEARRKLEEEARRVAEEARRMAEENKWTDNAEPTEDSSDYHVTTSQHARQAEDESDREVEGGRGRGRNAKAARPKKGNKHAESKADREEARAAVRGGKGGKRKGSSLQQGFQKPAQAVNRDVVIGETITVGE... | null | null | chaperone-mediated protein folding [GO:0061077]; response to cold [GO:0009409]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; ribosomal small subunit binding [GO:0043024]; translation initiation factor activity [GO:0003743] | PF00009;PF03144;PF11987;PF08364;PF04760; | 3.40.50.300;3.30.56.50;2.40.30.10;3.40.50.10050; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, IF-2 subfamily | PTM: A proteolyzed form, called IF2 gamma (begins with residue 290), can be detected during purification which has all the activities expected for this protein, although it is slightly less efficient than full-length protein. It is not clear if it exists in vivo. {ECO:0000269|PubMed:2444251}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1764105}. | null | null | null | null | null | FUNCTION: One of the essential components for the initiation of protein synthesis. May protect N-formylmethionyl-tRNA(fMet) from spontaneous hydrolysis. Promotes N-formylmethionyl-tRNA(fMet) binding to the 30S pre-initiation complex (PIC) (PubMed:1764105, PubMed:20224578). Also involved in the hydrolysis of GTP during ... | Escherichia coli (strain K12) |
P0A707 | IF3_ECOLI | MKGGKRVQTARPNRINGEIRAQEVRLTGLEGEQLGIVSLREALEKAEEAGVDLVEISPNAEPPVCRIMDYGKFLYEKSKSSKEQKKKQKVIQVKEIKFRPGTDEGDYQVKLRSLIRFLEEGDKAKITLRFRGREMAHQQIGMEVLNRVKDDLQELAVVESFPTKIEGRQMIMVLAPKKKQ | null | null | response to cold [GO:0009409]; ribosome disassembly [GO:0032790] | cytosol [GO:0005829]; membrane [GO:0016020] | ribosome binding [GO:0043022]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743] | PF00707;PF05198; | 3.30.110.10;3.10.20.80; | IF-3 family | PTM: Phosphorylated on threonine residue(s). {ECO:0000269|PubMed:1534259}.; PTM: The form lacking the initiator methionine is less abundant than the N-methylmethionine form. {ECO:0000269|PubMed:330233}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:330233}. | null | null | null | null | null | FUNCTION: One of the essential components for the initiation of protein synthesis.IF-3 binds to the 30S ribosomal subunit and shifts the equilibrium between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation b... | Escherichia coli (strain K12) |
P0A710 | YCIB_ECOLI | MKQFLDFLPLVVFFAFYKIYDIYAATAALIVATAIVLIYSWVRFRKVEKMALITFVLVVVFGGLTLFFHNDEFIKWKVTVIYALFAGALLVSQWVMKKPLIQRMLGKELTLPQPVWSKLNLAWAVFFILCGLANIYIAFWLPQNIWVNFKVFGLTALTLIFTLLSGIYIYRHMPQEDKS | null | null | null | plasma membrane [GO:0005886] | null | PF04279; | null | YciB family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00189, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:26391555, ECO:0000269|PubMed:26454142}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00189, ECO:0000269|PubMed:26454142, ECO:0000305|PubMed:15919996}. Note=Distributed in the inner membr... | null | null | null | null | null | FUNCTION: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis (PubMed:26391555, PubMed:26454142, PubMed:30368949, PubMed:33431434). Required for the normal cell elongation (PubMed:26391555). May participate in the cell division process (PubMed:26391555). Important f... | Escherichia coli (strain K12) |
P0A712 | KDGT_ECOLI | MQIKRSIEKIPGGMMLVPLFLGALCHTFSPGAGKYFGSFTNGMITGTVPILAVWFFCMGASIKLSATGTVLRKSGTLVVTKIAVAWVVAAIASRIIPEHGVEVGFFAGLSTLALVAAMDMTNGGLYASIMQQYGTKEEAGAFVLMSLESGPLMTMIILGTAGIASFEPHVFVGAVLPFLVGFALGNLDPELREFFSKAVQTLIPFFAFALGNTIDLTVIAQTGLLGILLGVAVIIVTGIPLIIADKLIGGGDGTAGIAASSSAGAAVATPVLIAEMVPAFKPMAPAATSLVATAVIVTSILVPILTSIWSRKVKARAAKI... | null | null | gluconate transmembrane transport [GO:0035429] | membrane [GO:0016020]; plasma membrane [GO:0005886] | 2-keto-3-deoxygluconate:proton symporter activity [GO:0015649] | PF03812; | null | KdgT transporter family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:6094479}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2-dehydro-3-deoxy-D-gluconate(in) + H(+)(in) = 2-dehydro-3-deoxy-D-gluconate(out) + H(+)(out); Xref=Rhea:RHEA:29943, ChEBI:CHEBI:15378, ChEBI:CHEBI:57990; Evidence={ECO:0000255|HAMAP-Rule:MF_00070, ECO:0000269|PubMed:15555}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29945; Eviden... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 mM for 2-keto-3-deoxygluconate {ECO:0000269|PubMed:15555}; KM=1.5 mM for D-glucuronate {ECO:0000269|PubMed:15555}; | null | null | null | FUNCTION: Catalyzes the proton-dependent uptake of 2-keto-3-deoxygluconate (KDG) into the cell (PubMed:15555, PubMed:6094479). Expression of this specific KDG-uptake system may allow growth with KDG as the sole carbon source (PubMed:4359651). Can also transport D-glucuronate (PubMed:15555, PubMed:6094479). {ECO:0000269... | Escherichia coli (strain K12) |
P0A715 | KDSA_ECOLI | MKQKVVSIGDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDRGANFGYDNLVVDMLGFSIMKKVSGNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPLAKLEPFLKQMKAIDDLVKGFEELDTSK | 2.5.1.55 | null | keto-3-deoxy-D-manno-octulosonic acid biosynthetic process [GO:0019294] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | 3-deoxy-8-phosphooctulonate synthase activity [GO:0008676]; identical protein binding [GO:0042802] | PF00793; | 3.20.20.70; | KdsA family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate; Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55; | null | PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3.; PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. | null | null | FUNCTION: Synthesis of KDO 8-P which is required for lipid A maturation and cellular growth. | Escherichia coli (strain K12) |
P0A717 | KPRS_ECOLI | MPDMKLFAGNATPELAQRIANRLYTSLGDAAVGRFSDGEVSVQINENVRGGDIFIIQSTCAPTNDNLMELVVMVDALRRASAGRITAVIPYFGYARQDRRVRSARVPITAKVVADFLSSVGVDRVLTVDLHAEQIQGFFDVPVDNVFGSPILLEDMLQLNLDNPIVVSPDIGGVVRARAIAKLLNDTDMAIIDKRRPRANVSQVMHIIGDVAGRDCVLVDDMIDTGGTLCKAAEALKERGAKRVFAYATHPIFSGNAANNLRNSVIDEVVVCDTIPLSDEIKSLPNVRTLTLSGMLAEAIRRISNEESISAMFEH | 2.7.6.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:10954724, ECO:0000269|PubMed:2542328, ECO:0000269|PubMed:3009477, ECO:0000269|PubMed:8679571, ECO:0000269|PubMed:9125530, ECO:0000305|Ref.13}; Note=Binds 2 Mg(2+) ions per subunit (Probable). Mn(2+), Co(2+) and ... | 5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; phosphorylation [GO:0016310]; protein hexamerization [GO:0034214]; purine nucleotide biosynthetic process [GO:0006164]; ribonucleoside monophosphate biosynthetic process [GO:0009156] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; ribose phosphate diphosphokinase complex [GO:0002189] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; phosphate ion binding [GO:0042301]; ribose phosphate diphosphokinase activity [GO:0004749] | PF14572;PF13793; | 3.40.50.2020; | Ribose-phosphate pyrophosphokinase family, Class I subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}. | CATALYTIC ACTIVITY: Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:2542328, ECO:0000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=138 uM for Rib-5-P (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:3009477}; KM=230 uM for ATP (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:2542328}; KM=280 uM for Rib-5-P (at pH 8.5 and 37 degrees Celsius) {ECO:0000269|PubMed:8679571}; KM=300 uM for R... | PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:8679571}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.7-9.8. {ECO:0000269|PubMed:3009477}; | null | FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:10954724, ECO:0000269|PubMed:2542328, ECO:0000269|PubMed:3... | Escherichia coli (strain K12) |
P0A720 | KTHY_ECOLI | MRSKYIVIEGLEGAGKTTARNVVVETLEQLGIRDMVFTREPGGTQLAEKLRSLVLDIKSVGDEVITDKAEVLMFYAARVQLVETVIKPALANGTWVIGDRHDLSTQAYQGGGRGIDQHMLATLRDAVLGDFRPDLTLYLDVTPEVGLKRARARGELDRIEQESFDFFNRTRARYLELAAQDKSIHTIDATQPLEAVMDAIRTTVTHWVKELDA | 2.7.4.9 | null | dTDP biosynthetic process [GO:0006233]; dTTP biosynthetic process [GO:0006235]; dUDP biosynthetic process [GO:0006227]; nucleobase-containing small molecule interconversion [GO:0015949]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; thymidylate kinase activity [GO:0004798] | PF02223; | 3.40.50.300; | Thymidylate kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000269|PubMed:8631667}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.04 mM for ATP (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:11369858}; KM=15 uM for dTMP (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:11369858}; Vmax=50 umol/min/mg enzyme with ATP and dTMP as substrates (at pH 7.4 and 30 degrees Celsius) {ECO:... | PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. | null | null | FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor (PubMed:8631667). Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DN... | Escherichia coli (strain K12) |
P0A725 | LPXC_ECOLI | MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEIPIMDGSAAPFVYLLLDAGIDELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDSSNQRYAMNFSADAFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMCGHNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLAFKAPSAVLA | 3.5.1.108 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:10026271, ECO:0000269|PubMed:20709752}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:20136146, ECO:0000269|PubMed:20709752}; Note=Can use either Fe(2+) or Zn(2+). The metal cofactor can swit... | lipid A biosynthetic process [GO:0009245] | cytoplasm [GO:0005737] | deacetylase activity [GO:0019213]; iron ion binding [GO:0005506]; UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity [GO:0008759]; UDP-3-O-acyl-N-acetylglucosamine deacetylase activity [GO:0103117]; zinc ion binding [GO:0008270] | PF03331; | 3.30.230.20;3.30.1700.10; | LpxC family | PTM: Degraded by FtsH. {ECO:0000269|PubMed:10048027, ECO:0000269|PubMed:16420369, ECO:0000269|PubMed:21193611, ECO:0000269|PubMed:23417489}. | null | CATALYTIC ACTIVITY: Reaction=a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate; Xref=Rhea:RHEA:67816, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:137740, ChEBI:CHEBI:173225; EC=3.5.1.108; Evidence={ECO:0000255|HAMAP-Rule:MF_00388, ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.1 uM for UDP-3-O-myristoyl-N-acetylglucosamine (at 30 degrees Celsius) {ECO:0000269|PubMed:10026271}; KM=0.6 uM for UDP-3-O-myristoyl-N-acetylglucosamine (at 1 degree Celsius) {ECO:0000269|PubMed:10026271}; Note=kcat is 3.3 sec(-1) at 30 degrees Celsius. kcat is ... | PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6. {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:8530464}. | null | null | FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:10026271, ECO:0000269|PubMed:8530464, ECO:0000269|PubMed:8824222, ECO:0000269|Ref.7}. | Escherichia coli (strain K12) |
P0A729 | NTPPB_ECOLI | MPKLILASTSPWRRALLEKLQISFECAAPEVDETPRSDESPRQLVLRLAQEKAQSLASRYPDHLIIGSDQVCVLDGEITGKPLTEENARLQLRKASGNIVTFYTGLALFNSANGHLQTEVEPFDVHFRHLSEAEIDNYVRKEHPLHCAGSFKSEGFGITLFERLEGRDPNTLVGLPLIALCQMLRREGKNPLMG | 3.6.1.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_00528}; | nucleotide metabolic process [GO:0009117] | cytoplasm [GO:0005737] | nucleoside triphosphate diphosphatase activity [GO:0047429] | PF02545; | 3.90.950.10; | Maf family, YceF subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP; Xref=Rhea:RHEA:58744, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58285, ChEBI:CHEBI:87133; Evidence={ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000269|PubMed:24210219}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32.8 uM for m(7)GTP {ECO:0000269|PubMed:24210219}; Note=kcat is 1.2 sec(-1). {ECO:0000269|PubMed:24210219}; | null | null | null | FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP) (PubMed:24210219). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids (PubMed:24210219). {ECO:0000269|PubMed:24210219}. | Escherichia coli (strain K12) |
P0A731 | MGSA_ECOLI | MELTTRTLPARKHIALVAHDHCKQMLMSWVERHQPLLEQHVLYATGTTGNLISRATGMNVNAMLSGPMGGDQQVGALISEGKIDVLIFFWDPLNAVPHDPDVKALLRLATVWNIPVATNVATADFIIQSPHFNDAVDILIPDYQRYLADRLK | 4.2.3.3 | null | methylglyoxal biosynthetic process [GO:0019242]; protein hexamerization [GO:0034214] | cytosol [GO:0005829] | identical protein binding [GO:0042802]; methylglyoxal synthase activity [GO:0008929] | PF02142; | 3.40.50.1380; | Methylglyoxal synthase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate; Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474, ChEBI:CHEBI:57642; EC=4.2.3.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:11389594, ECO:0000269|PubMed:15049687, ECO:0000269|PubMed:9665712}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for dihydroxyacetone phosphate {ECO:0000269|PubMed:9665712}; Note=kcat is 220 sec(-1) with dihydroxyacetone phosphate as substrate. {ECO:0000269|PubMed:9665712}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:15049687}; | null | FUNCTION: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. {ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:11389594, ECO:0000269|PubMed:15049687, ECO:0000269|PubMed:9665712}. | Escherichia coli (strain K12) |
P0A738 | MOAC_ECOLI | MSQLTHINAAGEAHMVDVSAKAETVREARAEAFVTMRSETLAMIIDGRHHKGDVFATARIAGIQAAKRTWDLIPLCHPLMLSKVEVNLQAEPEHNRVRIETLCRLTGKTGVEMEALTAASVAALTIYDMCKAVQKDMVIGPVRLLAKSGGKSGDFKVEADD | 4.6.1.17 | null | Mo-molybdopterin cofactor biosynthetic process [GO:0006777] | protein-containing complex [GO:0032991] | cyclic pyranopterin monophosphate synthase activity [GO:0061799]; identical protein binding [GO:0042802] | PF01967; | 3.30.70.640; | MoaC family | null | null | CATALYTIC ACTIVITY: Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate; Xref=Rhea:RHEA:49580, ChEBI:CHEBI:33019, ChEBI:CHEBI:59648, ChEBI:CHEBI:131766; EC=4.6.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01224, ECO:0000269|PubMed:25941396}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.21 uM for (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate {ECO:0000269|PubMed:25941396}; Note=kcat is 0.56 min(-1). {ECO:0000269|PubMed:25941396}; | PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01224}. | null | null | FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). {ECO:0000255|HAMAP-Rule:MF_01224, ECO:0000269|PubMed:25941396}. | Escherichia coli (strain K12) |
P0A742 | MSCL_ECOLI | MSIIKEFREFAMRGNVVDLAVGVIIGAAFGKIVSSLVADIIMPPLGLLIGGIDFKQFAVTLRDAQGDIPAVVMHYGVFIQNVFDFLIVAFAIFMAIKLINKLNRKKEEPAAAPAPTKEEVLLTEIRDLLKEQNNRS | null | null | monoatomic ion transmembrane transport [GO:0034220]; monoatomic ion transport [GO:0006811] | membrane [GO:0016020]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; mechanosensitive monoatomic ion channel activity [GO:0008381] | PF01741; | null | MscL family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00115, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23416054, ECO:0000269|PubMed:7511799, ECO:0000269|PubMed:8890153, ECO:0000269|PubMed:9632260, ECO:0000305|PubMed:21151884, ECO:0000305|PubMed:23875651}; Multi-pass membrane protein {ECO:0000255|HA... | null | null | null | null | null | FUNCTION: Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer. Forms a nonselective ion channel with a conductance of about 4 nanosiemens. Participates in the regulation of osmotic pressure changes within the cell. Opens at a pressure just below that which would cause cell di... | Escherichia coli (strain K12) |
P0A744 | MSRA_ECOLI | MSLFDKKHLVSPADALPGRNTPMPVATLHAVNGHSMTNVPDGMEIAIFAMGCFWGVERLFWQLPGVYSTAAGYTGGYTPNPTYREVCSGDTGHAEAVRIVYDPSVISYEQLLQVFWENHDPAQGMRQGNDHGTQYRSAIYPLTPEQDAAARASLERFQAAMLAADDDRHITTEIANATPFYYAEDDHQQYLHKNPYGYCGIGGIGVCLPPEA | 1.8.4.11 | null | cellular response to oxidative stress [GO:0034599]; protein modification process [GO:0036211]; protein repair [GO:0030091]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | L-methionine-(S)-S-oxide reductase activity [GO:0036456]; oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor [GO:0016671]; peptide-methionine (S)-S-oxide reductase activity [GO:0008113] | PF01625; | 3.30.1060.10; | MsrA Met sulfoxide reductase family | null | null | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]; Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHE... | null | null | null | null | FUNCTION: Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. {ECO:0000269|PubMed:10964927}. | Escherichia coli (strain K12) |
P0A746 | MSRB_ECOLI | MANKPSAEELKKNLSEMQFYVTQNHGTEPPFTGRLLHNKRDGVYHCLICDAPLFHSQTKYDSGCGWPSFYEPVSEESIRYIKDLSHGMQRIEIRCGNCDAHLGHVFPDGPQPTGERYCVNSASLRFTDGENGEEING | 1.8.4.12 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16251365}; Note=Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein. {ECO:0000269|PubMed:16251365}; | protein repair [GO:0030091]; response to cadmium ion [GO:0046686]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | iron ion binding [GO:0005506]; L-methionine-(R)-S-oxide reductase activity [GO:0033745]; peptide-methionine (R)-S-oxide reductase activity [GO:0033743]; zinc ion binding [GO:0008270] | PF01641; | 2.170.150.20; | MsrB Met sulfoxide reductase family | null | null | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]; Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHE... | null | null | null | null | null | Escherichia coli (strain K12) |
P0A749 | MURA_ECOLI | MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNGSVHIDARDVNVFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEGT... | 2.5.1.7 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]; UDP-N-acetylgalactosamine biosynthetic process [GO:0019277] | cytosol [GO:0005829] | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity [GO:0008760] | PF00275; | 3.65.10.10; | EPSP synthase family, MurA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00111, ECO:0000269|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 uM for UDP-N-acetylglucosamine {ECO:0000269|PubMed:21445328}; | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00111, ECO:0000269|PubMed:1512209}. | null | null | FUNCTION: Cell wall formation (PubMed:1512209). Adds enolpyruvyl to UDP-N-acetylglucosamine (PubMed:1512209, PubMed:20392080). Target for the antibiotic fosfomycin. {ECO:0000269|PubMed:1512209, ECO:0000269|PubMed:20392080}. | Escherichia coli (strain K12) |
P0A754 | KEFF_ECOLI | MILIIYAHPYPHHSHANKRMLEQARTLEGVEIRSLYQLYPDFNIDIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVFSHGWAYGHGGTALHGKHLLWAVTTGGGESHFEIGAHPGFDVLSQPLQATAIYCGLNWLPPFAMHCTFICDDETLEGQARHYKQRLLEWQEAHHG | 1.6.5.2 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_01414, ECO:0000269|PubMed:21742892}; | intracellular pH elevation [GO:0051454]; positive regulation of potassium ion transmembrane transport [GO:1901381]; potassium ion transport [GO:0006813]; regulation of intracellular pH [GO:0051453] | plasma membrane [GO:0005886]; potassium:proton antiporter complex [GO:1903103] | electron transfer activity [GO:0009055]; FMN binding [GO:0010181]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]; NADH dehydrogenase (quinone) activity [GO:0050136]; NADPH dehydrogenase (quinone) activity [GO:0008753]; protein homodimerization activity [GO:0042803] | PF02525; | 3.40.50.360; | NAD(P)H dehydrogenase (quinone) family, KefF subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01414}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01414}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01414}. | 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_01414, ECO:0000269|PubMed:21742892}; CATALYTIC ACTIVITY: Reaction=a quinone + H(... | null | null | null | null | FUNCTION: Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC. Can use a wide range of substrates, including electrophilic quinones, and its f... | Escherichia coli (strain K12) |
P0A759 | NAGB_ECOLI | MRLIPLTTAEQVGKWAARHIVNRINAFKPTADRPFVLGLPTGGTPMTTYKALVEMHKAGQVSFKHVVTFNMDEYVGLPKEHPESYYSFMHRNFFDHVDIPAENINLLNGNAPDIDAECRQYEEKIRSYGKIHLFMGGVGNDGHIAFNEPASSLASRTRIKTLTHDTRVANSRFFDNDVNQVPKYALTVGVGTLLDAEEVMILVLGSQKALALQAAVEGCVNHMWTISCLQLHPKAIMVCDEPSTMELKVKTLRYFNELEAENIKGL | 3.5.99.6 | null | carbohydrate metabolic process [GO:0005975]; glucosamine catabolic process [GO:0006043]; N-acetylglucosamine catabolic process [GO:0006046]; N-acetylneuraminate catabolic process [GO:0019262]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | glucosamine-6-phosphate deaminase activity [GO:0004342]; identical protein binding [GO:0042802] | PF01182; | 3.40.50.1360; | Glucosamine/galactosamine-6-phosphate isomerase family, NagB subfamily | null | null | CATALYTIC ACTIVITY: Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6; Evidence={ECO:0000269|PubMed:1734962, ECO:0000269|PubMed:2821923}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 mM for GlcN6P {ECO:0000269|PubMed:2821923}; | PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5. | null | null | FUNCTION: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. {ECO:0000269|PubMed:1734962, ECO:0000269|PubMed:2821923}. | Escherichia coli (strain K12) |
P0A763 | NDK_ECOLI | MAIERTFSIIKPNAVAKNVIGNIFARFEAAGFKIVGTKMLHLTVEQARGFYAEHDGKPFFDGLVEFMTSGPIVVSVLEGENAVQRHRDLLGATNPANALAGTLRADYADSLTENGTHGSDSVESAAREIAYFFGEGEVCPRTR | 2.7.4.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00451}; | CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; phosphorylation [GO:0016310]; purine nucleotide metabolic process [GO:0006163]; pyrimidine nucleotide metabolic process [GO:0006220]; UTP biosynthetic process [GO:0006228] | cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleoside diphosphate kinase activity [GO:0004550] | PF00334; | 3.30.70.141; | NDK family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00451, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00451, ECO:0000269|PubMed:7730286}; CATALYTIC AC... | null | null | null | null | FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. {ECO:0000255|HAMAP-Rule:MF_00451, ECO:0000269|PubMed:7730286}. | Escherichia coli (strain K12) |
P0A769 | MNTH_ECOLI | MTNYRVESSSGRAARKMRLALMGPAFIAAIGYIDPGNFATNIQAGASFGYQLLWVVVWANLMAMLIQILSAKLGIATGKNLAEQIRDHYPRPVVWFYWVQAEIIAMATDLAEFIGAAIGFKLILGVSLLQGAVLTGIATFLILMLQRRGQKPLEKVIGGLLLFVAAAYIVELIFSQPNLAQLGKGMVIPSLPTSEAVFLAAGVLGATIMPHVIYLHSSLTQHLHGGSRQQRYSATKWDVAIAMTIAGFVNLAMMATAAAAFHFSGHTGVADLDEAYLTLQPLLSHAAATVFGLSLVAAGLSSTVVGTLAGQVVMQGFIRF... | null | null | cadmium ion transport [GO:0015691]; cellular response to iron ion [GO:0071281]; cobalt ion transport [GO:0006824]; intracellular manganese ion homeostasis [GO:0030026]; iron ion transmembrane transport [GO:0034755]; iron ion transport [GO:0006826]; manganese ion transport [GO:0006828]; metal ion transport [GO:0030001] | plasma membrane [GO:0005886] | cadmium ion transmembrane transporter activity [GO:0015086]; manganese ion transmembrane transporter activity [GO:0005384]; metal ion binding [GO:0046872]; proton transmembrane transporter activity [GO:0015078]; symporter activity [GO:0015293]; uniporter activity [GO:0015292] | PF01566; | null | NRAMP family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00221, ECO:0000269|PubMed:14607838}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00221, ECO:0000269|PubMed:14607838}. | null | null | null | null | null | FUNCTION: H(+)-stimulated, divalent metal cation uptake system. Involved in manganese and iron uptake. Can also transport cadmium, cobalt, zinc and to a lesser extent nickel and copper. Involved in response to reactive oxygen. {ECO:0000255|HAMAP-Rule:MF_00221, ECO:0000269|PubMed:10712688, ECO:0000269|PubMed:10844693}. | Escherichia coli (strain K12) |
P0A776 | RPPH_ECOLI | MIDDDGYRPNVGIVICNRQGQVMWARRFGQHSWQFPQGGINPGESAEQAMYRELFEEVGLSRKDVRILASTRNWLRYKLPKRLVRWDTKPVCIGQKQKWFLLQLVSGDAEINMQTSSTPEFDGWRWVSYWYPVRQVVSFKRDVYRRVMKEFASVVMSLQENTPKPQNASAYRRKRG | 3.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11479323}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11479323}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11479323}; Note=Magnesium or zinc. Manganese can be used to a lesser extent. {ECO:0000269|... | deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; mRNA catabolic process [GO:0006402]; NAD-cap decapping [GO:0110155]; RNA decapping [GO:0110154]; RNA destabilization [GO:0050779]; tRNA processing [GO:0008033] | cytoplasm [GO:0005737]; P-body [GO:0000932] | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; magnesium ion binding [GO:0000287]; mRNA 5'-diphosphatase activity [GO:0034353]; RNA NAD-cap (NMN-forming) hydrolase activity [GO:0110153] | PF00293; | 3.90.79.10; | Nudix hydrolase family, RppH subfamily | null | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:11479323}; | null | FUNCTION: Master regulator of 5'-end-dependent mRNA decay (PubMed:18202662). Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage (PubMed:18202662). Preferentia... | Escherichia coli (strain K12) |
P0A784 | ORN_ECOLI | MSANENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNILAEGPTIAVHQSDEQLALMDDWNVRTHTASGLVERVKASTMGDREAELATLEFLKQWVPAGKSPICGNSIGQDRRFLFKYMPELEAYFHYRYLDVSTLKELARRWKPEILDGFTKQGTHQAMDDIRESVAELAYYREHFIKL | 3.1.15.- | null | RNA catabolic process [GO:0006401] | cytosol [GO:0005829] | 3'-5'-RNA exonuclease activity [GO:0000175]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; oligoribonucleotidase activity [GO:0034611]; single-stranded DNA 3'-5' DNA exonuclease activity [GO:0008310] | PF00929; | 3.30.420.10; | Oligoribonuclease family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides 2 to 5 nucleotides in length, as well as small (2 to 5 nucleotides) ssDNA oligomers. Probably responsible for the final step in mRNA degradation. {ECO:0000269|PubMed:16682444, ECO:0000269|PubMed:7608090, ECO:0000269|PubMed:9573169}. | Escherichia coli (strain K12) |
P0A786 | PYRB_ECOLI | MANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEYANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL | 2.1.3.2 | null | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; glutamine metabolic process [GO:0006541]; protein homotrimerization [GO:0070207] | aspartate carbamoyltransferase complex [GO:0009347]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | amino acid binding [GO:0016597]; aspartate carbamoyltransferase activity [GO:0004070]; identical protein binding [GO:0042802] | PF00185;PF02729; | 3.40.50.1370; | Aspartate/ornithine carbamoyltransferase superfamily, ATCase family | null | null | CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000269|PubMed:13319326}; | null | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:13319326}. | null | null | FUNCTION: Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway. {ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000269|PubMed:13319326}. | Escherichia coli (strain K12) |
P0A790 | PAND_ECOLI | MIRTMLQGKLHRVKVTHADLHYEGSCAIDQDFLDAAGILENEAIDIWNVTNGKRFSTYAIAAERGSRIISVNGAAAHCASVGDIVIIASFVTMPDEEARTWRPNVAYFEGDNEMKRTAKAIPVQVA | 4.1.1.11 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Note=Binds 1 pyruvoyl group covalently per subunit.; | alanine biosynthetic process [GO:0006523]; pantothenate biosynthetic process [GO:0015940]; protein autoprocessing [GO:0016540] | cytosol [GO:0005829] | aspartate 1-decarboxylase activity [GO:0004068] | PF02261; | 2.40.40.20; | PanD family | PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:6767707}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000269|PubMed:6767707}; | null | PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. | null | null | FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. {ECO:0000269|PubMed:6767707}. | Escherichia coli (strain K12) |
P0A794 | PDXJ_ECOLI | MAELLLGVNIDHIATLRNARGTAYPDPVQAAFIAEQAGADGITVHLREDRRHITDRDVRILRQTLDTRMNLEMAVTEEMLAIAVETKPHFCCLVPEKRQEVTTEGGLDVAGQRDKMRDACKRLADAGIQVSLFIDADEEQIKAAAEVGAPFIEIHTGCYADAKTDAEQAQELARIAKAATFAASLGLKVNAGHGLTYHNVKAIAAIPEMHELNIGHAIIGRAVMTGLKDAVAEMKRLMLEARG | 2.6.99.2 | null | pyridoxine biosynthetic process [GO:0008615] | cytosol [GO:0005829] | identical protein binding [GO:0042802]; pyridoxine 5'-phosphate synthase activity [GO:0033856] | PF03740; | 3.20.20.70; | PNP synthase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate; Xref=Rhea:RHEA:15265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57279, ChEBI:CHEBI:57792, ChEBI:CHEBI:58589; EC=2.6.99.2; Evidence={ECO:0000269|Pub... | null | PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5. {ECO:0000269|PubMed:10225425}. | null | null | FUNCTION: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. {ECO:0000269|PubMed:10225425}. | Escherichia coli (strain K12) |
P0A796 | PFKA_ECOLI | MIKKIGVLTSGGDAPGMNAAIRGVVRSALTEGLEVMGIYDGYLGLYEDRMVQLDRYSVSDMINRGGTFLGSARFPEFRDENIRAVAIENLKKRGIDALVVIGGDGSYMGAMRLTEMGFPCIGLPGTIDNDIKGTDYTIGFFTALSTVVEAIDRLRDTSSSHQRISVVEVMGRYCGDLTLAAAIAGGCEFVVVPEVEFSREDLVNEIKAGIAKGKKHAIVAITEHMCDVDELAHFIEKETGRETRATVLGHIQRGGSPVPYDRILASRMGAYAIDLLLAGYGGRCVGIQNEQLVHHDIIDAIENMKRPFKGDWLDCAKKLY | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:2975709}; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; glucose catabolic process [GO:0006007]; glycolytic process [GO:0006096]; protein homotetramerization [GO:0051289] | 6-phosphofructokinase complex [GO:0005945]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; GDP binding [GO:0019003]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; monosaccharide binding [GO:0048029]; ribonucleotide binding [GO:0032553] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Prokaryotic clade 'B1' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000305|PubMed:17895580}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:2953977, ECO:00... | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00339}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (PubMed:2953977, PubMed:3158524). In addition, is involved in the utilization of D-sedoheptulose 7-phosphate, an intermediate of the pentose phosphate pathway, via the sedoheptu... | Escherichia coli (strain K12) |
P0A799 | PGK_ECOLI | MSVIKMTDLDLAGKRVFIRADLNVPVKDGKVTSDARIRASLPTIELALKQGAKVMVTSHLGRPTEGEYNEEFSLLPVVNYLKDKLSNPVRLVKDYLDGVDVAEGELVVLENVRFNKGEKKDDETLSKKYAALCDVFVMDAFGTAHRAQASTHGIGKFADVACAGPLLAAELDALGKALKEPARPMVAIVGGSKVSTKLTVLDSLSKIADQLIVGGGIANTFIAAQGHDVGKSLYEADLVDEAKRLLTTCNIPVPSDVRVATEFSETAPATLKSVNDVKADEQILDIGDASAQELAEILKNAKTILWNGPVGVFEFPNFRK... | 2.7.2.3 | null | gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310] | cytosol [GO:0005829] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; guanosine tetraphosphate binding [GO:0097216]; phosphoglycerate kinase activity [GO:0004618] | PF00162; | 3.40.50.1260; | Phosphoglycerate kinase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. | null | null | null | Escherichia coli (strain K12) |
P0A7A7 | PLSB_ECOLI | MSGWPRIYYKLLNLPLSILVKSKSIPADPAPELGLDTSRPIMYVLPYNSKADLLTLRAQCLAHDLPDPLEPLEIDGTLLPRYVFIHGGPRVFTYYTPKEESIKLFHDYLDLHRSNPNLDVQMVPVSVMFGRAPGREKGEVNPPLRMLNGVQKFFAVLWLGRDSFVRFSPSVSLRRMADEHGTDKTIAQKLARVARMHFARQRLAAVGPRLPARQDLFNKLLASRAIAKAVEDEARSKKISHEKAQQNAIALMEEIAANFSYEMIRLTDRILGFTWNRLYQGINVHNAERVRQLAHDGHELVYVPCHRSHMDYLLLSYVLY... | 2.3.1.15 | null | CDP-diacylglycerol biosynthetic process [GO:0016024]; ether lipid biosynthetic process [GO:0008611]; fatty acid metabolic process [GO:0006631]; glycerol-3-phosphate metabolic process [GO:0006072]; phospholipid biosynthetic process [GO:0008654]; triglyceride biosynthetic process [GO:0019432] | peroxisomal membrane [GO:0005778]; plasma membrane [GO:0005886] | glycerol-3-phosphate O-acyltransferase activity [GO:0004366]; glycerone-phosphate O-acyltransferase activity [GO:0016287]; sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity [GO:0102420] | PF01553;PF19277; | null | GPAT/DAPAT family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16294310, ECO:0000269|PubMed:4943977}; Peripheral membrane protein {ECO:0000269|PubMed:16294310, ECO:0000269|PubMed:4943977}; Cytoplasmic side {ECO:0000269|PubMed:16294310, ECO:0000269|PubMed:4943977}. | CATALYTIC ACTIVITY: Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15; Evidence={ECO:0000269|PubMed:10231527}; CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + sn-glycerol 3... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=49 uM for glycerol-3-phosphate {ECO:0000269|PubMed:10231527, ECO:0000269|PubMed:7026564}; Vmax=13.1 nmol/min/mg enzyme with glycerol-3-phosphate as substrate {ECO:0000269|PubMed:10231527, ECO:0000269|PubMed:7026564}; | PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:10231527, ECO:0000269|PubMed:7026564}; | null | FUNCTION: Catalyzes the transfer of an acyl group from acyl-ACP to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme can utilize either acyl-CoA or acyl-ACP as the fatty acyl donor. {ECO:0000269|PubMed:17645809, ECO:0000269|PubMed:6997313}. | Escherichia coli (strain K12) |
P0A7A9 | IPYR_ECOLI | MSLLNVPAGKDLPEDIYVVIEIPANADPIKYEIDKESGALFVDRFMSTAMFYPCNYGYINHTLSLDGDPVDVLVPTPYPLQPGSVIRCRPVGVLKMTDEAGEDAKLVAVPHSKLSKEYDHIKDVNDLPELLKAQIAHFFEHYKDLEKGKWVKVEGWENAEAAKAEIVASFERAKNK | 3.6.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00209}; | phosphate-containing compound metabolic process [GO:0006796] | cytosol [GO:0005829]; membrane [GO:0016020] | inorganic diphosphate phosphatase activity [GO:0004427]; inorganic triphosphate phosphatase activity [GO:0050355]; magnesium ion binding [GO:0000287]; zinc ion binding [GO:0008270] | PF00719; | 3.90.80.10; | PPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00209}. | CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00209}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}. | Escherichia coli (strain K12) |
P0A7B1 | PPK1_ECOLI | MGQEKLYIEKELSWLSFNERVLQEAADKSNPLIERMRFLGIYSNNLDEFYKVRFAELKRRIIISEEQGSNSHSRHLLGKIQSRVLKADQEFDGLYNELLLEMARNQIFLINERQLSVNQQNWLRHYFKQYLRQHITPILINPDTDLVQFLKDDYTYLAVEIIRGDTIRYALLEIPSDKVPRFVNLPPEAPRRRKPMILLDNILRYCLDDIFKGFFDYDALNAYSMKMTRDAEYDLVHEMEASLMELMSSSLKQRLTAEPVRFVYQRDMPNALVEVLREKLTISRYDSIVPGGRYHNFKDFINFPNVGKANLVNKPLPRLR... | 2.7.4.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00347, ECO:0000269|PubMed:10660553}; | phosphorylation [GO:0016310]; polyphosphate biosynthetic process [GO:0006799] | cytosol [GO:0005829]; periplasmic side of cell outer membrane [GO:0031241]; plasma membrane [GO:0005886]; polyphosphate kinase complex [GO:0009358] | ATP binding [GO:0005524]; diphosphotransferase activity [GO:0016778]; metal ion binding [GO:0046872]; phosphotransferase activity, phosphate group as acceptor [GO:0016776]; polyphosphate kinase activity [GO:0008976]; polyphosphate:AMP phosphotransferase activity [GO:0043751]; protein homodimerization activity [GO:00428... | PF02503;PF13090;PF17941;PF13089; | 3.30.870.10;3.30.1840.10;1.20.58.310; | Polyphosphate kinase 1 (PPK1) family | PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond. {ECO:0000255|HAMAP-Rule:MF_00347, ECO:0000269|PubMed:8962061}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1331061}; Peripheral membrane protein {ECO:0000269|PubMed:1331061}. Note=Associated with the outer membrane in overproducing cells. {ECO:0000269|PubMed:1331061}. | CATALYTIC ACTIVITY: Reaction=[phosphate](n) + ATP = [phosphate](n+1) + ADP; Xref=Rhea:RHEA:19573, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280, ChEBI:CHEBI:16838, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.4.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00347, ECO:0000269|PubMed:10660553, ECO:0000269|PubMed:1331061, ECO:00002... | null | null | null | null | FUNCTION: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Can form linear polymers of orthophosphate with chain lengths up to 1000 or more. Can use GTP instead of ATP, but the efficiency of GTP is 5% that of ATP. Also exhibits several other enzymatic activi... | Escherichia coli (strain K12) |
P0A7B3 | NADK_ECOLI | MNNHFKCIGIVGHPRHPTALTTHEMLYRWLCTKGYEVIVEQQIAHELQLKNVKTGTLAEIGQLADLAVVVGGDGNMLGAARTLARYDIKVIGINRGNLGFLTDLDPDNAQQQLADVLEGHYISEKRFLLEAQVCQQDCQKRISTAINEVVLHPGKVAHMIEFEVYIDEIFAFSQRSDGLIISTPTGSTAYSLSAGGPILTPSLDAITLVPMFPHTLSARPLVINSSSTIRLRFSHRRNDLEISCDSQIALPIQEGEDVLIRRCDYHLNLIHPKDYSYFNTLSTKLGWSKKLF | 2.7.1.23 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:11488932}; | NAD metabolic process [GO:0019674]; NADP biosynthetic process [GO:0006741]; phosphorylation [GO:0016310] | cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; NAD+ kinase activity [GO:0003951] | PF01513;PF20143; | null | NAD kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}. | CATALYTIC ACTIVITY: Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540, ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:15855156, ECO:0000269|PubMed:302... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mM for NAD (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:15855156, ECO:0000269|PubMed:3025169}; KM=2.5 mM for ATP (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:15855156, ECO:0000269|PubMed:30... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7.2 and 7.5. {ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:15855156, ECO:0000269|PubMed:3025169}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius and half of the activity is lost on treatment at 65 degrees Celsius for 10 minutes. {ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:15855156, ECO:0000269|PubMed:3025169}; | FUNCTION: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (UTP, CTP, GTP, dATP, TTP) as phos... | Escherichia coli (strain K12) |
P0A7B5 | PROB_ECOLI | MSDSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILAGADKLLLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKPGVIGDVMEGISVGTLFHAQATPLENRKRWIFGAPPAGEITVDEGATAAILERGSSLLPKGIKSVTGNFSRGEVIRICNLEG... | 2.7.2.11 | null | L-proline biosynthetic process [GO:0055129]; phosphorylation [GO:0016310]; proline biosynthetic process [GO:0006561] | cytosol [GO:0005829] | ATP binding [GO:0005524]; glutamate 5-kinase activity [GO:0004349]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; proline binding [GO:1901973]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723] | PF00696;PF01472; | 3.40.1160.10;2.30.130.10; | Glutamate 5-kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00456}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00456, ECO:0000269|PubMed:6319365}; | null | PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00456, ECO:0000269|PubMed:6319365}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:6319365}; | null | FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00456, ECO:0000269|PubMed:6319365}. | Escherichia coli (strain K12) |
P0A7B8 | HSLV_ECOLI | MTTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELAKDWRTDRMLRKLEALLAVADETASLIITGNGDVVQPENDLIAIGSGGPYAQAAARALLENTELSAREIAEKALDIAGDICIYTNHFHTIEELSYKA | 3.4.25.2 | null | cellular response to heat [GO:0034605]; protein denaturation [GO:0030164]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; response to heat [GO:0009408] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; HslUV protease complex [GO:0009376]; proteasome core complex [GO:0005839] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein domain specific binding [GO:0019904]; threonine-type endopeptidase activity [GO:0004298] | PF00227; | 3.60.20.10; | Peptidase T1B family, HslV subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP-dependent cleavage of peptide bonds with broad specificity.; EC=3.4.25.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00248, ECO:0000269|PubMed:10419524, ECO:0000269|PubMed:10452560, ECO:0000269|PubMed:8650174, ECO:0000269|PubMed:9288941, ECO:0000269|PubMed:9393683}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.2 uM for Arc-MYL-st11 (at 37 degrees Celsius) {ECO:0000269|PubMed:15696175}; Note=Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:15696175}; | FUNCTION: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed b... | Escherichia coli (strain K12) |
P0A7C2 | LEXA_ECOLI | MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL | 3.4.21.88 | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; negative regulation of DNA-templated transcription [GO:0045892]; proteolysis [GO:0006508]; SOS response [GO:0009432] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | DNA binding [GO:0003677]; DNA-binding transcription repressor activity [GO:0001217]; identical protein binding [GO:0042802]; serine-type endopeptidase activity [GO:0004252]; transcription cis-regulatory region binding [GO:0000976] | PF01726;PF00717; | 2.10.109.10;1.10.10.10; | Peptidase S24 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Ala-|-Gly bond in repressor LexA.; EC=3.4.21.88; Evidence={ECO:0000255|HAMAP-Rule:MF_00015}; | null | null | null | null | FUNCTION: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of ... | Escherichia coli (strain K12) |
P0A7D4 | PURA_ECOLI | MGNNVVVLGTQWGDEGKGKIVDLLTERAKYVVRYQGGHNAGHTLVINGEKTVLHLIPSGILRENVTSIIGNGVVLSPAALMKEMKELEDRGIPVRERLLLSEACPLILDYHVALDNAREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAEAVDYQKVLDDTMAVADILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGILKAYSTRVGAGPFPTELFDETGEFLCKQGNEFGATTGRRRRTGWLDTVAVRRAV... | 6.3.4.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; | 'de novo' AMP biosynthetic process [GO:0044208]; adenosine biosynthetic process [GO:0046086]; DNA damage response [GO:0006974]; IMP metabolic process [GO:0046040]; nucleobase-containing small molecule interconversion [GO:0015949]; purine nucleotide biosynthetic process [GO:0006164] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | adenylosuccinate synthase activity [GO:0004019]; GTP binding [GO:0005525]; guanosine tetraphosphate binding [GO:0097216]; magnesium ion binding [GO:0000287] | PF00709; | 3.40.440.10;1.10.300.10;3.90.170.10; | Adenylosuccinate synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-Rule:MF_0001... | null | PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00011}. | null | null | FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. | Escherichia coli (strain K12) |
P0A7E1 | PYRD_ECOLI | MYYPFVRKALFQLDPERAHEFTFQQLRRITGTPFEALVRQKVPAKPVNCMGLTFKNPLGLAAGLDKDGECIDALGAMGFGSIEIGTVTPRPQPGNDKPRLFRLVDAEGLINRMGFNNLGVDNLVENVKKAHYDGVLGINIGKNKDTPVEQGKDDYLICMEKIYAYAGYIAINISSPNTPGLRTLQYGEALDDLLTAIKNKQNDLQAMHHKYVPIAVKIAPDLSEEELIQVADSLVRHNIDGVIATNTTLDRSLVQGMKNCDQTGGLSGRPLQLKSTEIIRRLSLELNGRLPIIGVGGIDSVIAAREKIAAGASLVQIYSG... | 1.3.5.2 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:12220493}; Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:12220493}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; pyrimidine ribonucleotide biosynthetic process [GO:0009220] | cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886] | dihydroorotate dehydrogenase (quinone) activity [GO:0106430]; dihydroorotate dehydrogenase activity [GO:0004152]; FMN binding [GO:0010181] | PF01180; | 3.20.20.70; | Dihydroorotate dehydrogenase family, Type 2 subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; Evidence={ECO:0000269|PubMed:10074342}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28.8 uM for dihydroorotate {ECO:0000269|PubMed:10074342}; Vmax=180 umol/min/mg enzyme {ECO:0000269|PubMed:10074342}; | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. | null | null | FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000269|PubMed:10074342}. | Escherichia coli (strain K12) |
P0A7E3 | PYRE_ECOLI | MKPYQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTAVALAEHHDLDLPYCFNRKEAKDHGEGGNLVGSALQGRVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISAIQEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYREEFGV | 2.4.2.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01208}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; pyrimidine nucleotide biosynthetic process [GO:0006221]; pyrimidine ribonucleoside biosynthetic process [GO:0046132] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | magnesium ion binding [GO:0000287]; orotate phosphoribosyltransferase activity [GO:0004588]; protein homodimerization activity [GO:0042803] | PF00156; | 3.40.50.2020; | Purine/pyrimidine phosphoribosyltransferase family, PyrE subfamily | null | null | CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208}; | null | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01208}. | null | null | FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000269|PubMed:8620002}. | Escherichia coli (strain K12) |
P0A7E5 | PYRG_ECOLI | MTTNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAVEIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR... | 6.3.4.2 | null | 'de novo' CTP biosynthetic process [GO:0044210]; CTP biosynthetic process [GO:0006241]; glutamine metabolic process [GO:0006541]; protein homotetramerization [GO:0051289]; pyrimidine nucleobase biosynthetic process [GO:0019856] | cytoophidium [GO:0097268]; cytosol [GO:0005829]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; CTP synthase activity [GO:0003883]; glutaminase activity [GO:0004359]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287] | PF06418;PF00117; | 3.40.50.880;3.40.50.300; | CTP synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32507415}. Note=Localizes to the cytoophidium, a subcellular filamentary structure where CTP synthase is compartmentalized. Many cells form cytoophidia which are observed in stationary phase. {ECO:0000269|PubMed:32507415}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2; Evidenc... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mM for ammonia {ECO:0000269|PubMed:11336655}; KM=0.3 mM for L-glutamine (in the presence of 0.25 mM GTP) {ECO:0000269|PubMed:11336655}; Note=kcat is 13 sec(-1) with ammonia as substrate. kcat is 6.6 sec(-1) with L-glutamine as substrate (in the presence of 0.25 m... | PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01227}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.7. {ECO:0000269|PubMed:8385490}; | null | FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. {ECO:0000269|PubMed:11336655, ECO:0000269|PubMed:8385490, ECO:0000305|PubMed:15157079}. | Escherichia coli (strain K12) |
P0A7E9 | PYRH_ECOLI | MATNAKPVYKRILLKLSGEALQGTEGFGIDASILDRMAQEIKELVELGIQVGVVIGGGNLFRGAGLAKAGMNRVVGDHMGMLATVMNGLAMRDALHRAYVNARLMSAIPLNGVCDSYSWAEAISLLRNNRVVILSAGTGNPFFTTDSAACLRGIEIEADVVLKATKVDGVFTADPAKDPTATMYEQLTYSEVLEKELKVMDLAAFTLARDHKLPIRVFNMNKPGALRRVVMGEKEGTLITE | 2.7.4.22 | null | 'de novo' CTP biosynthetic process [GO:0044210]; phosphorylation [GO:0016310]; pyrimidine nucleotide biosynthetic process [GO:0006221]; UDP biosynthetic process [GO:0006225] | cytosol [GO:0005829] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; UMP kinase activity [GO:0033862] | PF00696; | 3.40.1160.10; | UMP kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9922246}. Note=Is predominantly localized near the bacterial membranes. | CATALYTIC ACTIVITY: Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.22; Evidence={ECO:0000269|PubMed:17210578}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=210 uM for ATP (in the presence of 0.3 mM UMP) {ECO:0000269|PubMed:17210578}; KM=50 uM for UMP (in the presence of 0.2 mM ATP) {ECO:0000269|PubMed:17210578}; Vmax=62.4 umol/min/mg enzyme with ATP as substrate (in the presence of 0.3 mM UMP) {ECO:0000269|PubMed:1721... | PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1. {ECO:0000269|PubMed:17210578}. | null | null | FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP, with ATP as the most efficient phosphate donor. {ECO:0000269|PubMed:7711027}. | Escherichia coli (strain K12) |
P0A7F6 | SPED_ECOLI | MKKLKLHGFNNLTKSLSFCIYDICYAKTAEERDGYIAYIDELYNANRLTEILSETCSIIGANILNIARQDYEPQGASVTILVSEEPVDPKLIDKTEHPGPLPETVVAHLDKSHICVHTYPESHPEGGLCTFRADIEVSTCGVISPLKALNYLIHQLESDIVTIDYRVRGFTRDINGMKHFIDHEINSIQNFMSDDMKALYDMVDVNVYQENIFHTKMLLKEFDLKHYMFHTKPEDLTDSERQEITAALWKEMREIYYGRNMPAV | 4.1.1.50 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000269|PubMed:3316212, ECO:0000269|PubMed:3546296, ECO:0000269|PubMed:6749853}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000269|PubMed:3316212, ECO:0000269|PubMed:3546296, ECO:0000269|PubMed:6749853}; | self proteolysis [GO:0097264]; spermidine biosynthetic process [GO:0008295] | cytosol [GO:0005829] | adenosylmethionine decarboxylase activity [GO:0004014]; magnesium ion binding [GO:0000287] | PF02675; | 3.60.90.10; | Prokaryotic AdoMetDC family, Type 2 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... | null | CATALYTIC ACTIVITY: Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50; Evidence={ECO:0000269|PubMed:6749853}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 uM for S-adenosyl-L-methionine (at 25 degrees Celsius in the presence of 0.01 M MgCl(2)) {ECO:0000269|PubMed:6749853}; Vmax=3.8 umol/min/mg enzyme (at 25 degrees Celsius in the presence of 0.01M MgCl(2)) {ECO:0000269|PubMed:6749853}; Vmax=6.8 umol/min/mg enzyme ... | PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. Active from pH 6.7 to 8.5. {ECO:0000269|PubMed:17567041, ECO:0000269|PubMed:6749853}; | null | FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. | Escherichia coli (strain K12) |
P0A7F9 | QUEA_ECOLI | MRVTDFSFELPESLIAHYPMPERSSCRLLSLDGPTGALTHGTFTDLLDKLNPGDLLVFNNTRVIPARLFGRKASGGKIEVLVERMLDDKRILAHIRASKAPKPGAELLLGDDESINATMTARHGALFEVEFNDERSVLDILNSIGHMPLPPYIDRPDEDADRELYQTVYSEKPGAVAAPTAGLHFDEPLLEKLRAKGVEMAFVTLHVGAGTFQPVRVDTIEDHIMHSEYAEVPQDVVDAVLAAKARGNRVIAVGTTSVRSLESAAQAAKNDLIEPFFDDTQIFIYPGFQYKVVDALVTNFHLPESTLIMLVSAFAGYQHT... | 2.4.99.17 | null | queuosine biosynthetic process [GO:0008616]; response to radiation [GO:0009314]; tRNA wobble guanine modification [GO:0002099] | cytosol [GO:0005829] | S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity [GO:0051075] | PF02547; | 2.40.10.240;3.40.1780.10; | QueA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine; Xref=Rhea:RHEA:32155, Rhea:RHEA-COMP:10342, Rhea:RHEA-COMP:18582, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:8283... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=98 uM for S-adenosylmethionine {ECO:0000269|PubMed:12731872}; KM=1.9 uM for 7-(aminomethyl)-7-deazaguanosine {ECO:0000269|PubMed:12731872}; | PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. | null | null | FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | Escherichia coli (strain K12) |
P0A7G2 | RBFA_ECOLI | MAKEFGRPQRVAQEMQKEIALILQREIKDPRLGMMTTVSGVEMSRDLAYAKVYVTFLNDKDEDAVKAGIKALQEASGFIRSLLGKAMRLRIVPELTFFYDNSLVEGMRMSNLVTSVVKHDEERRVNPDDSKED | null | null | DNA damage response [GO:0006974]; maturation of SSU-rRNA [GO:0030490]; response to cold [GO:0009409]; ribosomal small subunit biogenesis [GO:0042274]; ribosome biogenesis [GO:0042254] | cytosol [GO:0005829] | ribosomal small subunit binding [GO:0043024] | PF02033; | 3.30.300.20; | RbfA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00003, ECO:0000269|PubMed:12963368, ECO:0000269|PubMed:7535280}. Note=About 1/3 associates with free 30S ribosomal subunits at 37 degrees Celsius, 6 hours after a 15 degrees Celsius cold-shock about 4-fold more protein is associated with 30S ribosomes (PubMed:1... | null | null | null | null | null | FUNCTION: One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late maturation steps of the functional core of the 30S subunit. Essential for efficient processing of pre-16S rRNA (PubMed:12628255, PubMed:12963368, PubMed:9422595). Probably part of the 30S subunit prior to or during the final st... | Escherichia coli (strain K12) |
P0A7G6 | RECA_ECOLI | MAIDENKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGKTCAFIDAEHALDPIYARKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAVKEGENVVGSETRVKVVKNKIAAPFKQAEFQILYGEGINFYGELVDLGVKEKLIEKAGAWYSYKGEKIGQGKANATAWLKDNPETAKEI... | null | null | cell motility [GO:0048870]; DNA damage response [GO:0006974]; DNA recombination [GO:0006310]; homologous recombination [GO:0035825]; recombinational repair [GO:0000725]; response to ionizing radiation [GO:0010212]; SOS response [GO:0009432]; translesion synthesis [GO:0019985] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; DNA polymerase V complex [GO:0009355] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent DNA damage sensor activity [GO:0140664]; damaged DNA binding [GO:0003684]; DNA-binding transcription factor binding [GO:0140297]; single-stranded DNA binding [GO:0003697] | PF00154;PF21096; | 3.40.50.300; | RecA family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Required for homologous recombination and the bypass of mutagenic DNA lesions by the SOS response. Catalyzes ATP-driven homologous pairing and strand exchange of DNA molecules necessary for DNA recombinational repair. Catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent up... | Escherichia coli (strain K12) |
P0A7I4 | RF3_ECOLI | MTLSPYLQEVAKRRTFAIISHPDAGKTTITEKVLLFGQAIQTAGTVKGRGSNQHAKSDWMEMEKQRGISITTSVMQFPYHDCLVNLLDTPGHEDFSEDTYRTLTAVDCCLMVIDAAKGVEDRTRKLMEVTRLRDTPILTFMNKLDRDIRDPMELLDEVENELKIGCAPITWPIGCGKLFKGVYHLYKDETYLYQSGKGHTIQEVRIVKGLNNPDLDAAVGEDLAQQLRDELELVKGASNEFDKELFLAGEITPVFFGTALGNFGVDHMLDGLVEWAPAPMPRQTDTRTVEASEDKFTGFVFKIQANMDPKHRDRVAFMRV... | null | null | maintenance of translational fidelity [GO:1990145]; regulation of translational termination [GO:0006449]; translational termination [GO:0006415] | cytosol [GO:0005829] | GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; translation release factor activity, codon nonspecific [GO:0016150]; translation release factor activity, codon specific [GO:0016149] | PF00009;PF03144;PF16658; | 3.40.50.300;3.30.70.3280; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, PrfC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GM... | Escherichia coli (strain K12) |
P0A7I7 | RIBA_ECOLI | MQLKRVAEAKLPTPWGDFLMVGFEELATGHDHVALVYGDISGHTPVLARVHSECLTGDALFSLRCDCGFQLEAALTQIAEEGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLGVNEVRLLTNNPKKVEILTEAGINIVERVPLIVGRNPNNEHYLDTKAEKMGHLLNK | 3.5.4.25 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12392559, ECO:0000269|PubMed:235552}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12392559, ECO:0000269|PubMed:235552}; | riboflavin biosynthetic process [GO:0009231] | cytosol [GO:0005829] | 3,4-dihydroxy-2-butanone-4-phosphate synthase activity [GO:0008686]; GTP binding [GO:0005525]; GTP cyclohydrolase II activity [GO:0003935]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF00925; | 3.40.50.10990; | GTP cyclohydrolase II family | null | null | CATALYTIC ACTIVITY: Reaction=GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate; Xref=Rhea:RHEA:23704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58614; EC=3.5.4.25; Evidence={ECO:0000269|PubMed:832022... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=41 uM for GTP {ECO:0000269|PubMed:235552}; | PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:235552}; | null | FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. {ECO:0000269|PubMed:235552}. | Escherichia coli (strain K12) |
P0A7J0 | RIBB_ECOLI | MNQTLLSSFGTPFERVENALAALREGRGVMVLDDEDRENEGDMIFPAETMTVEQMALTIRHGSGIVCLCITEDRRKQLDLPMMVENNTSAYGTGFTVTIEAAEGVTTGVSAADRITTVRAAIADGAKPSDLNRPGHVFPLRAQAGGVLTRGGHTEATIDLMTLAGFKPAGVLCELTNDDGTMARAPECIEFANKHNMALVTIEDLVAYRQAHERKAS | 4.1.99.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11687623}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_00180}; Note=Binds 2 divalent metal cations per subunit. Magnesium or manganese. {ECO:0000269|PubMed:11687623}; | riboflavin biosynthetic process [GO:0009231] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | 3,4-dihydroxy-2-butanone-4-phosphate synthase activity [GO:0008686]; GTP cyclohydrolase II activity [GO:0003935]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; protein homodimerization activity [GO:0042803] | PF00926; | 3.90.870.10; | DHBP synthase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+); Xref=Rhea:RHEA:18457, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, ChEBI:CHEBI:58830; EC=4.1.99.12; Evidence={ECO:0000269|PubMed:1597419}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18458; E... | null | PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. | null | null | FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. {ECO:0000269|PubMed:1597419}. | Escherichia coli (strain K12) |
P0A7J3 | RL10_ECOLI | MALNLQDKQAIVAEVSEVAKGALSAVVADSRGVTVDKMTELRKAGREAGVYMRVVRNTLLRRAVEGTPFECLKDAFVGPTLIAYSMEHPGAAARLFKEFAKANAKFEVKAAAFEGELIPASQIDRLATLPTYEEAIARLMATMKEASAGKLVRTLAAVRDAKEAA | null | null | cytoplasmic translation [GO:0002181]; negative regulation of translation [GO:0017148]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; large ribosomal subunit [GO:0015934] | large ribosomal subunit rRNA binding [GO:0070180]; ribosome binding [GO:0043022]; structural constituent of ribosome [GO:0003735] | PF00466; | 3.30.70.1730;6.10.250.2350; | Universal ribosomal protein uL10 family | null | null | null | null | null | null | null | FUNCTION: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. {ECO:0000269|PubMed:15923259}.; FUNCTION: Protein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA. {ECO:0... | Escherichia coli (strain K12) |
P0A7J7 | RL11_ECOLI | MAKKVQAYVKLQVAAGMANPSPPVGPALGQQGVNIMEFCKAFNAKTDSIEKGLPIPVVITVYADRSFTFVTKTPPAAVLLKKAAGIKSGSGKPNKDKVGKISRAQLQEIAQTKAADMTGADIEAMTRSIEGTARSMGLVVED | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit assembly [GO:0000027]; stringent response [GO:0015968]; translation [GO:0006412]; translational termination [GO:0006415] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | large ribosomal subunit rRNA binding [GO:0070180]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00298;PF03946; | 1.10.10.250;3.30.1550.10; | Universal ribosomal protein uL11 family | null | null | null | null | null | null | null | FUNCTION: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Escherichia coli (strain K12) |
P0A7K2 | RL7_ECOLI | MSITKDQIIEAVAAMSVMDVVELISAMEEKFGVSAAAAVAVAAGPVEAAEEKTEFDVILKAAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGVSKDDAEALKKALEEAGAEVEVK | null | null | cytoplasmic translation [GO:0002181]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; large ribosomal subunit [GO:0015934] | mRNA binding [GO:0003729]; protein homodimerization activity [GO:0042803]; ribosome binding [GO:0043022]; structural constituent of ribosome [GO:0003735] | PF00542;PF16320; | 3.30.1390.10;1.20.5.710; | Bacterial ribosomal protein bL12 family | PTM: Acetylation of Ser-2 converts L12 to L7.; PTM: Lys-82 was found to be 50% monomethylated. {ECO:0000269|PubMed:4573678}. | null | null | null | null | null | null | FUNCTION: The binding site for several of the GTPase factors involved in protein synthesis (IF-2, EF-Tu, EF-G and RF3). Is thus essential for accurate translation. Deletion of 1 of the L12 dimers from the ribosome (by deleting the binding site on L10) leads to decreased IF-2 association with the 70S ribosome and decrea... | Escherichia coli (strain K12) |
P0A7K6 | RL19_ECOLI | MSNIIKQLEQEQMKQDVPSFRPGDTVEVKVWVVEGSKKRLQAFEGVVIAIRNRGLHSAFTVRKISNGEGVERVFQTHSPVVDSISVKRRGAVRKAKLYYLRERTGKAARIKERLN | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit assembly [GO:0000027] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | large ribosomal subunit rRNA binding [GO:0070180]; structural constituent of ribosome [GO:0003735] | PF01245; | 2.30.30.790; | Bacterial ribosomal protein bL19 family | null | null | null | null | null | null | null | FUNCTION: This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8 (PubMed:12809609). In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16... | Escherichia coli (strain K12) |
P0A7L0 | RL1_ECOLI | MAKLTKRMRVIREKVDATKQYDINEAIALLKELATAKFVESVDVAVNLGIDARKSDQNVRGATVLPHGTGRSVRVAVFTQGANAEAAKAAGAELVGMEDLADQIKKGEMNFDVVIASPDAMRVVGQLGQVLGPRGLMPNPKVGTVTPNVAEAVKNAKAGQVRYRNDKNGIIHTTIGKVDFDADKLKENLEALLVALKKAKPTQAKGVYIKKVSISTTMGAGVAVDQAGLSASVN | null | null | cytoplasmic translation [GO:0002181]; negative regulation of translational initiation [GO:0045947]; ribosomal large subunit assembly [GO:0000027] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049] | PF00687; | 3.30.190.20;3.40.50.790; | Universal ribosomal protein uL1 family | null | null | null | null | null | null | null | FUNCTION: One of the primary rRNA binding proteins, it binds very close to the 3'-end of the 23S rRNA. Forms part of the L1 stalk. It is often not seen in high-resolution crystal structures, but can be seen in cryo_EM and 3D reconstruction models. These indicate that the distal end of the stalk moves by approximately 2... | Escherichia coli (strain K12) |
P0A7L3 | RL20_ECOLI | MARVKRGVIARARHKKILKQAKGYYGARSRVYRVAFQAVIKAGQYAYRDRRQRKRQFRQLWIARINAAARQNGISYSKFINGLKKASVEIDRKILADIAVFDKVAFTALVEKAKAALA | null | null | cytoplasmic translation [GO:0002181] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | large ribosomal subunit rRNA binding [GO:0070180]; mRNA binding [GO:0003729]; mRNA regulatory element binding translation repressor activity [GO:0000900]; structural constituent of ribosome [GO:0003735] | PF00453; | 6.10.160.10;1.10.1900.20; | Bacterial ribosomal protein bL20 family | null | null | null | null | null | null | null | FUNCTION: One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. {ECO:0000269|PubMed:3298242}. | Escherichia coli (strain K12) |
P0A7L8 | RL27_ECOLI | MAHKKAGGSTRNGRDSEAKRLGVKRFGGESVLAGSIIVRQRGTKFHAGANVGCGRDHTLFAKADGKVKFEVKGPKNRKFISIEAE | null | null | assembly of large subunit precursor of preribosome [GO:1902626]; cytoplasmic translation [GO:0002181]; cytosolic ribosome assembly [GO:0042256]; positive regulation of ribosome biogenesis [GO:0090070]; regulation of cell growth [GO:0001558]; ribosomal large subunit assembly [GO:0000027] | cytoplasm [GO:0005737]; cytosolic large ribosomal subunit [GO:0022625] | ribosome binding [GO:0043022]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049] | PF01016; | 2.40.50.100; | Bacterial ribosomal protein bL27 family | null | null | null | null | null | null | null | null | Escherichia coli (strain K12) |
P0A7M2 | RL28_ECOLI | MSRVCQVTGKRPVTGNNRSHALNATKRRFLPNLHSHRFWVESEKRFVTLRVSAKGMRVIDKKGIDTVLAELRARGEKY | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit assembly [GO:0000027] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00830; | 2.30.170.40; | Bacterial ribosomal protein bL28 family | null | null | null | null | null | null | null | null | Escherichia coli (strain K12) |
P0A7M6 | RL29_ECOLI | MKAKELREKSVEELNTELLNLLREQFNLRMQAASGQLQQSHLLKQVRRDVARVKTLLNEKAGA | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit assembly [GO:0000027] | cytoplasm [GO:0005737]; cytosolic large ribosomal subunit [GO:0022625] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00831; | 6.10.140.1970; | Universal ribosomal protein uL29 family | null | null | null | null | null | null | null | FUNCTION: Binds 23S rRNA. It is not essential for growth. {ECO:0000269|PubMed:12226666, ECO:0000269|PubMed:6170935}.; FUNCTION: One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666). {ECO:0000269|PubMed:12226666}. | Escherichia coli (strain K12) |
P0A7M9 | RL31_ECOLI | MKKDIHPKYEEITASCSCGNVMKIRSTVGHDLNLDVCSKCHPFFTGKQRDVATGGRVDRFNKRFNIPGSK | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:22196016}; Note=Binds 1 zinc ion per subunit. Only 1 ligand appears to be Cys, the other are thought to be His and either backbone amides or solvent (PubMed:22196016). {ECO:0000269|PubMed:22196016}; | cytoplasmic translation [GO:0002181]; negative regulation of cytoplasmic translational initiation [GO:1904689]; translation [GO:0006412]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]; zinc ion binding [GO:0008270] | PF01197; | 4.10.830.30; | Bacterial ribosomal protein bL31 family, Type A subfamily | PTM: Proteolytically cleaved by protease VII to yield a peptide lacking residues 63-70. It is not clear if this is due to protein degradation or is a bona fide processing event in the strain used in PubMed:339950 and PubMed:10556732. In strains B, D10, MRE-600 and Q13 the only protein seen in PubMed:10556732 was full-l... | null | null | null | null | null | null | FUNCTION: Binds the 23S rRNA. {ECO:0000250}. | Escherichia coli (strain K12) |
P0A7N4 | RL32_ECOLI | MAVQQNKPTRSKRGMRRSHDALTAVTSLSVDKTSGEKHLRHHITADGYYRGRKVIAK | null | null | cytoplasmic translation [GO:0002181]; response to radiation [GO:0009314]; response to reactive oxygen species [GO:0000302]; ribosomal large subunit assembly [GO:0000027] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | structural constituent of ribosome [GO:0003735] | PF01783; | null | Bacterial ribosomal protein bL32 family | null | null | null | null | null | null | null | null | Escherichia coli (strain K12) |
P0A7N9 | RL33_ECOLI | MAKGIREKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAKIK | null | null | cytoplasmic translation [GO:0002181]; response to antibiotic [GO:0046677]; ribosomal large subunit assembly [GO:0000027] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049] | PF00471; | 2.20.28.120; | Bacterial ribosomal protein bL33 family | null | null | null | null | null | null | null | null | Escherichia coli (strain K12) |
P0A7R1 | RL9_ECOLI | MQVILLDKVANLGSLGDQVNVKAGYARNFLVPQGKAVPATKKNIEFFEARRAELEAKLAEVLAAANARAEKINALETVTIASKAGDEGKLFGSIGTRDIADAVTAAGVEVAKSEVRLPNGVLRTTGEHEVSFQVHSEVFAKVIVNVVAE | null | null | cytoplasmic translation [GO:0002181] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | large ribosomal subunit rRNA binding [GO:0070180]; structural constituent of ribosome [GO:0003735] | PF03948;PF01281; | 3.10.430.100;3.40.5.10; | Bacterial ribosomal protein bL9 family | null | null | null | null | null | null | null | FUNCTION: One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA. {ECO:0000269|PubMed:3298242}. | Escherichia coli (strain K12) |
P0A7R5 | RS10_ECOLI | MQNQRIRIRLKAFDHRLIDQATAEIVETAKRTGAQVRGPIPLPTRKERFTVLISPHVNKDARDQYEIRTHLRLVDIVEPTEKTVDALMRLDLAAGVDVQISLG | null | null | cytoplasmic translation [GO:0002181]; regulation of DNA-templated transcription elongation [GO:0032784]; ribosome biogenesis [GO:0042254]; transcription antitermination [GO:0031564] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; small ribosomal subunit [GO:0015935]; transcription elongation factor complex [GO:0008023] | structural constituent of ribosome [GO:0003735]; transcription antitermination factor activity, RNA binding [GO:0001072]; tRNA binding [GO:0000049] | PF00338; | 3.30.70.600; | Universal ribosomal protein uS10 family | null | null | null | null | null | null | null | FUNCTION: Involved in the binding of tRNA to the ribosomes (PubMed:6759118). Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, c... | Escherichia coli (strain K12) |
P0A7R9 | RS11_ECOLI | MAKAPIRARKRVRKQVSDGVAHIHASFNNTIVTITDRQGNALGWATAGGSGFRGSRKSTPFAAQVAAERCADAVKEYGIKNLEVMVKGPGPGRESTIRALNAAGFRITNITDVTPIPHNGCRPPKKRRV | null | null | cytoplasmic translation [GO:0002181]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | small ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735] | PF00411; | 3.30.420.80; | Universal ribosomal protein uS11 family | null | null | null | null | null | null | null | FUNCTION: Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome (By similarity). {ECO:0000250}. | Escherichia coli (strain K12) |
P0A7S3 | RS12_ECOLI | MATVNQLVRKPRARKVAKSNVPALEACPQKRGVCTRVYTTTPKKPNSALRKVCRVRLTNGFEVTSYIGGEGHNLQEHSVILIRGGRVKDLPGVRYHTVRGALDCSGVKDRKQARSKYGVKRPKA | null | null | cytoplasmic translation [GO:0002181]; Group I intron splicing [GO:0000372]; maintenance of translational fidelity [GO:1990145]; positive regulation of RNA splicing [GO:0033120]; response to antibiotic [GO:0046677]; RNA folding [GO:0034337]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; ribosome [GO:0005840] | misfolded RNA binding [GO:0034336]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049] | PF00164; | 2.40.50.140; | Universal ribosomal protein uS12 family | null | null | null | null | null | null | null | FUNCTION: With S4 and S5 plays an important role in translational accuracy.; FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacti... | Escherichia coli (strain K12) |
P0A7S9 | RS13_ECOLI | MARIAGINIPDHKHAVIALTSIYGVGKTRSKAILAAAGIAEDVKISELSEGQIDTLRDEVAKFVVEGDLRREISMSIKRLMDLGCYRGLRHRRGLPVRGQRTKTNARTRKGPRKPIKK | null | null | cytoplasmic translation [GO:0002181] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; small ribosomal subunit [GO:0015935] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049] | PF00416; | 1.10.8.50;4.10.910.10; | Universal ribosomal protein uS13 family | null | null | null | null | null | null | null | FUNCTION: Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. {ECO:0000269|PubMed:15308780}.; FUNCTION: In the E.coli 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connec... | Escherichia coli (strain K12) |
P0A7T3 | RS16_ECOLI | MVTIRLARHGAKKRPFYQVVVADSRNARNGRFIERVGFFNPIASEKEEGTRLDLDRIAHWVGQGATISDRVAALIKEVNKAA | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028] | cytoplasm [GO:0005737]; cytosolic small ribosomal subunit [GO:0022627]; small ribosomal subunit [GO:0015935] | DNA endonuclease activity [GO:0004520]; four-way junction DNA binding [GO:0000400]; structural constituent of ribosome [GO:0003735] | PF00886; | 3.30.1320.10; | Bacterial ribosomal protein bS16 family | null | null | null | null | null | null | null | FUNCTION: In addition to being a ribosomal protein, S16 also has a cation-dependent endonuclease activity. {ECO:0000269|PubMed:8730873}.; FUNCTION: In-frame fusions with the ribosome maturation factor rimM suppress mutations in the latter (probably due to increased rimM expression) and are found in translationally acti... | Escherichia coli (strain K12) |
P0A7T7 | RS18_ECOLI | MARYFRRRKFCRFTAEGVQEIDYKDIATLKNYITESGKIVPSRITGTRAKYQRQLARAIKRARYLSLLPYTDRHQ | null | null | cytoplasmic translation [GO:0002181]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | mRNA 5'-UTR binding [GO:0048027]; small ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735] | PF01084; | 4.10.640.10; | Bacterial ribosomal protein bS18 family | null | null | null | null | null | null | null | FUNCTION: Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. | Escherichia coli (strain K12) |
P0A7U3 | RS19_ECOLI | MPRSLKKGPFIDLHLLKKVEKAVESGDKKPLRTWSRRSTIFPNMIGLTIAVHNGRQHVPVFVTDEMVGHKLGEFAPTRTYRGHAADKKAKKK | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049] | PF00203; | null | Universal ribosomal protein uS19 family | null | null | null | null | null | null | null | FUNCTION: In the E.coli 70S ribosome in the initiation state (PubMed:12809609) it has been modeled to contact the 23S rRNA of the 50S subunit forming part of bridge B1a; this bridge is broken in the model with bound EF-G. The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (PubMed... | Escherichia coli (strain K12) |
P0A7U7 | RS20_ECOLI | MANIKSAKKRAIQSEKARKHNASRRSMMRTFIKKVYAAIEAGDKAAAQKAFNEMQPIVDRQAAKGLIHKNKAARHKANLTAQINKLA | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; small ribosomal subunit [GO:0015935] | ornithine decarboxylase inhibitor activity [GO:0008073]; small ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735] | PF01649; | 1.20.58.110; | Bacterial ribosomal protein bS20 family | null | null | null | null | null | null | null | FUNCTION: Binds directly to 16S ribosomal RNA. | Escherichia coli (strain K12) |
P0A7V0 | RS2_ECOLI | MATVSMRDMLKAGVHFGHQTRYWNPKMKPFIFGARNKVHIINLEKTVPMFNEALAELNKIASRKGKILFVGTKRAASEAVKDAALSCDQFFVNHRWLGGMLTNWKTVRQSIKRLKDLETQSQDGTFDKLTKKEALMRTRELEKLENSLGGIKDMGGLPDALFVIDADHEHIAIKEANNLGIPVFAIVDTNSDPDGVDFVIPGNDDAIRAVTLYLGAVAATVREGRSQDLASQAEESFVEAE | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028] | cytoplasm [GO:0005737]; cytosolic small ribosomal subunit [GO:0022627] | structural constituent of ribosome [GO:0003735]; zinc ion binding [GO:0008270] | PF00318; | 1.10.287.610; | Universal ribosomal protein uS2 family | null | null | null | null | null | null | null | FUNCTION: Required for ribosomal protein S1 to bind to the 30S subunit. {ECO:0000269|PubMed:12068815}. | Escherichia coli (strain K12) |
P0A7V3 | RS3_ECOLI | MGQKVHPNGIRLGIVKPWNSTWFANTKEFADNLDSDFKVRQYLTKELAKASVSRIVIERPAKSIRVTIHTARPGIVIGKKGEDVEKLRKVVADIAGVPAQINIAEVRKPELDAKLVADSITSQLERRVMFRRAMKRAVQNAMRLGAKGIKVEVSGRLGGAEIARTEWYREGRVPLHTLRADIDYNTSEAHTTYGVIGVKVWIFKGEILGGMAAVEQPEKPAAQPKKQQRKGRK | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | mRNA binding [GO:0003729]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF07650;PF00189; | 3.30.300.20;3.30.1140.32; | Universal ribosomal protein uS3 family | null | null | null | null | null | null | null | FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation (By similarity). {ECO:0000250}.; FUNCTION: Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp. {ECO:0000269|PubMed:15652481}. | Escherichia coli (strain K12) |
P0A7V8 | RS4_ECOLI | MARYLGPKLKLSRREGTDLFLKSGVRAIDTKCKIEQAPGQHGARKPRLSDYGVQLREKQKVRRIYGVLERQFRNYYKEAARLKGNTGENLLALLEGRLDNVVYRMGFGATRAEARQLVSHKAIMVNGRVVNIASYQVSPNDVVSIREKAKKQSRVKAALELAEQREKPTWLEVDAGKMEGTFKRKPERSDLSADINEHLIVELYSK | null | null | cytoplasmic translation [GO:0002181]; DNA-templated transcription termination [GO:0006353]; maintenance of translational fidelity [GO:1990145]; negative regulation of translational initiation [GO:0045947]; response to antibiotic [GO:0046677]; ribosomal small subunit assembly [GO:0000028]; ribosomal small subunit biogen... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; small ribosomal subunit [GO:0015935] | mRNA 5'-UTR binding [GO:0048027]; mRNA regulatory element binding translation repressor activity [GO:0000900]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00163;PF01479; | 3.10.290.10; | Universal ribosomal protein uS4 family | null | null | null | null | null | null | null | FUNCTION: One of two assembly initiator proteins for the 30S subunit, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. {ECO:0000269|PubMed:2461734}.; FUNCTION: With S5 and S12 plays an important role in translational accuracy; many suppressors of streptomycin-dependent mutants o... | Escherichia coli (strain K12) |
P0A7W1 | RS5_ECOLI | MAHIEKQAGELQEKLIAVNRVSKTVKGGRIFSFTALTVVGDGNGRVGFGYGKAREVPAAIQKAMEKARRNMINVALNNGTLQHPVKGVHTGSRVFMQPASEGTGIIAGGAMRAVLEVAGVHNVLAKAYGSTNPINVVRATIDGLENMNSPEMVAAKRGKSVEEILGK | null | null | cytoplasmic translation [GO:0002181]; maintenance of translational fidelity [GO:1990145]; response to antibiotic [GO:0046677]; ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00333;PF03719; | 3.30.160.20;3.30.230.10; | Universal ribosomal protein uS5 family | null | null | null | null | null | null | null | FUNCTION: With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations). {ECO:0000269|PubMed:15652481}.; FUNCTION: Located at t... | Escherichia coli (strain K12) |
P0A7W7 | RS8_ECOLI | MSMQDPIADMLTRIRNGQAANKAAVTMPSSKLKVAIANVLKEEGFIEDFKVEGDTKPELELTLKYFQGKAVVESIQRVSRPGLRIYKRKDELPKVMAGLGIAVVSTSKGVMTDRAARQAGLGGEIICYVA | null | null | cytoplasmic translation [GO:0002181]; regulation of mRNA stability [GO:0043488]; regulation of translation [GO:0006417]; ribosomal small subunit assembly [GO:0000028] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00410; | 3.30.1370.30;3.30.1490.10; | Universal ribosomal protein uS8 family | null | null | null | null | null | null | null | FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. {ECO:0000250}.; FUNCTION: Protein S8 is a translational repressor protein, it controls the translation of the spc operon by binding to its mRNA. {ECO:00... | Escherichia coli (strain K12) |
P0A7X3 | RS9_ECOLI | MAENQYYGTGRRKSSAARVFIKPGNGKIVINQRSLEQYFGRETARMVVRQPLELVDMVEKLDLYITVKGGGISGQAGAIRHGITRALMEYDESLRSELRKAGFVTRDARQVERKKVGLRKARRRPQFSKR | null | null | cytoplasmic translation [GO:0002181] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049] | PF00380; | 3.30.230.10; | Universal ribosomal protein uS9 family | null | null | null | null | null | null | null | FUNCTION: The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Mutations that decrease this affinity are suppressed in the 70S ribosome. {ECO:0000269|PubMed:15308780}. | Escherichia coli (strain K12) |
P0A7X6 | RIMM_ECOLI | MSKQLTAQAPVDPIVLGKMGSSYGIRGWLRVFSSTEDAESIFDYQPWFIQKAGQWQQVQLESWKHHNQDMIIKLKGVDDRDAANLLTNCEIVVDSSQLPQLEEGDYYWKDLMGCQVVTTEGYDLGKVVDMMETGSNDVLVIKANLKDAFGIKERLVPFLDGQVIKKVDLTTRSIEVDWDPGF | null | null | maturation of SSU-rRNA [GO:0030490]; ribosomal small subunit assembly [GO:0000028] | cytosol [GO:0005829]; ribosome [GO:0005840] | ribosome binding [GO:0043022]; rRNA binding [GO:0019843] | PF05239;PF01782; | 2.30.30.240;2.40.30.60; | RimM family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11514519, ECO:0000269|PubMed:9226267}. Note=Binds 30S subunit, but not 70S ribosomes (PubMed:9226267). {ECO:0000269|PubMed:9226267}. | null | null | null | null | null | FUNCTION: One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late assembly stage of the 30S ribosomal subunit. An accessory protein needed during the final step in assembly of the 30S ribosomal subunit, for assembly of the head region (the 16S rRNA 3' domain) (PubMed:11514519, PubMed:15496525... | Escherichia coli (strain K12) |
P0A7Y0 | RNC_ECOLI | MNPIVINRLQRKLGYTFNHQELLQQALTHRSASSKHNERLEFLGDSILSYVIANALYHRFPRVDEGDMSRMRATLVRGNTLAELAREFELGECLRLGPGELKSGGFRRESILADTVEALIGGVFLDSDIQTVEKLILNWYQTRLDEISPGDKQKDPKTRLQEYLQGRHLPLPTYLVVQVRGEAHDQEFTIHCQVSGLSEPVVGTGSSRRKAEQAAAEQALKKLELE | 3.1.26.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11305928, ECO:0000269|PubMed:15699182, ECO:0000269|PubMed:932008}; Note=Divalent metal cations, preferably Mg(2+). While only 1 Mg(2+) is detected by crystallography, other evidence indicates there may be more than 1 metal necessary for catalys... | mRNA processing [GO:0006397]; pre-miRNA processing [GO:0031054]; primary miRNA processing [GO:0031053]; regulation of gene expression [GO:0010468]; RNA processing [GO:0006396]; rRNA processing [GO:0006364]; termination of RNA polymerase II transcription [GO:0006369]; tRNA processing [GO:0008033]; U4 snRNA 3'-end proces... | cytosol [GO:0005829] | ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; ribonuclease III activity [GO:0004525]; rRNA binding [GO:0019843] | PF00035;PF14622; | 3.30.160.20;1.10.1520.10; | Ribonuclease III family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:4865702}. Note=Loosely associated with ribosomes. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; Evidence={ECO:0000269|PubMed:4592261}; | null | null | null | null | FUNCTION: Digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. Involved in the processing of rRNA precursors, viral transcripts, some mRNAs and at least 1 tRNA (metY, a minor form of tRNA-init-Met). Cleaves the 30S primary rRNA transcript to yield the immediate precursors to the ... | Escherichia coli (strain K12) |
P0A7Y4 | RNH_ECOLI | MLKQVEIFTDGSCLGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALKEHCEVILSTDSQYVRQGITQWIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEWVKGHAGHPENERCDELARAAAMNPTLEDTGYQVEV | 3.1.26.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9852071}; Note=Binds 1 Mg(2+) ion per subunit in the absence of substrate. Requires millimolar levels of Mg(2+) for maximal activity. Has low activity at micromolar concentrations of Mn(2+) and is inhibited at higher Mn(2+) levels. Can bind a s... | DNA replication, removal of RNA primer [GO:0043137] | cytoplasm [GO:0005737] | endonuclease activity [GO:0004519]; magnesium ion binding [GO:0000287]; nucleic acid binding [GO:0003676]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF00075; | 3.30.420.10; | RNase H family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; | null | null | null | null | FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. RNase H participates in DNA replication; it helps to specify the origin of genomic replication by suppressing initiation at origins other than the oriC locus; along with the 5'-3' exonuclease of pol1, it removes RNA primers from the Okazaki f... | Escherichia coli (strain K12) |
P0A7Z0 | RPIA_ECOLI | MTQDELKKAVGWAALQYVQPGTIVGVGTGSTAAHFIDALGTMKGQIEGAVSSSDASTEKLKSLGIHVFDLNEVDSLGIYVDGADEINGHMQMIKGGGAALTREKIIASVAEKFICIADASKQVDILGKFPLPVEVIPMARSAVARQLVKLGGRPEYRQGVVTDNGNVILDVHGMEILDPIAMENAINAIPGVVTVGLFANRGADVALIGTPDGVKTIVK | 5.3.1.6 | null | D-ribose metabolic process [GO:0006014]; pentose-phosphate shunt, non-oxidative branch [GO:0009052] | cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231] | identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; ribose-5-phosphate isomerase activity [GO:0004751] | PF06026; | 3.30.70.260;3.40.50.1360; | Ribose 5-phosphate isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170, ECO:0000269|PubMed:1104357, ECO:0000269|PubMed:12517338}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 mM for ribose-5-phosphate {ECO:0000269|PubMed:12517338}; KM=4.4 mM for D-ribose 5-phosphate (at 37 degrees Celsius) {ECO:0000269|PubMed:1104357}; Note=kcat is 2100 sec(-1) for ribose-5-phosphate.; | PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00170}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: After incubation at 45 degrees Celsius for 30 minutes RpiA retains 90% of its original activities. {ECO:0000269|PubMed:1104357, ECO:0000269|PubMed:12517338}; | FUNCTION: Involved in the first step of the non-oxidative branch of the pentose phosphate pathway. It catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. Can also act on D-ribose-5-diphosphate and D-ribose-5-triphosphate as substrate. {ECO:0000269|PubMed:1104357, ECO:0000269|PubMed:125173... | Escherichia coli (strain K12) |
P0A7Z4 | RPOA_ECOLI | MQGSVTEFLKPRLVDIEQVSSTHAKVTLEPLERGFGHTLGNALRRILLSSMPGCAVTEVEIDGVLHEYSTKEGVQEDILEILLNLKGLAVRVQGKDEVILTLNKSGIGPVTAADITHDGDVEIVKPQHVICHLTDENASISMRIKVQRGRGYVPASTRIHSEEDERPIGRLLVDACYSPVERIAYNVEAARVEQRTDLDKLVIEMETNGTIDPEEAIRRAATILAEQLEAFVDLRDVRQPEVKEEKPEFDPILLRPVDDLELTVRSANCLKAEAIHYIGDLVQRTEVELLKTPNLGKKSLTEIKDVLASRGLSLGMRLEN... | 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]; protein dimerization activity [GO:0046983] | PF01000;PF03118;PF01193; | 1.10.150.20;2.170.120.12;3.30.1360.10; | RNA polymerase alpha chain family | PTM: Acetylated on Lys-297 and Lys-298 in the presence of glucose. PatZ controls acetylation of Lys-298 but not of Lys-297. {ECO:0000269|PubMed:21696463}.; PTM: (Microbial infection) ADP-ribosylated on both alpha subunits by the phage T4 protein ModA (PubMed:10634320, PubMed:15489438). ADP-ribosylated on only one of th... | 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. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme. {ECO:00002... | Escherichia coli (strain K12) |
P0A800 | RPOZ_ECOLI | MARVTVQDAVEKIGNRFDLVLVAARRARQMQVGGKDPLVPEENDKTTVIALREIEEGLINNQILDVRERQEQQEQEAAELQAVTAIAEGRR | 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... | cytosol [GO:0005829]; cytosolic DNA-directed RNA polymerase complex [GO:0000345]; RNA polymerase complex [GO:0030880]; transcription elongation factor complex [GO:0008023] | DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899] | PF01192; | 3.90.940.10; | RNA polymerase subunit omega family | null | 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: Promotes RNA polymerase (RNAP) assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. {ECO:0000269|PubMed:24843001}.; FUNCTION: Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms... | Escherichia coli (strain K12) |
P0A809 | RUVA_ECOLI | MIGRLRGIIIEKQPPLVLIEVGGVGYEVHMPMTCFYELPEAGQEAIVFTHFVVREDAQLLYGFNNKQERTLFKELIKTNGVGPKLALAILSGMSAQQFVNAVEREEVGALVKLPGIGKKTAERLIVEMKDRFKGLHGDLFTPAADLVLTSPASPATDDAEQEAVAALVALGYKPQEASRMVSKIARPDASSETLIREALRAAL | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1617728}; Note=Branch migration by the RuvA-RuvB complex requires Mg(2+). {ECO:0000269|PubMed:1617728}; | recombinational repair [GO:0000725]; response to radiation [GO:0009314]; SOS response [GO:0009432] | cytoplasm [GO:0005737]; Holliday junction helicase complex [GO:0009379]; Holliday junction resolvase complex [GO:0048476] | ATP binding [GO:0005524]; four-way junction DNA binding [GO:0000400]; four-way junction helicase activity [GO:0009378]; identical protein binding [GO:0042802] | PF14520;PF07499;PF01330; | 1.10.150.20;1.10.8.10;2.40.50.140; | RuvA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00031, ECO:0000269|PubMed:21219465}. Note=In 15% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours. | null | null | null | null | null | FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair (PubMed:21531731, PubMed:6374379). The RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR); RFR and homologous recombination requ... | Escherichia coli (strain K12) |
P0A812 | RUVB_ECOLI | MIEADRLISAGTTLPEDVADRAIRPKLLEEYVGQPQVRSQMEIFIKAAKLRGDALDHLLIFGPPGLGKTTLANIVANEMGVNLRTTSGPVLEKAGDLAAMLTNLEPHDVLFIDEIHRLSPVVEEVLYPAMEDYQLDIMIGEGPAARSIKIDLPPFTLIGATTRAGSLTSPLRDRFGIVQRLEFYQVPDLQYIVSRSARFMGLEMSDDGALEVARRARGTPRIANRLLRRVRDFAEVKHDGTISADIAAQALDMLNVDAEGFDYMDRKLLLAVIDKFFGGPVGLDNLAAAIGEERETIEDVLEPYLIQQGFLQRTPRGRMA... | 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1617728}; Note=Branch migration by the RuvA-RuvB complex requires Mg(2+). {ECO:0000269|PubMed:1617728}; | recombinational repair [GO:0000725]; response to UV [GO:0009411]; SOS response [GO:0009432] | cytosol [GO:0005829]; Holliday junction helicase complex [GO:0009379]; Holliday junction resolvase complex [GO:0048476] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; four-way junction DNA binding [GO:0000400]; four-way junction helicase activity [GO:0009378] | PF17864;PF05491;PF05496; | 1.10.8.60;3.40.50.300;1.10.10.10; | RuvB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:21219465}. Note=In 15% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours. | 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=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:8433990}; | null | null | null | null | FUNCTION: The RuvABC complex is involved in recombinational repair of UV or chemically damaged DNA (PubMed:6374379). The RuvAB complex also plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR); RFR and homologous recombination required for UV light survival can be s... | Escherichia coli (strain K12) |
P0A814 | RUVC_ECOLI | MAIILGIDPGSRVTGYGVIRQVGRQLSYLGSGCIRTKVDDLPSRLKLIYAGVTEIITQFQPDYFAIEQVFMAKNADSALKLGQARGVAIVAAVNQELPVFEYAARQVKQTVVGIGSAEKSQVQHMVRTLLKLPANPQADAADALAIAITHCHVSQNAMQMSESRLNLARGRLR | 3.1.21.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00034, ECO:0000269|PubMed:1661673, ECO:0000269|PubMed:1758493, ECO:0000269|PubMed:1829835, ECO:0000269|PubMed:36000732, ECO:0000269|PubMed:7638215, ECO:0000269|PubMed:8001122, ECO:0000269|PubMed:8106500, ECO:0000269|PubMed:8195150}; Note... | recombinational repair [GO:0000725]; response to radiation [GO:0009314] | cytoplasm [GO:0005737]; Holliday junction resolvase complex [GO:0048476] | crossover junction DNA endonuclease activity [GO:0008821]; DNA binding [GO:0003677]; magnesium ion binding [GO:0000287] | PF02075; | 3.30.420.10; | RuvC family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00034, ECO:0000269|PubMed:21219465}. Note=In 15% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).; EC=3.1.21.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00034, ECO:0000269|PubMed:10471285, ECO:0000269|PubMed:1661673, ECO:0000269|PubMed:36000732, ECO:... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 (PubMed:8106500) or pH 7.0-9.0 (PubMed:8195150). {ECO:0000269|PubMed:8106500, ECO:0000269|PubMed:8195150}; | null | FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junctions during genetic recombination and DNA repair (PubMed:6374379). Endonuclease that resolves Holliday junction (HJ) intermediates. Cleaves cruciform DNA by making single-stranded nicks across the junction at symmetrical positions within the homologous arms, ... | Escherichia coli (strain K12) |
P0A817 | METK_ECOLI | MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTSAWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQGLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVGIDAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSYAIGVAEPTSIMVETFGTEK... | 2.5.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:14967023, ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:8550549, ECO:0000269|PubMed:8611562}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:6251075}; Name=Co(2+)... | one-carbon metabolic process [GO:0006730]; S-adenosylmethionine biosynthetic process [GO:0006556]; S-adenosylmethionine cycle [GO:0033353] | cytosol [GO:0005829] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; methionine adenosyltransferase activity [GO:0004478]; potassium ion binding [GO:0030955] | PF02773;PF02772;PF00438; | 3.30.300.10; | AdoMet synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00086}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:105... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 mM for Mg(2+) {ECO:0000269|PubMed:7629147}; KM=0.11 mM for ATP {ECO:0000269|PubMed:7629147}; KM=0.08 mM for L-methionine {ECO:0000269|PubMed:7629147}; | PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:10660564, ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:7629176, ECO:0000269|PubMed:... | null | null | FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme (PubMed:10551856, PubMed:10660564, PubMe... | Escherichia coli (strain K12) |
P0A821 | SELA_ECOLI | MTTETRSLYSQLPAIDRLLRDSSFLSLRDTYGHTRVVELLRQMLDEAREVIRGSQTLPAWCENWAQEVDARLTKEAQSALRPVINLTGTVLHTNLGRALQAEAAVEAVAQAMRSPVTLEYDLDDAGRGHRDRALAQLLCRITGAEDACIVNNNAAAVLLMLAATASGKEVVVSRGELVEIGGAFRIPDVMRQAGCTLHEVGTTNRTHANDYRQAVNENTALLMKVHTSNYSIQGFTKAIDEAELVALGKELDVPVVTDLGSGSLVDLSQYGLPKEPMPQELIAAGVSLVSFSGDKLLGGPQAGIIVGKKEMIARLQSHPL... | 2.9.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:2007584}; | selenocysteine biosynthetic process [GO:0016260]; selenocysteine incorporation [GO:0001514] | cytosol [GO:0005829] | identical protein binding [GO:0042802]; L-seryl-tRNA(Sec) selenium transferase activity [GO:0004125]; pyridoxal phosphate binding [GO:0030170] | PF12390;PF03841; | 3.90.1150.180;3.40.640.10; | SelA family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate; Xref=Rhea:RHEA:22728, Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:9743, ChEBI:CHEBI:15378, ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78533, ChEBI:CHEBI:78573; EC=2.9.1.1; Evidence={ECO:0000269|PubMed:20075... | null | PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1. | null | null | FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. Requires selenophosphate as the selenium-donor molecule. {ECO:0000269|PubMed:2007584, ECO:0000269|PubMed:2007585}. | Escherichia coli (strain K12) |
P0A825 | GLYA_ECOLI | MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGADYANVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSPVNFSGKLYNIVPYGIDATGHIDYADLEKQAKEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKGGSEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLERGYKVVSGGTDNHLFL... | 2.1.2.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|PubMed:10858298, ECO:0000269|PubMed:1517215, ECO:0000269|PubMed:17341210, ECO:0000269|PubMed:19883126, ECO:0000269|PubMed:3891721}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; glycine catabolic process [GO:0006546]; L-serine biosynthetic process [GO:0006564]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999]; tetrahydrofolate metabolic process [GO:0046653] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | cobalt ion binding [GO:0050897]; glycine hydroxymethyltransferase activity [GO:0004372]; identical protein binding [GO:0042802]; L-allo-threonine aldolase activity [GO:0008732]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:00... | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=800 uM for L-serine {ECO:0000269|PubMed:3891721}; KM=140 uM for serine {ECO:0000269|PubMed:19883126}; KM=300 uM for serine {ECO:0000269|PubMed:12773539, ECO:0000269|PubMed:1517215}; KM=80 uM for tetrahydrofolate {ECO:0000269|PubMed:3891721}; KM=7 uM for tetrahydrof... | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000255|HAMAP-Rule:MF_00051}.; PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000305}. | null | null | FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules (PubMed:10858298, PubM... | Escherichia coli (strain K12) |
P0A830 | DCTA_ECOLI | MKTSLFKSLYFQVLTAIAIGILLGHFYPEIGEQMKPLGDGFVKLIKMIIAPVIFCTVVTGIAGMESMKAVGRTGAVALLYFEIVSTIALIIGLIIVNVVQPGAGMNVDPATLDAKAVAVYADQAKDQGIVAFIMDVIPASVIGAFASGNILQVLLFAVLFGFALHRLGSKGQLIFNVIESFSQVIFGIINMIMRLAPIGAFGAMAFTIGKYGVGTLVQLGQLIICFYITCILFVVLVLGSIAKATGFSIFKFIRYIREELLIVLGTSSSESALPRMLDKMEKLGCRKSVVGLVIPTGYSFNLDGTSIYLTMAAVFIAQAT... | null | null | DNA damage response [GO:0006974]; fumarate transport [GO:0015741]; L-aspartate transmembrane transport [GO:0070778] | membrane [GO:0016020]; plasma membrane [GO:0005886] | fumarate transmembrane transporter activity [GO:0015138]; L-aspartate transmembrane transporter activity [GO:0015183]; malate:proton symporter activity [GO:0015366]; succinate transmembrane transporter activity [GO:0015141] | PF00375; | 1.10.3860.10; | Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. | null | null | null | null | null | FUNCTION: Responsible for the aerobic transport of the dicarboxylates fumarate, L- and D-malate and to a lesser extent succinate, from the periplasm across the inner membrane. {ECO:0000269|PubMed:17088549}. | Escherichia coli (strain K12) |
P0A832 | SSRP_ECOLI | MTKKKAHKPGSATIALNKRARHEYFIEEEFEAGLALQGWEVKSLRAGKANISDSYVLLRDGEAFLFGANITPMAVASTHVVCDPTRTRKLLLNQRELDSLYGRVNREGYTVVALSLYWKNAWCKVKIGVAKGKKQHDKRSDIKEREWQVDKARIMKNAHR | null | null | trans-translation [GO:0070929] | cytosol [GO:0005829] | RNA binding [GO:0003723] | PF01668; | 2.40.280.10; | SmpB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00023, ECO:0000269|PubMed:11917023, ECO:0000269|PubMed:15069072}. Note=The tmRNA-SmpB complex associates with stalled ribosomes (PubMed:10393194, PubMed:11917023, PubMed:15699355, PubMed:20940705, PubMed:22622583). SmpB associates with ribosomes even in the abs... | null | null | null | null | null | FUNCTION: Required for rescue of stalled ribosomes mediated by trans-translation. Binds to tmRNA RNA (also known as SsrA or 10Sa RNA, 363 nucleotides in this organism), required for stable binding of tmRNA to ribosomes (PubMed:10393194, PubMed:11904185, PubMed:11917023). tmRNA and SmpB together mimic tRNA shape, replac... | Escherichia coli (strain K12) |
P0A836 | SUCC_ECOLI | MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKRLVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQGRELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDPREAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG... | 6.2.1.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475, ECO:0000269|PubMed:7040388}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475}; | succinyl-CoA metabolic process [GO:0006104]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; succinate-CoA ligase complex [GO:0042709]; succinate-CoA ligase complex (ADP-forming) [GO:0009361] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; succinate-CoA ligase (ADP-forming) activity [GO:0004775]; succinate-CoA ligase (GDP-forming) activity [GO:0004776] | PF08442;PF00549; | 3.30.1490.20;3.30.470.20;3.40.50.261; | Succinate/malate CoA ligase beta subunit family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA; Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10353839, ECO:0000269|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=70 uM for ATP {ECO:0000269|PubMed:10353839}; KM=394 uM for GTP {ECO:0000269|PubMed:10353839}; Note=kcat is 2684 min(-1) with ATP as substrate and 1471 min(-1) with GTP as substrate. {ECO:0000269|PubMed:10353839}; | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000305|PubMed:10353839}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:8144675}; | null | FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrat... | Escherichia coli (strain K12) |
P0A840 | SURE_ECOLI | MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFENGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLDGHKHYDTAAAVTCSILRALCKEPLRTGRILNINVPDLPLDQIKGIRVTRCGTRHPADQVIPQQDPRGNTLYWIGPPGGKCDAGPGTDFAAVDEGYVSITPLHVDLTAHSAQDVVSDWLNSVGVGTQW | 3.1.3.5; 3.1.3.6; 3.6.1.11 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15489502}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:15489502}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:15489502}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15489502}; Na... | UMP catabolic process [GO:0046050] | cytoplasm [GO:0005737] | 3'-nucleotidase activity [GO:0008254]; 5'-nucleotidase activity [GO:0008253]; exopolyphosphatase activity [GO:0004309]; GMP 5'-nucleotidase activity [GO:0050484]; manganese ion binding [GO:0030145]; nucleotide binding [GO:0000166]; XMP 5'-nucleosidase activity [GO:0106411] | PF01975; | 3.40.1210.10; | SurE nucleotidase 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 ribonucleoside 3'-phosphate + H2O = a ribo... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.32 mM for 5'-AMP {ECO:0000269|PubMed:15489502}; KM=0.26 mM for 5'-GMP {ECO:0000269|PubMed:15489502}; KM=0.28 mM for 5'-dGMP {ECO:0000269|PubMed:15489502}; KM=0.1 mM for 3'-AMP {ECO:0000269|PubMed:15489502}; KM=0.37 mM for 3'-CMP {ECO:0000269|PubMed:15489502}; KM=... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.2 for nucleotidase activity. {ECO:0000269|PubMed:15489502}; | null | FUNCTION: Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP (PubMed:15489502). Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-ch... | Escherichia coli (strain K12) |
P0A847 | TGT_ECOLI | MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDR... | 2.4.2.29 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:7893665}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:7893665}; | queuosine biosynthetic process [GO:0008616]; tRNA wobble guanine modification [GO:0002099]; tRNA-guanine transglycosylation [GO:0101030] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | tRNA-guanosine(34) queuine transglycosylase activity [GO:0008479]; zinc ion binding [GO:0008270] | PF01702; | 3.20.20.105; | Queuine tRNA-ribosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7-aminomethyl-7-carbaguanosine(34) in tRNA + guanine; Xref=Rhea:RHEA:24104, Rhea:RHEA-COMP:10341, Rhea:RHEA-COMP:10342, ChEBI:CHEBI:16235, ChEBI:CHEBI:58703, ChEBI:CHEBI:74269, ChEBI:CHEBI:82833; EC=2.4.2.29; Evidence={ECO:0000255|HAMAP... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.12 uM for tRNA(Tyr) {ECO:0000269|PubMed:11714265}; KM=0.1 uM for guanine {ECO:0000269|PubMed:11714265}; Note=kcat is 0.00121 sec(-1) with tRNA(Tyr) and guanine as substrates. {ECO:0000269|PubMed:11714265}; | PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:1706703}. | null | null | FUNCTION: Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site ... | Escherichia coli (strain K12) |
P0A850 | TIG_ECOLI | MQVSVETTQGLGRRVTITIAADSIETAVKSELVNVAKKVRIDGFRKGKVPMNIVAQRYGASVRQDVLGDLMSRNFIDAIIKEKINPAGAPTYVPGEYKLGEDFTYSVEFEVYPEVELQGLEAIEVEKPIVEVTDADVDGMLDTLRKQQATWKEKDGAVEAEDRVTIDFTGSVDGEEFEGGKASDFVLAMGQGRMIPGFEDGIKGHKAGEEFTIDVTFPEEYHAENLKGKAAKFAINLKKVEERELPELTAEFIKRFGVEDGSVEGLRAEVRKNMERELKSAIRNRVKSQAIEGLVKANDIDVPAALIDSEIDVLRRQAAQ... | 5.2.1.8 | null | 'de novo' cotranslational protein folding [GO:0051083]; cell cycle [GO:0007049]; cell division [GO:0051301]; chaperone-mediated protein folding [GO:0061077]; protein transport [GO:0015031]; protein unfolding [GO:0043335]; response to heat [GO:0009408]; stress response to copper ion [GO:1990169] | cytosol [GO:0005829]; membrane [GO:0016020] | identical protein binding [GO:0042802]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; protein folding chaperone [GO:0044183]; ribosome binding [GO:0043022] | PF00254;PF05698;PF05697; | 3.10.50.40;3.30.70.1050;1.10.3120.10; | FKBP-type PPIase family, Tig subfamily | PTM: (Microbial infection) ADP-ribosylated by the phage T4 protein ModB. {ECO:0000269|PubMed:16112649}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8633085}. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. {ECO:0000269|PubMed:8633085}. | 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:8633085}; | null | null | null | null | FUNCTION: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates (PubMed:2481240... | Escherichia coli (strain K12) |
P0A853 | TNAA_ECOLI | MENFKHLPEPFRIRVIEPVKRTTRAYREEAIIKSGMNPFLLDSEDVFIDLLTDSGTGAVTQSMQAAMMRGDEAYSGSRSYYALAESVKNIFGYQYTIPTHQGRGAEQIYIPVLIKKREQEKGLDRSKMVAFSNYFFDTTQGHSQINGCTVRNVYIKEAFDTGVRYDFKGNFDLEGLERGIEEVGPNNVPYIVATITSNSAGGQPVSLANLKAMYSIAKKYDIPVVMDSARFAENAYFIKQREAEYKDWTIEQITRETYKYADMLAMSAKKDAMVPMGGLLCMKDDSFFDVYTECRTLCVVQEGFPTYGGLEGGAMERLAV... | 4.1.99.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | indole metabolic process [GO:0042431]; tryptophan catabolic process [GO:0006569] | cell pole [GO:0060187]; cytosol [GO:0005829]; membrane [GO:0016020]; protein-containing complex [GO:0032991] | identical protein binding [GO:0042802]; L-cysteine desulfhydrase activity [GO:0080146]; potassium ion binding [GO:0030955]; pyridoxal phosphate binding [GO:0030170]; tryptophanase activity [GO:0009034] | PF01212; | 3.90.1150.10;3.40.640.10; | Beta-eliminating lyase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22380631}. Note=Almost exclusively localized in foci near 1 cell pole in mid-to-late exponential phase, fewer cells have foci at stationary phase; polar localization depends on the minCDE operon. | CATALYTIC ACTIVITY: Reaction=H2O + L-tryptophan = indole + NH4(+) + pyruvate; Xref=Rhea:RHEA:19553, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:16881, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; EC=4.1.99.1; | null | PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate pathway; indole and pyruvate from L-tryptophan: step 1/1. | null | null | null | Escherichia coli (strain K12) |
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