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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P0A031 | FTSZ_STAAU | MLEFEQGFNHLATLKVIGVGGGGNNAVNRMIDHGMNNVEFIAINTDGQALNLSKAESKIQIGEKLTRGLGAGANPEIGKKAAEESREQIEDAIQGADMVFVTSGMGGGTGTGAAPVVAKIAKEMGALTVGVVTRPFSFEGRKRQTQAAAGVEAMKAAVDTLIVIPNDRLLDIVDKSTPMMEAFKEADNVLRQGVQGISDLIAVSGEVNLDFADVKTIMSNQGSALMGIGVSSGENRAVEAAKKAISSPLLETSIVGAQGVLMNITGGESLSLFEAQEAADIVQDAADEDVNMIFGTVINPELQDEIVVTVIATGFDDKPT... | null | null | chloroplast fission [GO:0010020]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093]; protein polymerization [GO:0051258] | cell division site [GO:0032153]; cytoplasm [GO:0005737] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF12327;PF00091; | 3.30.1330.20;3.40.50.1440; | FtsZ family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}. Note=Assembles at midcell at the inner surface of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_00909}. | null | null | null | null | null | FUNCTION: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produc... | Staphylococcus aureus |
P0A038 | G3P_STAAU | MAVKVAINGFGRIGRLAFRRIQEVEGLEVVAVNDLTDDDMLAHLLKYDTMQGRFTGEVEVVDGGFRVNGKEVKSFSEPDASKLPWKDLNIDVVLECTGFYTDKDKAQAHIEAGAKKVLISAPATGDLKTIVFNTNHQELDGSETVVSGASCTTNSLAPVAKVLNDDFGLVEGLMTTIHAYTGDQNTQDAPHRKGDKRRARAAAENIIPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATGSLTELTVVLEKQDVTVEQVNEAMKNASNESFGYTEDEIVSSDVVGMTYGSLFDATQTRVMSVGDRQLVKVAAWYDNEMSY... | 1.2.1.12 | null | glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; NADH regeneration [GO:0006735]; response to iron ion [GO:0010039] | catalytic complex [GO:1902494]; cytoplasm [GO:0005737]; peptidoglycan-based cell wall [GO:0009274] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NAD+ binding [GO:0070403]; NADP binding [GO:0050661]; protease binding [GO:0002020]; transferrin receptor activity [GO:0004998] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000250|UniProtKB:Q6GIL8}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester,... | Staphylococcus aureus |
P0A0L2 | ETXA_STAAU | MKKTAFTLLLFIALTLTTSPLVNGSEKSEEINEKDLRKKSELQGTALGNLKQIYYYNEKAKTENKESHDQFLQHTILFKGFFTDHSWYNDLLVDFDSKDIVDKYKGKKVDLYGAYYGYQCAGGTPNKTACMYGGVTLHDNNRLTEEKKVPINLWLDGKQNTVPLETVKTNKKNVTVQELDLQARRYLQEKYNLYNSDVFDGKVQRGLIVFHTSTEPSVNYDLFGAQGQYSNTLLRIYRDNKTINSENMHIDIYLYTS | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit. The zinc ion is necessary for the toxin interaction with MHC class II.; | null | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; MHC class II protein binding [GO:0042289]; toxin activity [GO:0090729] | PF02876;PF01123; | 2.40.50.110;3.10.20.120; | Staphylococcal/streptococcal toxin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules (PubMed:12467569, PubMed:2658055). In turn, waves of cellular activation, cytokine production, and migration into the lung... | Staphylococcus aureus |
P0A0M0 | ETXH_STAAU | MINKIKILFSFLALLLSFTSYAKAEDLHDKSELTDLALANAYGQYNHPFIKENIKSDEISGEKDLIFRNQGDSGNDLRVKFATADLAQKFKNKNVDIYGASFYYKCEKISENISECLYGGTTLNSEKLAQERVIGANVWVDGIQKETELIRTNKKNVTLQELDIKIRKILSDKYKIYYKDSEISKGLIEFDMKTPRDYSFDIYDLKGENDYEIDKIYEDNKTLKSDDISHIDVNLYTKKKV | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit. The zinc ion is necessary for interaction with host MHC class II molecules. {ECO:0000269|PubMed:10586065, ECO:0000269|PubMed:11432818}; | null | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; MHC class II protein binding [GO:0042289]; T cell receptor binding [GO:0042608]; toxin activity [GO:0090729] | PF02876;PF01123; | 2.40.50.110;3.10.20.120; | Staphylococcal/streptococcal toxin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules via their alpha domain, in particular TRAV27 (PubMed:12682246, PubMed:17709482, PubMed:21081917). In turn, this ternary co... | Staphylococcus aureus |
P0A110 | NDOB_PSEPU | MNYNNKILVSESGLSQKHLIHGDEELFQHELKTIFARNWLFLTHDSLIPAPGDYVTAKMGIDEVIVSRQNDGSIRAFLNVCRHRGKTLVSVEAGNAKGFVCSYHGWGFGSNGELQSVPFEKDLYGESLNKKCLGLKEVARVESFHGFIYGCFDQEAPPLMDYLGDAAWYLEPMFKHSGGLELVGPPGKVVIKANWKAPAENFVGDAYHVGWTHASSLRSGESIFSSLAGNAALPPEGAGLQMTSKYGSGMGVLWDGYSGVHSADLVPELMAFGGAKQERLNKEIGDVRARIYRSHLNCTVFPNNSMLTCSGVFKVWNPID... | 1.14.12.12 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:10669618, ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729, ECO:0000269|PubMed:6874638, ECO:0000269|PubMed:9634695}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:10669618, ECO:0000269|PubMed:12586937, ECO:0000269|PubMed... | aromatic compound catabolic process [GO:0019439] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; iron ion binding [GO:0005506]; naphthalene 1,2-dioxygenase activity [GO:0018625] | PF00355;PF00848; | 2.102.10.10; | Bacterial ring-hydroxylating dioxygenase alpha subunit family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + NADH + naphthalene + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(+); Xref=Rhea:RHEA:19173, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16482, ChEBI:CHEBI:44343, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.12.12; Evidence={ECO:0000269|PubMed:10692370, ECO:0000269|PubMed... | null | PATHWAY: Aromatic compound metabolism; naphthalene degradation. {ECO:0000305|PubMed:10692370}. | null | null | FUNCTION: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The alpha subunit has a catalytic role in the holoenzyme. Also able to catalyze the cis-dihydro... | Pseudomonas putida (Arthrobacter siderocapsulatus) |
P0A111 | NDOB_PSEU8 | MNYNNKILVSESGLSQKHLIHGDEELFQHELKTIFARNWLFLTHDSLIPAPGDYVTAKMGIDEVIVSRQNDGSIRAFLNVCRHRGKTLVSVEAGNAKGFVCSYHGWGFGSNGELQSVPFEKDLYGESLNKKCLGLKEVARVESFHGFIYGCFDQEAPPLMDYLGDAAWYLEPMFKHSGGLELVGPPGKVVIKANWKAPAENFVGDAYHVGWTHASSLRSGESIFSSLAGNAALPPEGAGLQMTSKYGSGMGVLWDGYSGVHSADLVPELMAFGGAKQERLNKEIGDVRARIYRSHLNCTVFPNNSMLTCSGVFKVWNPID... | 1.14.12.12 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:16980501, ECO:0000269|Ref.3}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000269|PubMed:16980501, ECO:0000269|Ref.3}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:16980501, ECO:0000269|Ref.3}; Note... | aromatic compound catabolic process [GO:0019439] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; iron ion binding [GO:0005506]; naphthalene 1,2-dioxygenase activity [GO:0018625] | PF00355;PF00848; | 2.102.10.10; | Bacterial ring-hydroxylating dioxygenase alpha subunit family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + NADH + naphthalene + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(+); Xref=Rhea:RHEA:19173, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16482, ChEBI:CHEBI:44343, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.12.12; Evidence={ECO:0000250|UniProtKB:P0A110}; | null | PATHWAY: Aromatic compound metabolism; naphthalene degradation. {ECO:0000305|PubMed:8226631}. | null | null | FUNCTION: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The alpha subunit has a catalytic role in the holoenzyme. {ECO:0000269|PubMed:8226631}. | Pseudomonas sp. (strain C18) |
P0A182 | QADG_PSEPU | MSAVAGCTATTDPGWEVDAFGGVSSLCQPMEADLYGCSDPCWWPAQVPDMMSTYQDWNAQASNSAEDWRNLGTVFPKDK | 1.4.9.- | COFACTOR: Name=cysteine tryptophylquinone residue; Xref=ChEBI:CHEBI:20252; Evidence={ECO:0000269|PubMed:11555656, ECO:0000269|PubMed:11704672}; Note=Contains 1 cysteine tryptophylquinone per subunit. {ECO:0000269|PubMed:11555656, ECO:0000269|PubMed:11704672}; | null | periplasmic space [GO:0042597] | amine dehydrogenase activity [GO:0030058] | PF08992; | 4.10.940.10; | Quinohemoprotein amine dehydrogenase subunit gamma family | PTM: The cysteine tryptophylquinone (CTQ) is generated by oxidation of the indole ring of a tryptophan residue to form tryptophylquinone, followed by covalent cross-linking with a cysteine residue. {ECO:0000269|PubMed:11555656, ECO:0000269|PubMed:11704672}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:27315927}. Note=Is probably co-translocated into the periplasm when associated with the alpha and/or beta subunit, which contain both a signal peptide. {ECO:0000250|UniProtKB:Q8VUS8}. | CATALYTIC ACTIVITY: Reaction=A + an aliphatic amine + H2O = AH2 + an aldehyde + NH4(+); Xref=Rhea:RHEA:51128, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17478, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:58001; Evidence={ECO:0000269|PubMed:27315927}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:511... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 8.0 for n-butylamine oxidation. {ECO:0000269|PubMed:27315927}; | null | FUNCTION: Catalyzes the oxidative deamination of a wide range of aliphatic monoamines and diamines (PubMed:27315927). The physiological electron acceptor is an azurin-like blue protein (PubMed:27315927). {ECO:0000269|PubMed:27315927}. | Pseudomonas putida (Arthrobacter siderocapsulatus) |
P0A185 | NDOA_PSEPU | MTVKWIEAVALSDILEGDVLGVTVEGKELALYEVEGEIYATDNLCTHGSARMSDGYLEGREIECPLHQGRFDVCTGKALCAPVTQNIKTYPVKIENLRVMIDLS | null | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:18719951, ECO:0000269|PubMed:2294093}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:2294093}; | aromatic compound catabolic process [GO:0019439] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872] | PF00355; | 2.102.10.10; | Bacterial ring-hydroxylating dioxygenase ferredoxin component family | null | null | null | null | PATHWAY: Aromatic compound metabolism; naphthalene degradation. {ECO:0000305|PubMed:10692370}. | null | null | FUNCTION: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene (PubMed:10692370, PubMed:2294093, PubMed:6874638). Functions as an intermediate electron transfe... | Pseudomonas putida (Arthrobacter siderocapsulatus) |
P0A1A5 | ILVE_SALTY | MTTKKADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYDSHKGPVVFRHREHMQRLRDSAKIYRFPVSQSIDELMEACRDVIRKNNLTSAYIRPLVFVGDVGMGVNPPPGYTTDVIIAAFPWGAYLGAEALDQGIDAMVSSWNRAAPNTIPTAAKAGGNYLSSLLVGSEARRHGYQEGIALDVNGYISEGAGENLFEVKDGVLFTPPFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLADEVFMSGTAAEITPVRSVDGIQVGEGRCGPVTKRIQQAFFGLFTGETEDKWGWLDPVNS | 2.6.1.42 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | aspartate biosynthetic process [GO:0006532]; isoleucine biosynthetic process [GO:0009097]; leucine biosynthetic process [GO:0009098]; valine biosynthetic process [GO:0009099] | cytosol [GO:0005829] | branched-chain-amino-acid transaminase activity [GO:0004084]; L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655] | PF01063; | 3.30.470.10;3.20.10.10; | Class-IV pyridoxal-phosphate-dependent aminotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=R... | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.; PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. | null | null | FUNCTION: Acts on leucine, isoleucine and valine. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A1B9 | SCTN1_SALTY | MKTPRLLQYLAYPQKITGPIIEAELRDVAIGELCEIRRGWHQKQVVARAQVVGLQRERTVLSLIGNAQGLSRDVVLYPTGRALSAWVGYSVLGAVLDPTGKIVERFTPEVAPISEERVIDVAPPSYASRVGVREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTMLMHMLIEQTEADVFVIGLIGERGREVTEFVDMLRASHKKEKCVLVFATSDFPSVDRCNAAQLATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALASGERPARRGYPASVFDNLPRLLERPGATSEGSITAFYTVLLESEEEADPMADEIRS... | 7.4.2.8 | null | protein secretion by the type III secretion system [GO:0030254] | cytoplasm [GO:0005737]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261]; type III protein secretion system complex [GO:0030257] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; protein-exporting ATPase activity [GO:0008564]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933] | PF00006;PF02874;PF18269; | 3.40.50.12240; | ATPase alpha/beta chains family, T3SS ATPase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28283062, ECO:0000305|PubMed:15060043}. Note=Associated with the membrane, presumably through interactions with other components of the SPI-1-encoded T3SS. {ECO:0000269|PubMed:15060043, ECO:0000269|PubMed:28283062}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000305|PubMed:8045880}; | null | null | null | null | FUNCTION: ATPase component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:15060043, PubMed:16208377, PubMed:26170413). Acts as a molecular motor to provide the energy that is required for the export of proteins (Pr... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A1C1 | SCTN_SHIFL | MSYTKLLTQLSFPNRISGPILETSLSDVSIGEICNIQAGIESNEIVARAQVVGFHDEKTILSLIGNSRGLSRQTLIKPTAQFLHTQVGRGLLGAVVNPLGEVTDKFAVTDNSEILYRPVDNAPPLYSERAAIEKPFLTGIKVIDSLLTCGEGQRMGIFASAGCGKTFLMNMLIEHSGADIYVIGLIGERGREVTETVDYLKNSEKKSRCVLVYATSDYSSVDRCNAAYIATAIAEFFRTEGHKVALFIDSLTRYARALRDVALAAGESPARRGYPVSVFDSLPRLLERPGKLKAGGSITAFYTVLLEDDDFADPLAEEVR... | 7.4.2.8 | null | protein secretion by the type III secretion system [GO:0030254] | cytoplasm [GO:0005737]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261]; type III protein secretion system complex [GO:0030257] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; protein-exporting ATPase activity [GO:0008564]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933] | PF00006;PF02874;PF18269; | 3.40.50.12240; | ATPase alpha/beta chains family, T3SS ATPase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18657109, ECO:0000269|PubMed:25583506}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000305|PubMed:26947936, ECO:0000305|PubMed:27770024}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=181 uM for ATP (monomeric form) {ECO:0000269|PubMed:29595954}; KM=114 uM for ATP (trimeric form) {ECO:0000269|PubMed:29595954}; KM=201 uM for ATP (monomeric form, in the presence of MxiN/SctL) {ECO:0000269|PubMed:29595954}; KM=116 uM for ATP (trimeric form, in the ... | null | null | null | FUNCTION: ATPase component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:26947936, PubMed:27770024, PubMed:29595954). Acts as a molecular motor to provide the energy that is required for the export of proteins (Pr... | Shigella flexneri |
P0A1C7 | PDUA_SALTY | MQQEALGMVETKGLTAAIEAADAMVKSANVMLVGYEKIGSGLVTVIVRGDVGAVKAATDAGAAAARNVGEVKAVHVIPRPHTDVEKILPKGISQ | null | null | propanediol catabolic process [GO:0051144] | propanediol degradation polyhedral organelle [GO:0031472] | null | PF00936; | 3.30.70.1710; | Bacterial microcompartments protein family | null | SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000269|PubMed:11844753, ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:24747050, ECO:0000269|PubMed:25713376, ECO:0000269|PubMed:27063436, ECO:0000269|PubMed:28585808}. Note=The C-terminus probably faces the interior of the BMC (Probable). Modeling suggests the co... | null | null | PATHWAY: Polyol metabolism; 1,2-propanediol degradation. {ECO:0000305|PubMed:10498708}. | null | null | FUNCTION: One of the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation (Probable) (PubMed:11844753, PubMed:21239588). At least one of PduA or PduJ is required for BMC assembly; it must be encoded as the first gene in the pdu operon (PubMed:27561553, PubMed:33... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A1C9 | EUTL_SALTY | MPALDLIRPSVTAMRVIASVNDGFARELKLPPHIRSLGLITADSDDVTYIAADEATKQAMVEVVYGRSLYAGAAHGPSPTAGEVLIMLGGPNPAEVRAGLDAMVASIENGAAFQWANDAENTAFLAHVVSRTGSYLSSTAGIALGDPMAYLVAPPLEATFGIDAAMKSADVQLVTYVPPPSETNYSAAFLTGSQAACKAACNAFTDAVLDIARNPVQRA | null | null | ethanolamine catabolic process [GO:0046336]; generation of precursor metabolites and energy [GO:0006091] | ethanolamine degradation polyhedral organelle [GO:0031471] | structural molecule activity [GO:0005198] | PF00936; | 3.30.70.1710; | EutL/PduB family | null | SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000269|PubMed:27063436}. | null | null | PATHWAY: Amine and polyamine degradation; ethanolamine degradation. {ECO:0000269|PubMed:3045078}. | null | null | FUNCTION: A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation (PubMed:22428024, PubMed:27063436). Forms a hexagonal trimer with 3 small channels and a large central pore that has been seen in both open and closed forms and is probably used for gated transport into and out of ... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A1E3 | CYSK_SALTY | MSKIYEDNSLTIGHTPLVRLNRIGNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASDPQKYLLLQQFSNPANPEIHEKTTGPEIWEDTDGQVDVFISGVGTGGTLTGVTRYIKGTKGKTDLITVAVEPTDSPVIAQALAGEEIKPGPHKIQGIGAGFIPGNLDLKLIDKVVGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDESFTNKNIVVILPSSGERYLSTALFADLFTEKE... | 2.5.1.47 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11023792, ECO:0000269|PubMed:9761678}; | cysteine biosynthetic process from serine [GO:0006535] | cytoplasm [GO:0005737] | cystathionine beta-synthase activity [GO:0004122]; cysteine synthase activity [GO:0004124]; L-cysteine desulfhydrase activity [GO:0080146] | PF00291; | 3.40.50.1100; | Cysteine synthase/cystathionine beta-synthase family | null | null | CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; Evidence={ECO:0000269|PubMed:4977445}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 mM for O-acetyl-L-serine as isolated subunit and in complex with CysK {ECO:0000269|PubMed:4977445}; | PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2. | null | null | FUNCTION: Two cysteine synthase enzymes are found, this enzyme and CysM; both catalyze the same reaction. Cysteine synthase B (CysM) can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. {ECO:0000269|PubMed:4977445}. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A1P6 | GLN1B_SALTY | MSAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFDGSSIGGWKGINESDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGYDRDPRSIAKRAEDYLRATGIADTVLFGPEPEFFLFDDIRFGASISGSHVAIDDIEGAWNSSTKYEGGNKGHRPGVKGGYFPVPPVDSAQDIRSEMCLVMEQMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRFGKTATFMPKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIGGVIKHAKAINALANPTTNSY... | 6.3.1.2 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447}; Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:809944... | glutamine biosynthetic process [GO:0006542]; nitrogen utilization [GO:0019740]; protein homooligomerization [GO:0051260] | cytoplasm [GO:0005737]; membrane [GO:0016020] | ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356]; manganese ion binding [GO:0030145] | PF00120;PF03951; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000305|PubMed:7727369}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.58 mM for ATP {ECO:0000269|PubMed:7727369}; | null | null | null | FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. {ECO:0000269|PubMed:7727369}. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A1S2 | HNS_SALTY | MSEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESAAAAEVEERTRKLQQYREMLIADGIDPNELLNSMAAAKSGTKAKRAARPAKYSYVDENGETKTWTGQGRTPAVIKKAMEEQGKQLEDFLIKE | null | null | negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression, epigenetic [GO:0045814] | cytosol [GO:0005829]; nucleoid [GO:0009295]; protein-DNA complex [GO:0032993] | bent DNA binding [GO:0003681]; DNA binding [GO:0003677]; DNA-binding transcription repressor activity [GO:0001217]; identical protein binding [GO:0042802]; minor groove of adenine-thymine-rich DNA binding [GO:0003680]; protein dimerization activity [GO:0046983]; structural constituent of chromatin [GO:0030527]; transcr... | PF00816; | 1.10.287.1050;4.10.430.10; | Histone-like protein H-NS family | null | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000250|UniProtKB:P0ACF8}. | null | null | null | null | null | FUNCTION: Acts as a global transcriptional repressor and binds to the minor groove of AT-rich DNA (PubMed:10844682, PubMed:1423593, PubMed:16933988, PubMed:17630976, PubMed:21059643, PubMed:21673140). Silences genes by altering DNA topology; in magnesium concentrations equivalent to inside Salmonella-containing vacuole... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A1V6 | KPRS_SALTY | MPDMKLFAGNATPELAQRIANRLYTSLGDAAVGRFSDGEVSVQINENVRGGDIFIIQSTCAPTNDNLMELVVMVDALRRASAGRITAVIPYFGYARQDRRVRSARVPITAKVVADFLSSVGVDRVLTVDLHAEQIQGFFDVPVDNVFGSPILLEDMLQLNLDNPIVVSPDIGGVVRARAIAKLLNDTDMAIIDKRRPRANVSQVMHIIGDVAGRDCVLVDDMIDTGGTLCKAAEALKERGAKRVFAYATHPIFSGNAANNLRNSVIDEVVVCDTIPLTDEIKALPNVRTLTLSGMLAEAIRRISNEESISAMFEH | 2.7.6.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:4306285, ECO:0000269|PubMed:4324215}; Note=Binds 2 Mg(2+) ions per subunit (Potential). Can also use Mn(2+) ions (PubMed:4306285). {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:4306285}; | 5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; phosphorylation [GO:0016310]; purine nucleotide biosynthetic process [GO:0006164]; ribonucleoside monophosphate biosynthetic process [GO:0009156] | cytoplasm [GO:0005737]; ribose phosphate diphosphokinase complex [GO:0002189] | ATP binding [GO:0005524]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; 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:0000305|PubMed:4306285, ECO:0000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=46 uM for ATP {ECO:0000269|PubMed:4324215}; KM=160 uM for Rib-5-P {ECO:0000269|PubMed:4324215}; | 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}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.1-8.6. {ECO:0000269|PubMed:4306285}; | 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:4306285, ECO:0000269|PubMed:4324215, ECO:0000305|PubMed:28... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A223 | SCTF_SHIFL | MSVTVPNDDWTLSSLSETFDDGTQTLQGELTLALDKLAKNPSNPQLLAEYQSKLSEYTLYRNAQSNTVKVIKDVDAAIIQNFR | null | null | protein secretion by the type III secretion system [GO:0030254] | cell surface [GO:0009986]; extracellular region [GO:0005576]; type III protein secretion system complex [GO:0030257] | identical protein binding [GO:0042802] | PF09392; | 1.20.58.90; | SctF family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cell surface {ECO:0000305}. | null | null | null | null | null | FUNCTION: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:16888041, PubMed:16920362, PubMed:32092125, PubMed:36790757). MxiH/SctF forms the external needle filament that protrudes from the bacterial surfac... | Shigella flexneri |
P0A251 | AHPC_SALTY | MSLINTKIKPFKNQAFKNGEFIEVTEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDTHFTHKAWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVAAHPGEVCPAKWKEGEATLAPSLDLVGKI | 1.11.1.26 | null | cell redox homeostasis [GO:0045454]; cellular response to stress [GO:0033554]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | cytosol [GO:0005829] | NADH-dependent peroxiredoxin activity [GO:0102039]; thioredoxin peroxidase activity [GO:0008379] | PF10417;PF00578; | 3.40.30.10; | Peroxiredoxin family, AhpC/Prx1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}. | CATALYTIC ACTIVITY: Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+); Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.11.1.26; Evidence={ECO:0000269|PubMed:2643600}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for H(2)O(2) {ECO:0000269|PubMed:16060667}; Note=kcat is 55.1 sec(-1) with H(2)O(2) as substrate. {ECO:0000269|PubMed:16060667}; | null | null | null | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. {ECO:0000269|PubMed:2643600, ECO:0000269|PubMed:8041738}. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A283 | PTGA_SALTY | MGLFDKLKSLVSDDKKDTGTIEIVAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMVAPVDGTIGKIFETNHAFSIESDSGIELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDPVIEFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P69783}; Note=Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization. {ECO:0000250|UniProtKB:P69783}; | phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | kinase activity [GO:0016301]; metal ion binding [GO:0046872] | PF00358; | 2.70.70.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 uM for methyl alpha-glucoside (with phospho-IIIGlc Slow) {ECO:0000269|PubMed:6754734}; KM=6 uM for methyl alpha-glucoside {ECO:0000269|PubMed:6292227}; KM=10 uM for glucose {ECO:0000269|PubMed:6292227}; KM=40 uM for mannose {ECO:0000269|PubMed:6292227}; KM=200 ... | null | null | null | FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A2D5 | CHEY_SALTY | MADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16674976, ECO:0000269|PubMed:18083806, ECO:0000269|PubMed:8257674}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:16674976, ECO:0000269|PubMed:18083806, ECO:0000269|PubMed:8257674}; | archaeal or bacterial-type flagellum-dependent cell motility [GO:0097588]; chemotaxis [GO:0006935] | cytoplasm [GO:0005737] | histidine phosphotransfer kinase activity [GO:0009927]; metal ion binding [GO:0046872]; phosphorelay sensor kinase activity [GO:0000155] | PF00072; | 3.40.50.2300; | null | PTM: Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available (By similarity). Dephosphorylated (inactivated) by CheZ. {ECO:0000250|UniProtKB:P0AE67, ECO:0000269|PubMed:1902474, ECO:0000269|PubMed:3280143}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation (B... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A2F2 | NPD_SALTY | MQSRRFHRLSRFRKNKRLLRERLRQRIFFRDRVVPEMMENPRVLVLTGAGISAESGIRTFRAADGLWEEHRVEDVATPEGFARNPGLVQTFYNARRQQLQQPEIQPNAAHLALAKLEEALGDRFLLVTQNIDNLHERAGNRNIIHMHGELLKVRCSQSGQILEWNGDVMPEDKCHCCQFPAPLRPHVVWFGEMPLGMDEIYMALSMADIFIAIGTSGHVYPAAGFVHEAKLHGAHTVELNLEPSQVGSEFEEKHYGPASQVVPEFVDKFLKGL | 2.3.1.286 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01121}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01121}; | null | cytoplasm [GO:0005737] | NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; NAD-dependent protein de-2-hydroxyisobutyrylase activity [GO:0160013]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuccinylase activity [GO:0036055]; zinc ion binding [GO:0008270] | PF02146; | 3.30.1600.10;3.40.50.1220; | Sirtuin family, Class III subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01121}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=... | null | null | null | null | FUNCTION: NAD-dependent lysine deacetylase that specifically removes acetyl groups on target proteins. Also acts as a protein-lysine deacylase by mediating protein desuccinylation and de-2-hydroxyisobutyrylation. Modulates the activities of several proteins which are inactive in their acylated form (By similarity). Act... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A2I3 | GYRB_SALTY | MSNSYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGHCKDIVVTIHADNSVSVTDDGRGIPTGIHPEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSQKLELVIQRDGKIHRQIYEHGVPQAPLAVTGDTDKTGTMVRFWPSHETFTNVTEFEYEILAKRLRELSFLNSGVSIRLRDKRDGKEDHFHYEGGIKAFVEYLNKNKTPIHPNIFYFSTEKDGIGVEVALQWNDGFQENIYCFTNNIPQRDGGTHLAGFRAAMTRTLNAYMDKEGYSKKAKVSATGDDAREGLI... | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bri... | DNA topological change [GO:0006265]; DNA-templated DNA replication [GO:0006261]; response to antibiotic [GO:0046677] | chromosome [GO:0005694]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; metal ion binding [GO:0046872] | PF00204;PF00986;PF21249;PF18053;PF02518;PF01751; | 3.10.20.690;3.30.230.10;3.40.50.670;3.30.565.10; | Type II topoisomerase GyrB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; | null | null | null | null | FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state, and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A2K1 | TRPB_SALTY | MTTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKNYAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSISAGLDFPSVGPQHAYLNSIG... | 4.2.1.20 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | tryptophan biosynthetic process [GO:0000162] | cytoplasm [GO:0005737] | identical protein binding [GO:0042802]; tryptophan synthase activity [GO:0004834] | PF00291; | 3.40.50.1100; | TrpB family | null | null | CATALYTIC ACTIVITY: Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; | null | PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. | null | null | FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A2M9 | SPVC_SALTY | MPINRPNLNLNIPPLNIVAAYDGAEIPSTNKHLKNNFNSLHNQMRKMPVSHFKEALDVPDYSGMRQSGFFAMSQGFQLNNHGYDVFIHARRESPQSQGKFAGDKFHISVLRDMVPQAFQALSGLLFSEDSPVDKWKVTDMEKVVQQARVSLGAQFTLYIKPDQENSQYSASFLHKTRQFIECLESRLSENGVISGQCPESDVHPENWKYLSYRNELRSGRDGGEMQRQALREEPFYRLMTE | 4.2.3.- | null | null | extracellular region [GO:0005576] | lyase activity [GO:0016829] | PF03536; | 3.30.2430.10; | Phosphothreonine lyase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18284579}. Note=Can be secreted in vitro by either the SPI-1 or SPI-2 type III secretion systems (T3SS). Translocation of the protein into the cytosol of infected macrophages by intracellular bacteria is dependent on the SPI-2 T3SS. Translocated SpvC proteins appear to... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=52.2 uM for the Erk2 phosphopeptide DHTGFL-pT-E-pY-VATR {ECO:0000269|PubMed:18060821}; Vmax=22.72 umol/min/mg enzyme with the Erk2 phosphopeptide DHTGFL-pT-E-pY-VATR as substrate {ECO:0000269|PubMed:18060821}; Note=kcat is 10.60 sec(-1) with the Erk2 phosphopeptide... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:18060821}; | null | FUNCTION: Secreted effector that irreversibly inactivates host MAP kinases by catalyzing the dephosphorylation of the phosphothreonine residue in the pT-X-pY motif in MAPK2/ERK2, MAPK3/ERK1, and p38, via a beta-elimination reaction leading to a dehydrobutyrine residue. Is also able to remove the phosphate group from ph... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A2R8 | CORA_SALTY | MLSAFQLEKNRLTRLEVEESQSLIDAVWVDLVEPDDDERLRVQSELGQSLATRPELEDIEASARFFEDEDGLHIHSFFFFEDAEDHAGNSTVAFTIRDGRLFTLRERELPAFRLYRMRARSQAMVDGNAYELLLDLFETKIEQLADEIENIYSDLEKLSRVIMEGHQGDEYDEALSTLAELEDIGWKVRLCLMDTQRALNFLVRKARLPGGQLEQAREILRDIESLLPHNESLFQKVNFLMQAAMGFINIEQNRIIKIFSVVSVVFLPPTLVASSYGMNFEFMPELKWSFGYPGAIIFMILAGLAPYLYFKRKNWL | null | null | null | plasma membrane [GO:0005886] | cobalt ion transmembrane transporter activity [GO:0015087]; magnesium ion transmembrane transporter activity [GO:0015095]; nickel cation transmembrane transporter activity [GO:0015099] | PF01544; | 1.20.58.340; | CorA metal ion transporter (MIT) (TC 1.A.35) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2548999, ECO:0000269|PubMed:8314774, ECO:0000305|PubMed:10601252}; Multi-pass membrane protein {ECO:0000269|PubMed:8314774}. | CATALYTIC ACTIVITY: Reaction=Mg(2+)(in) = Mg(2+)(out); Xref=Rhea:RHEA:29827, ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:2670893, ECO:0000269|PubMed:3536881}; CATALYTIC ACTIVITY: Reaction=Co(2+)(in) = Co(2+)(out); Xref=Rhea:RHEA:28578, ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:2670893, ECO:0000269|PubMed:3536... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 uM for magnesium ions {ECO:0000269|PubMed:2670893, ECO:0000269|PubMed:3536881}; KM=30 uM for cobalt ions {ECO:0000269|PubMed:3536881}; KM=300 uM for nickel ions {ECO:0000269|PubMed:3536881}; | null | null | null | FUNCTION: Mediates both influx and efflux of magnesium ions (PubMed:10601252, PubMed:10748031, PubMed:2548998, PubMed:2670893, PubMed:3536881, PubMed:9786860). Can also mediate cobalt and nickel uptake, albeit only at extracellular concentrations that are toxic to the cell (PubMed:2670893, PubMed:3536881). Does not tra... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A2T6 | CRP_SALTY | MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMRLSSQMARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKITRQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVVYGTR | null | null | positive regulation of DNA-templated transcription [GO:0045893] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | cAMP binding [GO:0030552]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976] | PF00027;PF13545; | 2.60.120.10;1.10.10.10; | null | null | null | null | null | null | null | null | FUNCTION: A global transcription regulator. Complexes with cyclic AMP (cAMP) which allosterically activates DNA binding to regulate transcription. It can act as an activator, repressor, coactivator or corepressor. Induces a severe bend in DNA. Acts as a negative regulator of its own synthesis as well as for adenylate c... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0A2X8 | ARCC1_ENTFC | MGKKMVVALGGNAILSNDASAHAQQQALVQTSAYLVHLIKQGHRLIVSHGNGPQVGNLLLQQQAADSEKNPAMPLDTCVAMTQGSIGYWLSNALNQELNKAGIKKQVATVLTQVVVDPADEAFKNPTKPIGPFLTEAEAKEAMQAGAIFKEDAGRGWRKVVPSPKPIDIHEAETINTLIKNDIITISCGGGGIPVVGQELKGVEAVIDKDFASEKLAELVDADALVILTGVDYVCINYGKPDEKQLTNVTVAELEEYKQAGHFAPGSMLPKIEAAIQFVESQPNKQAIITSLENLGSMSGDEIVGTVVTK | 2.7.2.2 | null | arginine deiminase pathway [GO:0019546]; phosphorylation [GO:0016310] | cytosol [GO:0005829] | ATP binding [GO:0005524]; carbamate kinase activity [GO:0008804] | PF00696; | 3.40.1160.10; | Carbamate kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate + H(+) + H2O; Xref=Rhea:RHEA:10152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=2.7.2.2; | null | PATHWAY: Metabolic intermediate metabolism; carbamoyl phosphate degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1. | null | null | FUNCTION: Catalyzes the reversible synthesis of carbamate and ATP from carbamoyl phosphate and ADP. Can also catalyze, although with low efficiency, the phosphorylation of bicarbonate, leading to the formation of carboxyphosphate, an unstable intermediate found in the reactions catalyzed by carbamoyl-phosphate synthase... | Enterococcus faecium (Streptococcus faecium) |
P0A386 | CY550_THEVB | MLKKCVWLAVALCLCLWQFTMGTALAAELTPEVLTVPLNSEGKTITLTEKQYLEGKRLFQYACASCHVGGITKTNPSLDLRTETLALATPPRDNIEGLVDYMKNPTTYDGEQEIAEVHPSLRSADIFPKMRNLTEKDLVAIAGHILVEPKILGDKWGGGKVYY | null | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Note=Binds 1 heme c group covalently per subunit. PSII binds multiple chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12881497, ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689, ECO:00... | photosynthesis, light reaction [GO:0019684]; respiratory electron transport chain [GO:0022904] | photosystem II [GO:0009523]; plasma membrane-derived thylakoid membrane [GO:0031676] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF14495; | 1.10.760.10; | Cytochrome c family, PsbV subfamily | null | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12881497, ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786, ECO:... | null | null | null | null | null | FUNCTION: One of the extrinsic, lumenal subunits of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. The extrinsic proteins stabilize the structure of photosystem II ox... | Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1) |
P0A387 | CY550_THEVL | MLKKCVWLAVALCLCLWQFTMGTALAAELTPEVLTVPLNSEGKTITLTEKQYLEGKRLFQYACASCHVGGITKTNPSLDLRTETLALATPPRDNIEGLVDYMKNPTTYDGEQEIAEVHPSLRSADIFPKMRNLTEKDLVAIAGHILVEPKILGDKWGGGKVYY | null | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624, ECO:0000269|PubMed:8397205}; Note=Binds 1 heme c group covalently per subunit. PSII binds multiple chlorophylls, c... | photosynthesis, light reaction [GO:0019684]; respiratory electron transport chain [GO:0022904] | photosystem II [GO:0009523]; plasma membrane-derived thylakoid membrane [GO:0031676] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF14495; | 1.10.760.10; | Cytochrome c family, PsbV subfamily | null | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,... | null | null | null | null | null | FUNCTION: One of the extrinsic, lumenal subunits of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. The extrinsic proteins stabilize the structure of photosystem II ox... | Thermostichus vulcanus (Synechococcus vulcanus) |
P0A3B2 | BIPA_ECO27 | MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCG... | 3.6.5.- | null | ribosome biogenesis [GO:0042254] | cytosol [GO:0005829]; ribonucleoprotein complex [GO:1990904] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; ribosome binding [GO:0043022]; rRNA binding [GO:0019843]; tRNA binding [GO:0000049] | PF21018;PF00679;PF00009;PF03144; | 3.30.70.240;2.40.50.250;3.30.70.870;3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, BipA subfamily | PTM: Phosphorylated on tyrosine, probably by autophosphorylation (Probable) (PubMed:9622352, PubMed:9642082). Phosphorylation is strongly activated by proteins present in strain E2348/69 / EPEC / MAR001 but not K12 / DH5 alpha. Phosphorylation increases GTPase activity (PubMed:9622352). {ECO:0000269|PubMed:9622352, ECO... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00849}. Note=Binds to ribosomes. {ECO:0000255|HAMAP-Rule:MF_00849}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000269|PubMed:9622352}; | null | null | null | null | FUNCTION: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribos... | Escherichia coli O127:H6 (strain E2348/69 / EPEC) |
P0A3C5 | FABH_STRPN | MAFAKISQVAHYVPEQVVTNHDLAQIMDTNDEWISSRTGIRQRHISRTESTSDLATEVAKKLMAKAGITGEELDFIILATITPDSMMPSTAARVQANIGANKAFAFDLTAACSGFVFALSTAEKFIASGRFQKGLVIGSETLSKAVDWSDRSTAVLFGDGAGGVLLEASEQEHFLAESLNSDGSRSECLTYGHSGLHSPFSDQESADSFLKMDGRTVFDFAIRDVAKSIKQTIDESPIEVTDLDYLLLHQANDRILDKMARKIGVDRAKLPANMMEYGNTSAASIPILLSECVEQGLIPLDGSQTVLLSGFGGGLTWGTL... | 2.3.1.180; 2.3.1.300 | null | fatty acid biosynthetic process [GO:0006633] | cytoplasm [GO:0005737] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; beta-ketoacyl-acyl-carrier-protein synthase III activity [GO:0033818] | PF08545;PF08541; | 3.40.47.10; | Thiolase-like superfamily, FabH family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Ru... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40.3 uM for acetyl-CoA {ECO:0000269|PubMed:11375394}; KM=18.6 uM for malonyl-ACP {ECO:0000269|PubMed:11375394}; | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01815}. | null | null | FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
P0A3C7 | FER1_NOSS1 | MATFKVTLINEAEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVDQSDQSFLDDDQIEAGYVLTCVAYPTSDVVIQTHKEEDLY | null | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Note=Binds 1 [2Fe-2S] cluster.; | electron transport chain [GO:0022900] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872] | PF00111; | 3.10.20.30; | 2Fe2S plant-type ferredoxin family | null | null | null | null | null | null | null | FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) |
P0A3C9 | FER_THEVB | MATYKVTLVRPDGSETTIDVPEDEYILDVAEEQGLDLPFSCRAGACSTCAGKLLEGEVDQSDQSFLDDDQIEKGFVLTCVAYPRSDCKILTNQEEELY | null | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Note=Binds 1 [2Fe-2S] cluster.; | electron transport chain [GO:0022900] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872] | PF00111; | 3.10.20.30; | 2Fe2S plant-type ferredoxin family | null | null | null | null | null | null | null | FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1) |
P0A3R0 | MSAB1_STRR6 | MAEIYLAGGCFWGLEEYFSRISGVLETSVGYANGQVETTNYQLLKETDHAETVQVIYDEKEVSLREILLYYFRVIDPLSINQQGNDRGRQYRTGIYYQDEADLPAIYTVVQEQERMLGRKIAVEVEQLRHYILAEDYHQDYLRKNPSGYCHIDVTDADKPLIDAANYEKPSQEVLKASLSEESYRVTQEAATEAPFTNAYDQTFEEGIYVDITTGEPLFFAKDKFASGCGWPSFSRPISKELIHYYKDLSHGMERIEVRSRSGSAHLGHVFTDGPRELGGLRYCINSASLRFVAKDEMEKAGYGYLLPYLNK | 1.8.4.11; 1.8.4.12 | null | protein modification process [GO:0036211]; protein repair [GO:0030091]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | L-methionine:thioredoxin-disulfide S-oxidoreductase activity [GO:0033744]; peptide-methionine (R)-S-oxide reductase activity [GO:0033743]; peptide-methionine (S)-S-oxide reductase activity [GO:0008113] | PF01625;PF01641; | 2.170.150.20;3.30.1060.10; | MsrA Met sulfoxide reductase family; MsrB Met sulfoxide reductase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. | 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: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. {ECO:0000250}. | Streptococcus pneumoniae (strain ATCC BAA-255 / R6) |
P0A407 | PSAB_THEVB | MATKFPKFSQDLAQDPTTRRIWYAIAMAHDFESHDGMTEENLYQKIFASHFGHLAIIFLWVSGSLFHVAWQGNFEQWVQDPVNTRPIAHAIWDPQFGKAAVDAFTQAGASNPVDIAYSGVYHWWYTIGMRTNGDLYQGAIFLLILASLALFAGWLHLQPKFRPSLSWFKNAESRLNHHLAGLFGVSSLAWAGHLIHVAIPESRGQHVGWDNFLSTMPHPAGLAPFFTGNWGVYAQNPDTASHVFGTAQGAGTAILTFLGGFHPQTESLWLTDMAHHHLAIAVLFIVAGHMYRTQFGIGHSIKEMMDAKDFFGTKVEGPFN... | 1.97.1.12 | COFACTOR: Note=PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones a... | photosynthesis [GO:0015979] | photosystem I [GO:0009522]; plasma membrane-derived thylakoid membrane [GO:0031676] | 4 iron, 4 sulfur cluster binding [GO:0051539]; chlorophyll binding [GO:0016168]; electron transfer activity [GO:0009055]; magnesium ion binding [GO:0000287]; oxidoreductase activity [GO:0016491] | PF00223; | 1.20.1130.10; | PsaA/PsaB family | null | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800, ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876}. | CATALYTIC ACTIVITY: Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036, ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChE... | null | null | null | null | FUNCTION: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair ... | Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1) |
P0A411 | PSAC_TRIV2 | MSHTVKIYDTCIGCTQCVRACPTDVLEMVPWDGCKAAQVASSPRTEDCVGCKRCETACPTDFLSIRVYLGAETTRSMGLAY | 1.97.1.12 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.; | photosynthetic electron transport in photosystem I [GO:0009773] | photosystem I [GO:0009522]; plasma membrane-derived thylakoid membrane [GO:0031676] | 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF12838; | 3.30.70.20; | null | null | SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. | CATALYTIC ACTIVITY: Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036, ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChE... | null | null | null | null | FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD ... | Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) |
P0A434 | OPD_BREDI | MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRV... | 3.1.8.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | catabolic process [GO:0009056] | plasma membrane [GO:0005886] | aryldialkylphosphatase activity [GO:0004063]; zinc ion binding [GO:0008270] | PF02126; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Phosphotriesterase family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1; | null | null | null | null | FUNCTION: Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoester... | Brevundimonas diminuta (Pseudomonas diminuta) |
P0A444 | PSBA1_THEVB | MTTTLQRRESANLWERFCNWVTSTDNRLYVGWFGVIMIPTLLAATICFVIAFIAAPPVDIDGIREPVSGSLLYGNNIITGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLIIFHFLLGASCYMGRQWELSYRLGMRPWICVAYSAPLASAFAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHQLGVAGVFGGALFCAMHGSLVTSSLIRETTETESANYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGVWFTALGISTMAFNLNGFNFNHSVIDAKGNVINTWADI... | 1.10.3.9 | COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster o... | photosynthetic electron transport in photosystem II [GO:0009772]; response to herbicide [GO:0009635] | photosystem II [GO:0009523]; plasma membrane-derived thylakoid membrane [GO:0031676] | chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor [GO:0016682]; oxygen evolv... | PF00124; | 1.20.85.10; | Reaction center PufL/M/PsbA/D family | PTM: C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379}.; PTM: Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000303|P... | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873, ECO:... | CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMe... | null | null | null | null | FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that conver... | Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1) |
P0A446 | PSBA2_THEVB | MTTVLQRRQTANLWERFCDWITSTENRLYIGWFGVIMIPTLLAATICFVIAFIAAPPVDIDGIREPVSGSLLYGNNIITAAVVPSSNAIGLHLYPIWDAASLDEWLYNGGPYQLIIFHFLIGIFCYMGREWELSYRLGMRPWIPVAFSAPVAAATAVLLIYPIGQGSFSDGLMLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGALFAAMHGSLVTSSLIRETTETESTNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFAALGISTMAFNLNGFNFNHSVVDAQGNVINTWADI... | 1.10.3.9 | COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster o... | photosynthetic electron transport in photosystem II [GO:0009772]; response to herbicide [GO:0009635] | photosystem II [GO:0009523]; plasma membrane-derived thylakoid membrane [GO:0031676] | chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor [GO:0016682]; oxygen evolv... | PF00124; | 1.20.85.10; | Reaction center PufL/M/PsbA/D family | PTM: C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379}.; PTM: Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379}. | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:19219048}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:19219048}. | CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01379}; | null | null | null | null | FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that conver... | Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1) |
P0A4G2 | MTSA_STRPN | MKKLGTLLVLFLSAIILVACASGKKDTTSGQKLKVVATNSIIADITKNIAGDKIDLHSIVPIGQDPHEYEPLPEDVKKTSEADLIFYNGINLETGGNAWFTKLVENAKKTENKDYFAVSDGVDVIYLEGQNEKGKEDPHAWLNLENGIIFAKNIAKQLSAKDPNNKEFYEKNLKEYTDKLDKLDKESKDKFNKIPAEKKLIVTSEGAFKYFSKAYGVPSAYIWEINTEEEGTPEQIKTLVEKLRQTKVPSLFVESSVDDRPMKTVSQDTNIPIYAQIFTDSIAEQGKEGDSYYSMMKYNLDKIAEGLAK | null | null | cell adhesion [GO:0007155]; metal ion transport [GO:0030001] | plasma membrane [GO:0005886] | metal ion binding [GO:0046872] | PF01297; | 3.40.50.1980; | Bacterial solute-binding protein 9 family, Lipoprotein receptor antigen (Lrai) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. | null | null | null | null | null | FUNCTION: Part of the ATP-binding cassette (ABC) transport system PsaABC involved in manganese import (PubMed:22072971, PubMed:9379902). Binds manganese with high affinity and specificity and delivers it to the membrane permease for translocation into the cytoplasm (PubMed:22072971). Also acts as an adhesin which is in... | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
P0A4Q0 | PLSY_STRR6 | MITIVLLILAYLLGSIPSGLWIGQVFFQINLREHGSGNTGTTNTFRILGKKAGMATFVIDFFKGTLATLLPIIFHLQGVSPLIFGLLAVIGHTFPIFAGFKGGKAVATSAGVIFGFAPIFCLYLAIIFFGALYLGSMISLSSVTASIAAVIGVLLFPLFGFILSNYDSLFIAIILALASLIIIRHKDNIARIKNKTENLVPWGLNLTHQDPKK | 2.3.1.275 | null | phospholipid biosynthetic process [GO:0008654] | plasma membrane [GO:0005886] | acyl-phosphate glycerol-3-phosphate acyltransferase activity [GO:0043772] | PF02660; | null | PlsY family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate; Xref=Rhea:RHEA:34075, ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:59918; EC=2.3.1.275; Evidence={ECO:0000269|PubMed:16949372}; CATALYTIC ACTIVITY: Reaction=hexadecanoyl phosph... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for glycerol-3-phosphate (at 37 degrees Celsius and at pH 7.4) {ECO:0000269|PubMed:17308305}; KM=30 uM for acyl-phosphate (at 37 degrees Celsius and at pH 7.4) {ECO:0000269|PubMed:17308305}; | PATHWAY: Lipid metabolism; phospholipid metabolism. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:17308305}; | null | FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. {ECO:0000269|PubMed:16949372}. | Streptococcus pneumoniae (strain ATCC BAA-255 / R6) |
P0A521 | CH602_MYCBO | MAKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKGAKEVETKEQIAATAAISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDPERQEAVLEDPYILLVSSKVSTVKDLLPLLEKVIGAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLTLENADLSLLGKARK... | 5.6.1.7 | null | chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activation [GO:0050870]; positive regulation of ... | capsule [GO:0042603]; cell surface [GO:0009986]; extracellular region [GO:0005576]; GroEL-GroES complex [GO:1990220] | ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; isomerase activity [GO:0016853]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082] | PF00118; | 3.50.7.10;1.10.560.10;3.30.260.10; | Chaperonin (HSP60) family | null | SUBCELLULAR LOCATION: Secreted, capsule {ECO:0000250|UniProtKB:P9WPE7}. Cell surface {ECO:0000250|UniProtKB:P9WPE7}. Secreted, cell wall {ECO:0000250|UniProtKB:P9WPE7}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00600}; | null | null | null | null | FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. {ECO:0000255|HAMAP-Rule:... | Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) |
P0A698 | UVRA_ECOLI | MDKIEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPAISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKGEHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVVDRFKVRDDLTQRLAESFETALELSGGTAVVADMDDPKAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDRRNFYYFQM... | null | null | DNA repair [GO:0006281]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage recognition [GO:0000715]; nucleotide-excision repair, preincision complex assembly [GO:0006294]; response to radiation [GO:0009314]; SOS response [GO:0009432] | cytosol [GO:0005829]; DNA repair complex [GO:1990391]; excinuclease repair complex [GO:0009380] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; excinuclease ABC activity [GO:0009381]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270] | PF00005;PF17755;PF17760; | 1.10.8.280;1.20.1580.10;3.30.1490.20;3.40.50.300; | ABC transporter superfamily, UvrA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}. | null | null | null | null | null | FUNCTION: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate... | Escherichia coli (strain K12) |
P0A6A0 | UBIB_ECOLI | MTPGEVRRLYFIIRTFLSYGLDELIPKMRITLPLRLWRYSLFWMPNRHKDKLLGERLRLALQELGPVWIKFGQMLSTRRDLFPPHIADQLALLQDKVAPFDGKLAKQQIEAAMGGLPVEAWFDDFEIKPLASASIAQVHTARLKSNGKEVVIKVIRPDILPVIKADLKLIYRLARWVPRLLPDGRRLRPTEVVREYEKTLIDELNLLRESANAIQLRRNFEDSPMLYIPEVYPDYCSEGMMVMERIYGIPVSDVAALEKNGTNMKLLAERGVQVFFTQVFRDSFFHADMHPGNIFVSYEHPENPKYIGIDCGIVGSLNKE... | 2.7.-.- | null | phosphorylation [GO:0016310]; regulation of ubiquinone biosynthetic process [GO:0010795]; ubiquinone biosynthetic process [GO:0006744] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672] | PF03109; | null | ABC1 family, UbiB subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00414, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00414, ECO:0000269|PubMed:15919996}. | null | null | PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation]. | null | null | FUNCTION: Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00414, ECO:0000269|PubMed:10960098, ECO:0000269|PubMed:9422602}. | Escherichia coli (strain K12) |
P0A6A3 | ACKA_ECOLI | MSSKLVLVLNCGSSSLKFAIIDAVNGEEYLSGLAECFHLPEARIKWKMDGNKQEAALGAGAAHSEALNFIVNTILAQKPELSAQLTAIGHRIVHGGEKYTSSVVIDESVIQGIKDAASFAPLHNPAHLIGIEEALKSFPQLKDKNVAVFDTAFHQTMPEESYLYALPYNLYKEHGIRRYGAHGTSHFYVTQEAAKMLNKPVEELNIITCHLGNGGSVSAIRNGKCVDTSMGLTPLEGLVMGTRSGDIDPAIIFHLHDTLGMSVDAINKLLTKESGLLGLTEVTSDCRYVEDNYATKEDAKRAMDVYCHRLAKYIGAYTAL... | 2.7.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00020}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_00020}; Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP-Rule:MF_00020}; | acetate biosynthetic process [GO:0019413]; acetate metabolic process [GO:0006083]; acetyl-CoA biosynthetic process [GO:0006085]; phosphorylation [GO:0016310]; propionate biosynthetic process [GO:0019542]; single-species biofilm formation on inanimate substrate [GO:0044011] | cytosol [GO:0005829]; membrane [GO:0016020] | acetate kinase activity [GO:0008776]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; zinc ion binding [GO:0008270] | PF00871; | 3.30.420.40; | Acetokinase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352, ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00020}; | null | PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00020}. | null | null | FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. During anaerobic growth of the organism, this enzyme is also involved in the synthesis of most of the ATP formed catabolically. The main pathway for acetate production during exponential phase (PubMed:160... | Escherichia coli (strain K12) |
P0A6A8 | ACP_ECOLI | MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEAEKITTVQAAIDYINGHQA | null | null | fatty acid biosynthetic process [GO:0006633]; lipid A biosynthetic process [GO:0009245]; lipid biosynthetic process [GO:0008610]; response to xenobiotic stimulus [GO:0009410] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | acyl binding [GO:0000035]; acyl carrier activity [GO:0000036]; lipid binding [GO:0008289]; phosphopantetheine binding [GO:0031177] | PF00550; | 1.10.1200.10; | Acyl carrier protein (ACP) family | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group. | SUBCELLULAR LOCATION: Cytoplasm. | null | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}. | null | null | FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis. | Escherichia coli (strain K12) |
P0A6B4 | ALR1_ECOLI | MQAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGLLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFFDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWMKLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQSHFDWVRPGIILYGVSPLEDRSTGADFGCQPVMSLTSSLIAVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGD... | 5.1.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:18434499}; | cell wall organization [GO:0071555]; D-alanine biosynthetic process [GO:0030632]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | cytosol [GO:0005829] | alanine racemase activity [GO:0008784]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF00842;PF01168; | 3.20.20.10; | Alanine racemase family | null | null | CATALYTIC ACTIVITY: Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249, ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1; Evidence={ECO:0000269|PubMed:18434499}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.31 mM for D-alanine {ECO:0000269|PubMed:18434499}; KM=1 mM for L-alanine {ECO:0000269|PubMed:18434499}; | PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. {ECO:0000269|PubMed:18434499}.; PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000305|PubMed:18434499}. | null | null | FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. {ECO:0000269|PubMed:18434499}. | Escherichia coli (strain K12) |
P0A6B7 | ISCS_ECOLI | MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDL... | 2.8.1.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:10600118, ECO:0000269|PubMed:12860127}; | [2Fe-2S] cluster assembly [GO:0044571]; detection of UV [GO:0009589]; iron-sulfur cluster assembly [GO:0016226]; L-cysteine catabolic process [GO:0019448]; oxazole or thiazole biosynthetic process [GO:0018131]; selenocysteine catabolic process [GO:0016261]; sulfur compound transport [GO:0072348]; thiamine biosynthetic ... | cytosol [GO:0005829]; IscS-IscU complex [GO:1990330]; IscS-TusA complex [GO:1990329]; L-cysteine desulfurase complex [GO:1990221]; sulfurtransferase complex [GO:1990228] | 2 iron, 2 sulfur cluster binding [GO:0051537]; cysteine desulfurase activity [GO:0031071]; metal ion binding [GO:0046872]; pyridoxal phosphate binding [GO:0030170]; selenocysteine lyase activity [GO:0009000]; sulfur carrier activity [GO:0097163] | PF00266; | 3.90.1150.10;3.40.640.10; | Class-V pyridoxal-phosphate-dependent aminotransferase family, NifS/IscS subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:8663056}... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.7 uM for L-cysteine {ECO:0000269|PubMed:11577100}; Note=kcat is 8.5 min(-1). {ECO:0000269|PubMed:11577100}; | PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305|PubMed:10544286}. | null | null | FUNCTION: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold as... | Escherichia coli (strain K12) |
P0A6B9 | ISCS_ECO57 | MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDL... | 2.8.1.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:20404999}; | [2Fe-2S] cluster assembly [GO:0044571]; tRNA processing [GO:0008033] | cytosol [GO:0005829] | 2 iron, 2 sulfur cluster binding [GO:0051537]; cysteine desulfurase activity [GO:0031071]; metal ion binding [GO:0046872]; pyridoxal phosphate binding [GO:0030170] | PF00266; | 3.90.1150.10;3.40.640.10; | Class-V pyridoxal-phosphate-dependent aminotransferase family, NifS/IscS subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00331}; | null | PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305|PubMed:20404999}. | null | null | FUNCTION: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis (biotin, thiamine, molybdopterin). Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine, then delivers the sulfur... | Escherichia coli O157:H7 |
P0A6C1 | END4_ECOLI | MKYIGAHVSAAGGLANAAIRAAEIDATAFALFTKNQRQWRAAPLTTQTIDEFKAACEKYHYTSAQILPHDSYLINLGHPVTEALEKSRDAFIDEMQRCEQLGLSLLNFHPGSHLMQISEEDCLARIAESINIALDKTQGVTAVIENTAGQGSNLGFKFEHLAAIIDGVEDKSRVGVCIDTCHAFAAGYDLRTPAECEKTFADFARTVGFKYLRGMHLNDAKSTFGSRVDRHHSLGEGNIGHDAFRWIMQDDRFDGIPLILETINPDIWAEEIAWLKAQQTEKAVA | 3.1.21.2 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 3 Zn(2+) ions. Can also bind Mn(2+) ions.; | base-excision repair [GO:0006284]; DNA repair [GO:0006281] | cytosol [GO:0005829] | 3'-5'-DNA exonuclease activity [GO:0008296]; deoxyribonuclease IV (phage-T4-induced) activity [GO:0008833]; DNA binding [GO:0003677]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; endonuclease activity [GO:0004519]; phosphatase activity [GO:0016791]; phosphoric diester hydrolase activity [GO:0... | PF01261; | 3.20.20.150; | AP endonuclease 2 family | null | null | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.; EC=3.1.21.2; | null | null | null | null | FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | Escherichia coli (strain K12) |
P0A6C8 | ARGB_ECOLI | MMNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVIVHGGGCVVDELMKGLNLPVKKKNGLRVTPADQIDIITGALAGTANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNADQAATALAATLGADLILLSDVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHAEQLPALFNGMPMGTRILA | 2.7.2.8 | null | arginine biosynthetic process [GO:0006526]; arginine biosynthetic process via ornithine [GO:0042450]; DNA damage response [GO:0006974]; glutamate metabolic process [GO:0006536]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | acetyl-CoA:L-glutamate N-acetyltransferase activity [GO:0004042]; acetylglutamate kinase activity [GO:0003991]; ATP binding [GO:0005524]; N-acetyl-gamma-glutamyl-phosphate reductase activity [GO:0003942] | PF00696; | 3.40.1160.10; | Acetylglutamate kinase family, ArgB subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00082}. | CATALYTIC ACTIVITY: Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:10393305, ECO:0000269|PubMed:14623187}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for N-acetyl-L-glutamate {ECO:0000269|PubMed:14623187}; KM=0.29 mM for ATP {ECO:0000269|PubMed:14623187}; | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000305}. | null | null | FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:10393305, ECO:0000269|PubMed:14623187}. | Escherichia coli (strain K12) |
P0A6D0 | ARGR_ECOLI | MRSSAKQEELVKAFKALLKEEKFSSQGEIVAALQEQGFDNINQSKVSRMLTKFGAVRTRNAKMEMVYCLPAELGVPTTSSPLKNLVLDIDYNDAVVVIHTSPGAAQLIARLLDSLGKAEGILGTIAGDDTIFTTPANGFTVKDLYEAILELFDQEL | null | null | arginine biosynthetic process [GO:0006526]; negative regulation of DNA-templated transcription initiation [GO:2000143]; plasmid recombination [GO:0042150]; positive regulation of DNA-templated transcription initiation [GO:2000144]; protein complex oligomerization [GO:0051259]; regulation of arginine biosynthetic proces... | cytoplasm [GO:0005737]; transcription regulator complex [GO:0005667] | arginine binding [GO:0034618]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802] | PF01316;PF02863; | 3.30.1360.40;1.10.10.10; | ArgR family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. | null | null | FUNCTION: Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carAB operon. Predominantly interacts with A/T residues in ARG boxes. It also binds to a specific site in cer locus. Thus it is essential for cer-mediated site-specific recombination in ColE1. It is necessary fo... | Escherichia coli (strain K12) |
P0A6D3 | AROA_ECOLI | MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTRCEIIGNGGPLHAEGALELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRLGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVEGDASSASYFLAAAAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGELNAIDMDMNHIPDAAMTIAT... | 2.5.1.19 | null | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423] | cytosol [GO:0005829] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF00275; | 3.65.10.10; | EPSP synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:12430021, ECO:0000269... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.0035 mM for S3P (at pH 7 and 25 degrees Celsius) {ECO:0000269|PubMed:6229418}; KM=0.015 mM for PEP (at pH 7 and 25 degrees Celsius) {ECO:0000269|PubMed:6229418}; KM=0.045 mM for PEP (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:19211556}; KM=0.048 mM for... | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6 and 6.5. {ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556, ECO:0000269|PubMed:6229418}; | null | FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:16... | Escherichia coli (strain K12) |
P0A6D5 | YDIB_ECOLI | MDVTAKYELIGLMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPGAIEGLKALKMRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNTDGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNRRDEFFDKALAFAQRVNENTDCVVTVTDLADQQAFAEALASADILTNGTKVGMKPLENESLVNDISLLHPGLLVTECVYNPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTGKDFPLEYVKQVMGFGA | 1.1.1.282 | null | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; shikimate metabolic process [GO:0019632] | cytosol [GO:0005829] | NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]; quinate 3-dehydrogenase (NAD+) activity [GO:0030266]; quinate 3-dehydrogenase (NADP+) activity [GO:0052733]; shikimate 3-dehydrogenase (NAD+) activity [GO:0052734]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764] | PF18317;PF08501; | 3.40.50.10860;3.40.50.720; | Shikimate dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH; Xref=Rhea:RHEA:22364, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751, ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578, ECO:0000269|PubMed:12637497, ECO:0000269|PubMed:15596430}; CATAL... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.9 uM for shikimate (at pH 9 and 20 degrees Celsius) {ECO:0000269|PubMed:15596430}; KM=9.1 uM for quinate (at pH 9 and 20 degrees Celsius) {ECO:0000269|PubMed:15596430}; KM=12.2 uM for NAD (with shikimate at pH 9 and 20 degrees Celsius) {ECO:0000269|PubMed:1559643... | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_01578}. | null | null | FUNCTION: The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use ... | Escherichia coli (strain K12) |
P0A6D7 | AROK_ECOLI | MAEKRNIFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTGADVGWVFDLEGEEGFRDREEKVINELTEKQGIVLATGGGSVKSRETRNRLSARGVVVYLETTIEKQLARTQRDKKRPLLHVETPPREVLEALANERNPLYEEIADVTIRTDDQSAKVVANQIIHMLESN | 2.7.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305}; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]; response to antibiotic [GO:0046677] | cytosol [GO:0005829] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; shikimate kinase activity [GO:0004765] | PF01202; | 3.40.50.300; | Shikimate kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 mM for shikimate {ECO:0000269|PubMed:3001029}; | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. | null | null | FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. {ECO:0000269|PubMed:1309529}. | Escherichia coli (strain K12) |
P0A6E1 | AROL_ECOLI | MTQPLFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRARETAALEAVTAPSTVIATGGGIILTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAAPEEDLRPTLTGKPLSEEVQEVLEERDALYREVAHIIIDATNEPSQVISEIRSALAQTINC | 2.7.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:3001029}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:3001029}; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytosol [GO:0005829] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; metal ion binding [GO:0046872]; shikimate kinase activity [GO:0004765] | PF01202; | 3.40.50.300; | Shikimate kinase family, AroL subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000269|PubMed:3001029}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=200 uM for shikimate {ECO:0000269|PubMed:3001029}; KM=160 uM for ATP {ECO:0000269|PubMed:3001029}; | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000305|PubMed:3001029}. | null | null | FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. {ECO:0000269|PubMed:3001029, ECO:0000269|PubMed:3026317}. | Escherichia coli (strain K12) |
P0A6E4 | ASSY_ECOLI | MTTILKHLPVGQRIGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQPDEEDYDAIPRRAMEYGAENARLIDCRKQLVAEGIAAIQCGAFHNTTGGLTYFNTTPLGRAVTGTMLVAAMKEDGVNIWGDGSTYKGNDIERFYRYGLLTNAELQIYKPWLDTDFIDELGGRHEMSEFMIACGFDYKMSVEKAYSTDSNMLGATHEAKDLEYLNSSVKIVNPIMGVKFWDESVKIPAEEVTVRFEQGHPVALNGKTFSDDVEMMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALLHIAYERLLTGIHNEDTIEQY... | 6.3.4.5 | null | arginine biosynthetic process [GO:0006526]; argininosuccinate metabolic process [GO:0000053]; urea cycle [GO:0000050] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | argininosuccinate synthase activity [GO:0004055]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF20979;PF00764; | 1.10.287.400;3.90.1260.10;3.40.50.620; | Argininosuccinate synthase family, Type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; | null | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. | null | null | null | Escherichia coli (strain K12) |
P0A6E6 | ATPE_ECOLI | MAMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGNVTVLADTAIRGQDLDEARAMEAKRKAEEHISSSHGDVDYAQASAELAKAIAQLRVIELTKKAM | null | null | proton motive force-driven ATP synthesis [GO:0015986]; proton motive force-driven plasma membrane ATP synthesis [GO:0042777] | plasma membrane [GO:0005886]; proton-transporting ATP synthase complex [GO:0045259]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261] | ATP binding [GO:0005524]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933] | PF00401;PF02823; | 1.20.5.440;2.60.15.10; | ATPase epsilon chain family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229}; Peripheral membrane protein {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229}. | null | null | null | null | null | FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. | Escherichia coli (strain K12) |
P0A6F1 | CARA_ECOLI | MIKSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLVIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDNPDAALALEKARAFPGLNGMDLAKEVTTAEAYSWTQGSWTLTGGLPEAKKEDELPFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEAT... | 6.3.5.5 | null | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; arginine biosynthetic process [GO:0006526]; glutamine metabolic process [GO:0006541]; pyrimidine nucleobase biosynthetic process [GO:0019856] | carbamoyl-phosphate synthase complex [GO:0005951]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; glutaminase activity [GO:0004359]; protein heterodimerization activity [GO:0046982] | PF00988;PF00117; | 3.40.50.880;3.50.30.20; | CarA family | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI... | null | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01209, ECO:0000305|Ref.10}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_01209, ECO:00... | null | null | FUNCTION: Small subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and... | Escherichia coli (strain K12) |
P0A6F3 | GLPK_ECOLI | MTEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTLVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPISGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYALEGAVFMAGASIQWLRDE... | 2.7.1.30 | null | DNA damage response [GO:0006974]; glycerol catabolic process [GO:0019563]; glycerol metabolic process [GO:0006071]; glycerol-3-phosphate biosynthetic process [GO:0046167]; phosphorylation [GO:0016310]; triglyceride metabolic process [GO:0006641] | cytosol [GO:0005829] | ATP binding [GO:0005524]; glycerol kinase activity [GO:0004370]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; zinc ion binding [GO:0008270] | PF02782;PF00370; | 3.30.420.40; | FGGY kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216; EC=2.7.1.30; Evidence={ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:5335908}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 uM for glycerol {ECO:0000269|PubMed:2985549, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908, ECO:0000269|PubMed:9817843}; KM=400 uM for D-glyceraldehyde {ECO:0000269|PubMed:2985549, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908, ECO:0000269|Pub... | PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00186}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.8. {ECO:0000269|PubMed:2985549, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908, ECO:0000269|PubMed:9817843}; | null | FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP. {ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:2... | Escherichia coli (strain K12) |
P0A6F5 | CH60_ECOLI | MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQA... | 5.6.1.7 | null | chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activation [GO:0050870]; positive regulation of ... | cytosol [GO:0005829]; GroEL-GroES complex [GO:1990220]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; identical protein binding [GO:0042802]; isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082] | PF00118; | 3.50.7.10;1.10.560.10;3.30.260.10; | Chaperonin (HSP60) family | PTM: Phosphorylated reversibly during heat shock. {ECO:0000269|PubMed:1349729}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000269|PubMed:20094032, ECO:0000269|PubMed:22380631}. Note=Uniformly located in the cytoplasm (PubMed:20094032). Exclusively localized in foci, usually near 1 cell pole in mid-to-late exponential phase (PubMed:22380631); polar localization depends o... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000269|PubMed:9285585, ECO:0000269|PubMed:9285593}; | null | null | null | null | FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding (PubMed:10532860, PubMed:16751100, PubMed:1676490, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391, PubMed:2573517, PubMed:2897629, PubMed:8104102, PubMed:9285593). The GroEL-GroES system forms a nan... | Escherichia coli (strain K12) |
P0A6F9 | CH10_ECOLI | MNIRPLHDRVIVKRKEVETKSAGGIVLTGSAAAKSTRGEVLAVGNGRILENGEVKPLDVKVGDIVIFNDGYGVKSEKIDNEEVLIMSESDILAIVEA | null | null | chaperone cofactor-dependent protein refolding [GO:0051085]; protein folding [GO:0006457]; response to heat [GO:0009408]; virion assembly [GO:0019068] | cytosol [GO:0005829]; GroEL-GroES complex [GO:1990220] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein folding chaperone [GO:0044183]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082] | PF00166; | 2.30.33.40; | GroES chaperonin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580, ECO:0000269|PubMed:22380631}. Note=Exclusively localized in foci, usually near 1 cell pole in mid-to-late exponential phase; polar localization depends on the minCDE operon. Foci form near midcell. | null | null | null | null | null | FUNCTION: Together with the chaperonin GroEL, plays an essential role in assisting protein folding (PubMed:10532860, PubMed:16751100, PubMed:1676490, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391, PubMed:2573517, PubMed:2897629). The GroEL-GroES system forms a nano-cage that allows encapsulation of... | Escherichia coli (strain K12) |
P0A6G7 | CLPP_ECOLI | MSYSGERDNFAPHMALVPMVIEQTSRGERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN | 3.4.21.92 | null | positive regulation of programmed cell death [GO:0043068]; proteasomal protein catabolic process [GO:0010498]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; proteolysis [GO:0006508]; response to heat [GO:0009408]; response to radiation [GO:0009314]; response to temperature sti... | cytosol [GO:0005829]; endopeptidase Clp complex [GO:0009368]; HslUV protease complex [GO:0009376]; membrane [GO:0016020] | ATP-dependent peptidase activity [GO:0004176]; ATPase binding [GO:0051117]; identical protein binding [GO:0042802]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00574; | null | Peptidase S14 family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.4 mM for N-succinyl-Leu-Tyr-7-amino-4-methyl-coumarin (N-succinyl-Leu-Tyr-AMC) {ECO:0000269|PubMed:16406682, ECO:0000269|PubMed:20637416}; KM=1 mM for N-succinyl-Leu-Tyr-AMC {ECO:0000269|PubMed:16406682, ECO:0000269|PubMed:20637416}; | null | null | null | FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX... | Escherichia coli (strain K12) |
P0A6H1 | CLPX_ECOLI | MTDKRKDGSGKLLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREEIKEVAPHRERSALPTPHEIRNHLDDYVIGQEQAKKVLAVAVYNHYKRLRNGDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRVETGSGIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSEE... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 Zn(2+) ion per subunit.; | cell division [GO:0051301]; protein denaturation [GO:0030164]; protein unfolding [GO:0043335]; proteolysis involved in protein catabolic process [GO:0051603] | cytosol [GO:0005829]; endopeptidase Clp complex [GO:0009368]; HslUV protease complex [GO:0009376] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; protein dimerization activity [GO:0... | PF07724;PF10431;PF06689; | 1.10.8.60;6.20.220.10;3.40.50.300; | ClpX chaperone family | null | null | null | null | null | null | null | FUNCTION: ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of Rs... | Escherichia coli (strain K12) |
P0A6H5 | HSLU_ECOLI | MSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDAAVKMVRVQAIEKNRYRAEELAEERILDVLIPPAKNNWGQTEQQQEPSAARQAFRKKLREGQLDDKEIEIDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQIAKPSDLIP... | null | null | cellular response to heat [GO:0034605]; protein denaturation [GO:0030164]; protein unfolding [GO:0043335]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; response to heat [GO:0009408] | cytosol [GO:0005829]; HslUV protease complex [GO:0009376]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; peptidase activity [GO:0008233]; proteasome-activating activity [GO:0036402]; protein domain specific binding [GO:0019904] | PF00004;PF07724; | 1.10.8.60;1.10.8.10;3.40.50.300; | ClpX chaperone family, HslU subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.31 mM for ATP (in the absence of HslV) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; KM=0.28 mM for ATP (in the presence of HslV) {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; KM=5.2 uM for Arc-MYL-st11 (at 37 degrees Celsius) {ECO:00002... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828}; | FUNCTION: ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds th... | Escherichia coli (strain K12) |
P0A6H8 | CLSA_ECOLI | MTTVYTLVSWLAILGYWLLIAGVTLRILMKRRAVPSAMAWLLIIYILPLVGIIAYLAVGELHLGKRRAERARAMWPSTAKWLNDLKACKHIFAEENSSVAAPLFKLCERRQGIAGVKGNQLQLMTESDDVMQALIRDIQLARHNIEMVFYIWQPGGMADQVAESLMAAARRGIHCRLMLDSAGSVAFFRSPWPELMRNAGIEVVEALKVNLMRVFLRRMDLRQHRKMIMIDNYIAYTGSMNMVDPRYFKQDAGVGQWIDLMARMEGPIATAMGIIYSCDWEIETGKRILPPPPDVNIMPFEQASGHTIHTIASGPGFPED... | 2.7.8.- | null | cardiolipin biosynthetic process [GO:0032049] | cell pole [GO:0060187]; membrane [GO:0016020]; plasma membrane [GO:0005886] | cardiolipin synthase activity [GO:0008808] | PF13091;PF13396; | 3.30.870.10; | Phospholipase D family, Cardiolipin synthase subfamily, ClsA sub-subfamily | PTM: Seems to be post-translationally processed from a 53-55 kDa form to a 45-46 kDa form (PubMed:19341704, PubMed:7665497). | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00190, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:1663113, ECO:0000269|PubMed:19341704}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00190, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:1663113}. | CATALYTIC ACTIVITY: Reaction=2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol; Xref=Rhea:RHEA:31451, ChEBI:CHEBI:17754, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000255|HAMAP-Rule:MF_00190, ECO:0000269|PubMed:1663113}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:1663113}; | null | FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. {ECO:0000255|HAMAP-Rule:MF_00190, ECO:0000269|PubMed:1663113, ECO:0000269|PubMed:22988102}. | Escherichia coli (strain K12) |
P0A6I0 | KCY_ECOLI | MTAIAPVITIDGPSGAGKGTLCKAMAEALQWHLLDSGAIYRVLALAALHHHVDVASEDALVPLASHLDVRFVSTNGNLEVILEGEDVSGEIRTQEVANAASQVAAFPRVREALLRRQRAFRELPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEKGFSVNFERLLAEIKERDDRDRNRAVAPLVPAADALVLDSTTLSIEQVIEKALQYARQKLALA | 2.7.4.25 | null | nucleobase-containing small molecule interconversion [GO:0015949]; phosphorylation [GO:0016310]; pyrimidine nucleotide metabolic process [GO:0006220]; response to X-ray [GO:0010165] | cytosol [GO:0005829] | ATP binding [GO:0005524]; CMP kinase activity [GO:0036430]; cytidylate kinase activity [GO:0004127]; dCMP kinase activity [GO:0036431]; guanosine tetraphosphate binding [GO:0097216] | PF02224; | 3.40.50.300; | Cytidylate kinase family, Type 1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000269|PubMed:7836281, ECO:0000269|PubMed:9126287}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:3... | null | null | null | null | FUNCTION: ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors. {ECO:0000269|PubMed:7836281, ECO:0000269|PubMed:8190075}. | Escherichia coli (strain K12) |
P0A6I6 | COAD_ECOLI | MQKRAIYPGTFDPITNGHIDIVTRATQMFDHVILAIAASPSKKPMFTLEERVALAQQATAHLGNVEVVGFSDLMANFARNQHATVLIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSSLVKEVARHQGDVTHFLPENVHQALMAKLA | 2.7.7.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11812124}; Note=Crystallized in the absence of Mg(2+), the catalytic metal is not bound by the protein but probably by non-esterified oxygen atoms from ATP and/or ordered H(2)O (PubMed:11812124). {ECO:0000305|PubMed:11812124}; | coenzyme A biosynthetic process [GO:0015937] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; pantetheine-phosphate adenylyltransferase activity [GO:0004595] | PF01467; | 3.40.50.620; | Bacterial CoaD family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}. | CATALYTIC ACTIVITY: Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328, ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:10480925, ECO:0000269|PubMe... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 uM for 3'-dephospho-CoA {ECO:0000269|PubMed:10480925}; KM=17 uM for 3'-dephospho-CoA {ECO:0000269|PubMed:17873050}; KM=0.22 mM for diphosphate {ECO:0000269|PubMed:10480925}; KM=0.23 mM for diphosphate {ECO:0000269|PubMed:17873050}; KM=220 uM for ATP {ECO:0000269|... | PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00151}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.9. {ECO:0000269|PubMed:10480925}; | null | FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (PubMed:10480925, PubMed:17873050). CoA is not a substrate for the enzyme (PubMed:10480925). {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:10480925, ECO:0000269|PubMed:17873050}. | Escherichia coli (strain K12) |
P0A6J1 | CYSC_ECOLI | MALHDENVVWHSHPVTVQQRELHHGHRGVVLWFTGLSGSGKSTVAGALEEALHKLGVSTYLLDGDNVRHGLCSDLGFSDADRKENIRRVGEVANLMVEAGLVVLTAFISPHRAERQMVRERVGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPESAEIHLNGEQLVTNLVQQLLDLLRQNDIIRS | 2.7.1.25 | null | 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; hydrogen sulfide biosynthetic process [GO:0070814]; phosphorylation [GO:0016310]; sulfate assimilation [GO:0000103] | null | adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; identical protein binding [GO:0042802] | PF01583; | 3.40.50.300; | APS kinase family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339, ChEBI:CHEBI:456216; EC=2.7.1.25; Evidence={ECO:0000269|PubMed:1332767}; | null | PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3. {ECO:0000305|PubMed:1332767}. | null | null | FUNCTION: Catalyzes the synthesis of activated sulfate. | Escherichia coli (strain K12) |
P0A6J3 | CYSZ_ECOLI | MVSSFTSAPRSGFYYFAQGWKLVSQPGIRRFVILPLLVNILLMGGAFWWLFTQLDVWIPTLMSYVPDWLQWLSYLLWPLAVISVLLVFGYFFSTIANWIAAPFNGLLAEQLEARLTGATPPDTGIFGIMKDVPRIMKREWQKFAWYLPRAIVLLILYFIPGIGQTVAPVLWFLFSAWMLAIQYCDYPFDNHKVPFKEMRTALRTRKITNMQFGALTSLFTMIPLLNLFIMPVAVCGATAMWVDCYRDKHAMWR | null | null | cysteine biosynthetic process [GO:0019344]; sulfate assimilation [GO:0000103]; sulfate transmembrane transport [GO:1902358] | plasma membrane [GO:0005886] | high-affinity sulfate:proton symporter activity [GO:0009675]; sulfate transmembrane transporter activity [GO:0015116] | PF07264; | null | CysZ family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00468, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00468}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.72 uM for sulfate {ECO:0000269|PubMed:24657232}; KM=1.3 uM for sulfate (in the presence of 5 uM sulfite) {ECO:0000269|PubMed:24657232}; | null | null | null | FUNCTION: High affinity, high specificity proton-dependent sulfate transporter, which mediates sulfate uptake. Provides the sulfur source for the cysteine synthesis pathway. Does not transport thiosulfate. {ECO:0000269|PubMed:24657232}. | Escherichia coli (strain K12) |
P0A6J5 | DADA_ECOLI | MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQISPGYAAPWAAPGVPLKAIKWMFQRHAPLAVRLDGTQFQLKWMWQMLRNCDTSHYMENKGRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIAVLEDAGVPYQLLESSRLAEVEPALAEVAHKLTGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCGDEVIKADAYVMAFGSYSTAMLKGIVDIPVYPLKGYSLTIPIAQEDGAPVSTILDETYKIAITRFDNRIRVGGMAEIVGFN... | 1.4.99.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; | D-alanine catabolic process [GO:0055130]; L-alanine oxidation to pyruvate via D-alanine [GO:0019480] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | D-amino-acid dehydrogenase activity [GO:0008718]; protein homodimerization activity [GO:0042803] | PF01266; | 3.30.9.10;3.50.50.60; | DadA oxidoreductase family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424}; Peripheral membrane protein {ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424}. | CATALYTIC ACTIVITY: Reaction=A + a D-alpha-amino acid + H2O = a 2-oxocarboxylate + AH2 + NH4(+); Xref=Rhea:RHEA:18125, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; Evidence={ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 mM for D-alanine {ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424}; KM=6.4 mM for 3,4-dehydro-D-proline {ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424}; | PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and pyruvate from D-alanine: step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 8.9 with D-alanine as substrate and about 9 with 3,4-dehydro-D-proline as substrate. {ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424}; | null | FUNCTION: Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D-serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sol... | Escherichia coli (strain K12) |
P0A6K1 | DAPF_ECOLI | MQFSKMHGLGNDFMVVDAVTQNVFFSPELIRRLADRHLGVGFDQLLVVEPPYDPELDFHYRIFNADGSEVAQCGNGARCFARFVRLKGLTNKRDIRVSTANGRMVLTVTDDDLVRVNMGEPNFEPSAVPFRANKAEKTYIMRAAEQTILCGVVSMGNPHCVIQVDDVDTAAVETLGPVLESHERFPERANIGFMQVVKREHIRLRVYERGAGETQACGSGACAAVAVGIQQGLLAEEVRVELPGGRLDIAWKGPGHPLYMTGPAVHVYDGFIHL | 5.1.1.7 | null | lysine biosynthetic process via diaminopimelate [GO:0009089] | cytosol [GO:0005829] | diaminopimelate epimerase activity [GO:0008837]; enzyme activator activity [GO:0008047]; protein homodimerization activity [GO:0042803] | PF01678; | null | Diaminopimelate epimerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609, ChEBI:CHEBI:57791; EC=5.1.1.7; Evidence={ECO:0000269|PubMed:3042781, ECO:0000269|PubMed:6378903}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.16 mM for D,L-DAP (at pH 7.8 and at 25 degrees Celsius) {ECO:0000269|PubMed:3042781, ECO:0000269|PubMed:6378903}; KM=0.26 mM for L,L-DAP (at pH 7.8 and at 25 degrees Celsius) {ECO:0000269|PubMed:3042781, ECO:0000269|PubMed:6378903}; KM=0.36 mM for L,L-DAP (at pH ... | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. {ECO:0000305|PubMed:3283102}. | null | null | FUNCTION: Involved in the succinylase branch of the L-lysine biosynthesis and in the biosynthesis of the pentapeptide incorporated in the peptidoglycan moiety (PubMed:3283102). Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP) (PubMed:3031013, PubMed:3042781,... | Escherichia coli (strain K12) |
P0A6K3 | DEF_ECOLI | MSVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYAEEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEKSGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFELEADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEKLDRLKARA | 3.5.1.88 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:9610360, ECO:0000269|PubMed:9846875}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:8244948, ECO:0000305|PubMed:7896716}; Note=Upon overproduction is isolated with 1 Fe(2+) ion per monomer, a Ni(2+)-bound form is as active w... | co-translational protein modification [GO:0043686]; translation [GO:0006412] | cytosol [GO:0005829] | ferrous iron binding [GO:0008198]; hydrolase activity [GO:0016787]; peptide deformylase activity [GO:0042586]; ribosome binding [GO:0043022]; zinc ion binding [GO:0008270] | PF01327; | 3.90.45.10; | Polypeptide deformylase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]; Xref=Rhea:RHEA:24420, Rhea:RHEA-COMP:10639, Rhea:RHEA-COMP:10640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740, ChEBI:CHEBI:49298, ChEBI:CHEBI:64731; EC=3.5.1.88; Evidence={ECO:0000269|PubMed:7896716}; Phy... | null | null | null | null | FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins (PubMed:7896716). Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. {ECO:0000269|PubMed:7896716, ECO:000... | Escherichia coli (strain K12) |
P0A6K6 | DEOB_ECOLI | MKRAFIMVLDSFGIGATEDAERFGDVGADTLGHIAEACAKGEADNGRKGPLNLPNLTRLGLAKAHEGSTGFIPAGMDGNAEVIGAYAWAHEMSSGKDTPSGHWEIAGVPVLFEWGYFSDHENSFPQELLDKLVERANLPGYLGNCHSSGTVILDQLGEEHMKTGKPIFYTSADSVFQIACHEETFGLDKLYELCEIAREELTNGGYNIGRVIARPFIGDKAGNFQRTGNRHDLAVEPPAPTVLQKLVDEKHGQVVSVGKIADIYANCGITKKVKATGLDALFDATIKEMKEAGDNTIVFTNFVDFDSSWGHRRDVAGYAA... | 5.4.2.7 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_00740, ECO:0000269|PubMed:4992818}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:4992818}; Note=Binds 2 manganese ions (By similarity). Mn(2+) and Co(2+) are equally good activators (PubMed:4992818). Can also use Ni(... | 5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; cellular metabolic compound salvage [GO:0043094]; deoxyribonucleotide catabolic process [GO:0009264]; DNA damage response [GO:0006974] | cytosol [GO:0005829] | magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; phosphopentomutase activity [GO:0008973] | PF01676; | 3.40.720.10;3.30.70.1250; | Phosphopentomutase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00740, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-D-ribose 5-phosphate; Xref=Rhea:RHEA:27658, ChEBI:CHEBI:57259, ChEBI:CHEBI:62877; EC=5.4.2.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00740, ECO:0000269|PubMed:1089430, ECO:0000269|PubMed:4992818}; CATALYTIC ACTIVITY: Reaction=alpha-D-ribose 1-phosph... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for deoxy-ribose 1-phosphate {ECO:0000269|PubMed:4992818}; KM=43 uM for ribose 1-phosphate {ECO:0000269|PubMed:4992818}; | PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00740, ECO:0000305|PubMed:4992818}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:4992818}; | null | FUNCTION: Isomerase that catalyzes the conversion of deoxy-ribose 1-phosphate (dRib-1-P) and ribose 1-phosphate (Rib-1-P) to deoxy-ribose 5-phosphate (dRib-5-P) and ribose 5-phosphate (Rib-5-P), respectively. {ECO:0000255|HAMAP-Rule:MF_00740, ECO:0000269|PubMed:1089430, ECO:0000269|PubMed:4992818}. | Escherichia coli (strain K12) |
P0A6L0 | DEOC_ECOLI | MTDLKASSLRALKLMDLTTLNDDDTDEKVIALCHQAKTPVGNTAAICIYPRFIPIARKTLKEQGTPEIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIKAGADFIKTSTGKVAVNATPESARIMMEVIRDMGVEKTVGFKPAGGVRTAEDAQKYLAIADELFGADWADARHYRFGASSLLASLLKALGHGDGKSASSY | 4.1.2.4 | null | carbohydrate catabolic process [GO:0016052]; deoxyribonucleotide catabolic process [GO:0009264]; deoxyribose phosphate catabolic process [GO:0046386]; DNA damage response [GO:0006974]; nucleobase-containing small molecule interconversion [GO:0015949] | cytosol [GO:0005829]; membrane [GO:0016020] | deoxyribose-phosphate aldolase activity [GO:0004139]; lyase activity [GO:0016829] | PF01791; | 3.20.20.70; | DeoC/FbaB aldolase family, DeoC type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343, ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000269|PubMed:11598300, ECO:0000269|PubMed:17905878, ECO:0000269|PubMed:6749... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for 2-deoxy-D-ribose 5-phosphate {ECO:0000269|PubMed:17905878}; | PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 for 2-deoxy-D-ribose 5-phosphate cleavage. {ECO:0000269|PubMed:17905878}; | null | FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate (PubMed:11598300, PubMed:17905878, PubMed:6749498). Can also catalyze the double aldol condensation of three acetaldehyde molecules, leading to the formation of 2,4,6-trideoxyhe... | Escherichia coli (strain K12) |
P0A6L2 | DAPA_ECOLI | MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIKEATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHAGLL | 4.3.3.7 | null | diaminopimelate biosynthetic process [GO:0019877]; glyoxylate catabolic process [GO:0009436]; lysine biosynthetic process via diaminopimelate [GO:0009089] | cytosol [GO:0005829] | 4-hydroxy-2-oxoglutarate aldolase activity [GO:0008700]; 4-hydroxy-tetrahydrodipicolinate synthase activity [GO:0008840]; identical protein binding [GO:0042802] | PF00701; | 3.20.20.70; | DapA family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|Pub... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.26 mM for pyruvate {ECO:0000269|PubMed:14580236, ECO:0000269|PubMed:15066435}; KM=0.11 mM for L-aspartate-4-semialdehyde {ECO:0000269|PubMed:14580236, ECO:0000269|PubMed:15066435}; Vmax=0.58 umol/sec/mg enzyme {ECO:0000269|PubMed:14580236, ECO:0000269|PubMed:1506... | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00418}. | null | null | FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). {ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|PubMed:20503968, ECO:0000269|PubMed:8993314}. | Escherichia coli (strain K12) |
P0A6L4 | NANA_ECOLI | MATNLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCVSTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQERG | 4.1.3.3 | null | carbohydrate metabolic process [GO:0005975]; N-acetylneuraminate catabolic process [GO:0019262]; single-species biofilm formation [GO:0044010] | cytosol [GO:0005829] | identical protein binding [GO:0042802]; N-acetylneuraminate lyase activity [GO:0008747] | PF00701; | 3.20.20.70; | DapA family, NanA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=aceneuramate = N-acetyl-D-mannosamine + pyruvate; Xref=Rhea:RHEA:23296, ChEBI:CHEBI:15361, ChEBI:CHEBI:17122, ChEBI:CHEBI:173083; EC=4.1.3.3; Evidence={ECO:0000269|PubMed:12711733, ECO:0000269|PubMed:1646603, ECO:0000269|PubMed:24521460, ECO:0000269|PubMed:33895133}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.3 mM for N-acetylneuraminate {ECO:0000269|PubMed:1646603}; KM=2.5 mM for N-acetylneuraminate {ECO:0000269|PubMed:12711733}; KM=2.2 mM for N-acetylneuraminate {ECO:0000269|PubMed:24521460}; KM=3.3 mM for N-glycollylneuraminate {ECO:0000269|PubMed:1646603}; Vmax=71... | PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 1/5. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:1646603}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius. {ECO:0000269|PubMed:1646603}; | FUNCTION: Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate (PubMed:12711733, PubMed:1646603, PubMed:24521460, PubMed:33895133). Experiments show the true substrate is aceneuramate (linearized Neu5Ac)... | Escherichia coli (strain K12) |
P0A6M2 | DSBB_ECOLI | MLRFLNQCSQGRGAWLLMAFTALALELTALWFQHVMLLKPCVLCIYERCALFGVLGAALIGAIAPKTPLRYVAMVIWLYSAFRGVQLTYEHTMLQLYPSPFATCDFMVRFPEWLPLDKWVPQVFVASGDCAERQWDFLGLEMPQWLLGIFIAYLIVAVLVVISQPFKAKKRDLFGR | null | null | protein folding [GO:0006457]; response to heat [GO:0009408] | plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor [GO:0016672]; protein-disulfide reductase activity [GO:0015035]; ubiquinone binding [GO:0048039] | PF02600; | 1.20.1550.10; | DsbB family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:7957076, ECO:0000269|PubMed:8430071}; Multi-pass membrane protein {ECO:0000269|PubMed:7957076, ECO:0000269|PubMed:8430071}. | null | null | null | null | null | FUNCTION: Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/... | Escherichia coli (strain K12) |
P0A6M4 | DTD_ECOLI | MIALIQRVTRASVTVEGEVTGEIGAGLLVLLGVEKDDDEQKANRLCERVLGYRIFSDAEGKMNLNVQQAGGSVLVVSQFTLAADTERGMRPSFSKGASPDRAEALYDYFVERCRQQEMNTQTGRFAADMQVSLVNDGPVTFWLQV | 3.1.1.96 | null | aminoacyl-tRNA metabolism involved in translational fidelity [GO:0106074]; D-amino acid catabolic process [GO:0019478]; response to heat [GO:0009408]; tRNA metabolic process [GO:0006399] | cytoplasm [GO:0005737] | aminoacyl-tRNA editing activity [GO:0002161]; D-aminoacyl-tRNA deacylase activity [GO:0051499]; D-tyrosyl-tRNA(Tyr) deacylase activity [GO:0051500]; Gly-tRNA(Ala) hydrolase activity [GO:0106026]; protein homodimerization activity [GO:0042803]; Ser(Gly)-tRNA(Ala) hydrolase activity [GO:0043908]; tRNA binding [GO:0000049... | PF02580; | 3.50.80.10; | DTD family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518, ECO:0000305|PubMed:4292198}. | CATALYTIC ACTIVITY: Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala); Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96; Evidence={ECO:0000255|HAMAP-Rule:MF_00518, ECO:0000269|PubMed:283... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for D-tyrosyl-tRNA(Tyr) {ECO:0000269|PubMed:10383414}; KM=1 uM for glycyl-tRNA(Gly) {ECO:0000269|PubMed:27224426}; Note=kcat/KM is 6 uM(-1)sec(-1) for D-tyrosyl-tRNA(Tyr) (PubMed:10383414). kcat/KM is 2.8 uM(-1)sec(-1) for D-tryptophanyl-tRNA(Trp) (PubMed:1091... | null | null | null | FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid (PubMed:10383414, PubMed:10918062, PubMed:24302572, PubMed:27224426, PubMed:4292198). Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS (PubM... | Escherichia coli (strain K12) |
P0A6M8 | EFG_ECOLI | MARTTPIARYRNIGISAHIDAGKTTTTERILFYTGVNHKIGEVHDGAATMDWMEQEQERGITITSAATTAFWSGMAKQYEPHRINIIDTPGHVDFTIEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQANKYKVPRIAFVNKMDRMGANFLKVVNQIKTRLGANPVPLQLAIGAEEHFTGVVDLVKMKAINWNDADQGVTFEYEDIPADMVELANEWHQNLIESAAEASEELMEKYLGGEELTEAEIKGALRQRVLNNEIILVTCGSAFKNKGVQAMLDAVIDYLPSPVDVPAINGILDDGKDTPAERHASDDEPFSAL... | 3.6.5.- | null | ribosome disassembly [GO:0032790]; translational elongation [GO:0006414] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; translation elongation factor activity [GO:0003746] | PF00679;PF14492;PF03764;PF00009;PF03144; | 3.30.230.10;3.30.70.240;3.30.70.870;3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-G/EF-2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:8985244}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:8985244}; | null | null | null | null | FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:8985244). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to th... | Escherichia coli (strain K12) |
P0A6N4 | EFP_ECOLI | MATYYSNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVVDMNLTYLYNDGEFWHFMNNETFEQLSADAKAIGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEIVDTDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSRVK | null | null | negative regulation of translational frameshifting [GO:2001125]; rescue of stalled ribosome [GO:0072344]; translational elongation [GO:0006414] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ribosome binding [GO:0043022]; translation elongation factor activity [GO:0003746] | PF01132;PF08207;PF09285; | 2.30.30.30;2.40.50.140; | Elongation factor P family | PTM: Is beta-lysylated on the epsilon-amino group of Lys-34 by the combined action of EpmA and EpmB, and then hydroxylated on the C5 position of the same residue by EpmC. Lysylation is critical for the stimulatory effect of EF-P on peptide-bond formation. The lysylation moiety would extend toward the peptidyltransferas... | SUBCELLULAR LOCATION: Cytoplasm. | null | null | PATHWAY: Protein biosynthesis; polypeptide chain elongation. | null | null | FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Beta-lysylation at Lys-34 is required for alleviation. The Pro codons and ... | Escherichia coli (strain K12) |
P0A6P1 | EFTS_ECOLI | MAEITASLVKELRERTGAGMMDCKKALTEANGDIELAIENMRKSGAIKAAKKAGNVAADGVIKTKIDGNYGIILEVNCQTDFVAKDAGFQAFADKVLDAAVAGKITDVEVLKAQFEEERVALVAKIGENINIRRVAALEGDVLGSYQHGARIGVLVAAKGADEELVKHIAMHVAASKPEFIKPEDVSAEVVEKEYQVQLDIAMQSGKPKEIAEKMVEGRMKKFTGEVSLTGQPFVMEPSKTVGQLLKEHNAEVTGFIRFEVGEGIEKVETDFAAEVAAMSKQS | null | null | translational elongation [GO:0006414] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; guanyl-nucleotide exchange factor complex [GO:0032045]; membrane [GO:0016020] | guanyl-nucleotide exchange factor activity [GO:0005085]; translation elongation factor activity [GO:0003746]; zinc ion binding [GO:0008270] | PF00889; | 1.10.286.20;1.10.8.10;3.30.479.20; | EF-Ts family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}. | null | null | null | null | null | FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. {ECO:0000255|HAMAP-Rule:MF_00050}.; FUNCTION: (Microbial infection) In case of infection by bacteriophage Qbeta (and related Le... | Escherichia coli (strain K12) |
P0A6P5 | DER_ECOLI | MVPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEIEGREFICIDTGGIDGTEDGVETRMAEQSLLAIEEADVVLFMVDARAGLMPADEAIAKHLRSREKPTFLVANKTDGLDPDQAVVDFYSLGLGEIYPIAASHGRGVLSLLEHVLLPWMEDLAPQEEVDEDAEYWAQFEAEENGEEEEEDDFDPQSLPIKLAIVGRPNVGKSTLTNRILGEERVVVYDMPGTTRDSIYIPMERDGREYVLIDTAGVRKRGKITDAVEKFSVIKTLQAIEDANVVMLVIDAREGISDQDLSLLGFILNSGRSLVIVV... | null | null | ribosome biogenesis [GO:0042254] | cytosol [GO:0005829] | GTP binding [GO:0005525]; GTPase activating protein binding [GO:0032794]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; ribosomal large subunit binding [GO:0043023]; ribosome binding [GO:0043022] | PF14714;PF01926; | 3.30.300.20;3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, EngA (Der) GTPase family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=125 uM for GTP (to 143 uM) in the absence of YihI {ECO:0000269|PubMed:16930151, ECO:0000269|PubMed:20434458}; KM=59.2 uM for GTP in the presence of full-length YihI {ECO:0000269|PubMed:16930151, ECO:0000269|PubMed:20434458}; KM=50.1 uM for GTP in the presence of N-... | null | null | null | FUNCTION: GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defecti... | Escherichia coli (strain K12) |
P0A6P9 | ENO_ECOLI | MSKIVKIIGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALELRDGDKSRFLGKGVTKAVAAVNGPIAQALIGKDAKDQAGIDKIMIDLDGTENKSKFGANAILAVSLANAKAAAAAKGMPLYEHIAELNGTPGKYSMPVPMMNIINGGEHADNNVDIQEFMIQPVGAKTVKEAIRMGSEVFHHLAKVLKAKGMNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITLAMDCAASEFYKDGKYVLAGEGNKAFTSEEFTHFLEELTKQYPIVSIEDGLDESDWDGFAYQTKVLGDKIQLVGDDLF... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:11676541, ECO:0000269|PubMed:16516921, ECO:0000269|PubMed:20823555, ECO:0000269|PubMed:4942326}; Note=Mg(2+) is required for catalysis and for stabilizing the dimer (PubMed:4942326). A second Mg(2+) binds during... | glycolytic process [GO:0006096]; RNA catabolic process [GO:0006401]; RNA processing [GO:0006396] | bacterial degradosome [GO:1990061]; cell surface [GO:0009986]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular region [GO:0005576]; membrane [GO:0016020]; phosphopyruvate hydratase complex [GO:0000015] | identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; protein homodimerization activity [GO:0042803] | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | PTM: Phosphorylated on serine residue(s) (PubMed:2513001). Seven-fold more phosphate is incorporated in glucose grown cells as compared to acetate grown cells; less labeling is seen in stationary phase (PubMed:2513001). Another paper suggests this phosphorylation is actually due to poor resolution of substrate-bound en... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000305|PubMed:4942326}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17242352, ECO:0000269|PubMed:18337249}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15003462}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of en... | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:2513001, ECO:0000269|PubMed:30714720, ECO:0000269|PubMed:4942326}; PhysiologicalDire... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for 2-phosphoglycerate {ECO:0000269|PubMed:4942326}; | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.1. {ECO:0000269|PubMed:4942326}; | null | FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP) (PubMed:2513001, PubMed:4942326). It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:2513001, ECO:0000269|PubMed:4942326}.; FUNCTION: Part of t... | Escherichia coli (strain K12) |
P0A6Q3 | FABA_ECOLI | MVDKRESYTKEDLLASGRGELFGAKGPQLPAPNMLMMDRVVKMTETGGNFDKGYVEAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGFYLGWLGGEGKGRALGVGEVKFTGQVLPTAKKVTYRIHFKRIVNRRLIMGLADGEVLVDGRLIYTASDLKVGLFQDTSAF | 4.2.1.59; 5.3.3.14 | null | fatty acid biosynthetic process [GO:0006633] | cytosol [GO:0005829] | (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydratase activity [GO:0047450]; (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity [GO:0008693]; (3R)-3-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity [GO:0008659]; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity [GO:0047451... | PF07977; | 3.10.129.10; | Thioester dehydratase family, FabA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8910376}; CATALYTI... | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. | null | null | FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids (PubMed:8910376). Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to (2E)-decenoyl-ACP and then its isomerization to (3Z)-decenoyl-ACP (PubMed:8910376). Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated ch... | Escherichia coli (strain K12) |
P0A6Q6 | FABZ_ECOLI | MTTNTHTLQIEEILELLPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEPGELYYFAGIDEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCARSREA | 4.2.1.59 | null | fatty acid biosynthetic process [GO:0006633]; lipid A biosynthetic process [GO:0009245] | cytoplasm [GO:0005737] | (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydratase activity [GO:0047450]; (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity [GO:0008693]; (3R)-3-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity [GO:0008659]; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity [GO:0047451... | PF07977; | 3.10.129.10; | Thioester dehydratase family, FabZ subfamily | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7806516, ECO:0000269|PubMed:8910376}; Physiolo... | null | null | null | null | FUNCTION: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7806516, ECO:0000269|PubMed:8910376}. | Escherichia coli (strain K12) |
P0A6R0 | FABH_ECOLI | MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAGAAVLAASEEPGIISTHLHADGSYGELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVRF | 2.3.1.180 | null | fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631] | cytosol [GO:0005829] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; beta-ketoacyl-acyl-carrier-protein synthase III activity [GO:0033818] | PF08545;PF08541; | 3.40.47.10; | Thiolase-like superfamily, FabH family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Ru... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for acetyl-CoA {ECO:0000269|PubMed:8631920}; KM=5 uM for malonyl-[ACP] {ECO:0000269|PubMed:8631920}; | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01815}. | null | null | FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... | Escherichia coli (strain K12) |
P0A6R3 | FIS_ECOLI | MFEQRVNSDVLTVSTVNSQDQVTQKPLRDSVKQALKNYFAQLNGQDVNDLYELVLAEVEQPLLDMVMQYTRGNQTRAALMMGINRGTLRKKLKKYGMN | null | null | chromosome organization [GO:0051276]; DNA-templated transcription [GO:0006351]; positive regulation of DNA recombination [GO:0045911]; provirus excision [GO:0032359]; regulation of DNA-templated transcription [GO:0006355]; response to radiation [GO:0009314] | cytosol [GO:0005829]; invertasome [GO:0031421]; nucleoid [GO:0009295]; nucleosome [GO:0000786]; protein-DNA complex [GO:0032993] | core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription repressor activity [GO:0001217]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA bind... | PF02954; | 1.10.10.60; | Transcriptional regulatory Fis 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: Activates ribosomal RNA transcription, as well other genes. Plays a direct role in upstream activation of rRNA promoters. Binds to a recombinational enhancer sequence that is required to stimulate hin-mediated DNA inversion. Prevents initiation of DNA replication from oriC. Binds to hundreds of transcriptiona... | Escherichia coli (strain K12) |
P0A6S5 | FTSB_ECOLI | MGKLTLLLLAILVWLQYSLWFGKNGIHDYTRVNDDVAAQQATNAKLKARNDQLFAEIDDLNGGQEALEERARNELSMTRPGETFYRLVPDASKRAQSAGQNNR | null | null | cell division [GO:0051301]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093] | cell division site [GO:0032153]; cell septum [GO:0030428]; divisome complex [GO:1990586]; FtsBL complex [GO:1990588]; FtsQBL complex [GO:1990587]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802] | PF04977; | 1.20.5.400; | FtsB family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00599, ECO:0000269|PubMed:11972052, ECO:0000269|PubMed:15165235}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_00599, ECO:0000269|PubMed:11972052, ECO:0000269|PubMed:15165235}. Note=Localizes to the division septum. Localization req... | null | null | null | null | null | FUNCTION: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. {ECO:0000255|HAMAP-Rule:MF_00599, ECO:0000269|PubMed:11972052, ECO:0000269|PubMed:19233928}. | Escherichia coli (strain K12) |
P0A6S7 | GPDA_ECOLI | MNQRNASMTVIGAGSYGTALAITLARNGHEVVLWGHDPEHIATLERDRCNAAFLPDVPFPDTLHLESDLATALAASRNILVVVPSHVFGEVLRQIKPLMRPDARLVWATKGLEAETGRLLQDVAREALGDQIPLAVISGPTFAKELAAGLPTAISLASTDQTFADDLQQLLHCGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPATFMGMAGLGDLVLTCTDNQSRNRRFGMMLGQGMDVQSAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNA... | 1.1.1.94 | null | carbohydrate metabolic process [GO:0005975]; glycerol-3-phosphate biosynthetic process [GO:0046167]; glycerol-3-phosphate catabolic process [GO:0046168]; glycerol-3-phosphate metabolic process [GO:0006072]; glycerophospholipid biosynthetic process [GO:0046474]; NADH oxidation [GO:0006116] | cytosol [GO:0005829]; glycerol-3-phosphate dehydrogenase complex [GO:0009331] | glycerol-3-phosphate dehydrogenase [NAD(P)+] activity [GO:0047952]; NAD binding [GO:0051287]; protein homodimerization activity [GO:0042803] | PF07479;PF01210; | 3.40.50.720; | NAD-dependent glycerol-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394}. | CATALYTIC ACTIVITY: Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945; EC=1.1.1.94; Evidence={ECO:0000255|HAMAP-Rule:MF_00394, ECO:0000269|PubMed:28326}; PhysiologicalD... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 uM for NADPH {ECO:0000269|PubMed:28326}; KM=180 uM for dihydroxyacetone phosphate {ECO:0000269|PubMed:28326}; KM=165 uM for NADP(+) {ECO:0000269|PubMed:28326}; KM=30 uM for sn-glycerol 3-phosphate {ECO:0000269|PubMed:28326}; Vmax=78 umol/min/mg enzyme for the N... | PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000255|HAMAP-Rule:MF_00394}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.4. At pH 6.0 and pH 8.6, the observed maximum velocities are half the optimum velocities. {ECO:0000269|PubMed:28326}; | null | FUNCTION: Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis (PubMed:28326, PubMed:355254, PubMed:4597451). Is able to use both NADPH and NADH with similar efficiency. Can also catalyze the reverse react... | Escherichia coli (strain K12) |
P0A6T1 | G6PI_ECOLI | MKNINPTQTAAWQALQKHFDEMKDVTIADLFAKDGDRFSKFSATFDDQMLVDYSKNRITEETLAKLQDLAKECDLAGAIKSMFSGEKINRTENRAVLHVALRNRSNTPILVDGKDVMPEVNAVLEKMKTFSEAIISGEWKGYTGKAITDVVNIGIGGSDLGPYMVTEALRPYKNHLNMHFVSNVDGTHIAEVLKKVNPETTLFLVASKTFTTQETMTNAHSARDWFLKAAGDEKHVAKHFAALSTNAKAVGEFGIDTANMFEFWDWVGGRYSLWSAIGLSIVLSIGFDNFVELLSGAHAMDKHFSTTPAEKNLPVLLALI... | 5.3.1.9 | null | cellular response to oxidative stress [GO:0034599]; gluconeogenesis [GO:0006094]; glucose 6-phosphate metabolic process [GO:0051156]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | carbohydrate derivative binding [GO:0097367]; glucose-6-phosphate isomerase activity [GO:0004347]; identical protein binding [GO:0042802]; monosaccharide binding [GO:0048029]; protein homodimerization activity [GO:0042803] | PF00342; | 1.10.1390.10; | GPI family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473, ECO:0000269|PubMed:4344919}. | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225; EC=5.3.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00473}; | null | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|HAMAP-Rule:MF_00473}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00473}. | null | null | FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}. | Escherichia coli (strain K12) |
P0A6T3 | GAL1_ECOLI | MSLKEKTQSLFANAFGYPATHTIQAPGRVNLIGEHTDYNDGFVLPCAIDYQTVISCAPRDDRKVRVMAADYENQLDEFSLDAPIVAHENYQWANYVRGVVKHLQLRNNSFGGVDMVISGNVPQGAGLSSSASLEVAVGTVLQQLYHLPLDGAQIALNGQEAENQFVGCNCGIMDQLISALGKKDHALLIDCRSLGTKAVSMPKGVAVVIINSNFKRTLVGSEYNTRREQCETGARFFQQPALRDVTIEEFNAVAHELDPIVAKRVRHILTENARTVEAASALEQGDLKRMGELMAESHASMRDDFEITVPQIDTLVEIVK... | 2.7.1.6 | null | galactose catabolic process via UDP-galactose [GO:0033499]; galactose metabolic process [GO:0006012] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; galactokinase activity [GO:0004335]; L-arabinokinase activity [GO:0009702]; magnesium ion binding [GO:0000287] | PF10509;PF08544;PF00288; | 3.30.230.10;3.30.70.890; | GHMP kinase family, GalK subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00246}. | CATALYTIC ACTIVITY: Reaction=alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+); Xref=Rhea:RHEA:13553, ChEBI:CHEBI:15378, ChEBI:CHEBI:28061, ChEBI:CHEBI:30616, ChEBI:CHEBI:58336, ChEBI:CHEBI:456216; EC=2.7.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00246, ECO:0000269|PubMed:12816414, ECO:0000269|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.1 mM for D-galactose {ECO:0000269|PubMed:12816414, ECO:0000269|PubMed:14612558}; KM=3.6 mM for 2-deoxy-D-galactose {ECO:0000269|PubMed:12816414, ECO:0000269|PubMed:14612558}; KM=2.9 mM for D-galactosamine {ECO:0000269|PubMed:12816414, ECO:0000269|PubMed:14612558}... | PATHWAY: Carbohydrate metabolism; galactose metabolism. {ECO:0000255|HAMAP-Rule:MF_00246}. | null | null | FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). To a lesser extent, is also able to phosphorylate 2-deoxy-D-galactose and D-galactosamine. Is not able to use D-galacturonic acid, D-talose, L-altrose, and L-glucose as substrates. {ECO:0000255... | Escherichia coli (strain K12) |
P0A6T5 | GCH1_ECOLI | MPSLSKEAALVHEALVARGLETPLRPPVHEMDNETRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYVDEIFSGLDYANFPKITLIENKMKVDEMVTVRDITLTSTCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLGGLFKSSQNTRHEFLRAVRHHN | 3.5.4.16 | null | one-carbon metabolic process [GO:0006730]; queuosine biosynthetic process [GO:0008616]; tetrahydrobiopterin biosynthetic process [GO:0006729]; tetrahydrofolate biosynthetic process [GO:0046654] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; protein-containing complex [GO:0032991] | GTP binding [GO:0005525]; GTP cyclohydrolase I activity [GO:0003934]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270] | PF01227; | 1.10.286.10;3.30.1130.10; | GTP cyclohydrolase I family | null | null | CATALYTIC ACTIVITY: Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16; | null | PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. | null | null | null | Escherichia coli (strain K12) |
P0A6U3 | MNMG_ECOLI | MFYPDPFDVIIIGGGHAGTEAAMAAARMGQQTLLLTHNIDTLGQMSCNPAIGGIGKGHLVKEVDALGGLMAKAIDQAGIQFRILNASKGPAVRATRAQADRVLYRQAVRTALENQPNLMIFQQAVEDLIVENDRVVGAVTQMGLKFRAKAVVLTVGTFLDGKIHIGLDNYSGGRAGDPPSIPLSRRLRELPLRVGRLKTGTPPRIDARTIDFSVLAQQHGDNPMPVFSFMGNASQHPQQVPCYITHTNEKTHDVIRSNLDRSPMYAGVIEGVGPRYCPSIEDKVMRFADRNQHQIFLEPEGLTSNEIYPNGISTSLPFDV... | null | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:17062623}; | regulation of cytoplasmic translational fidelity [GO:0140018]; response to UV [GO:0009411]; tRNA methylation [GO:0030488]; tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation [GO:0002926]; tRNA wobble uridine modification [GO:0002098] | cytosol [GO:0005829]; cytosolic tRNA wobble base thiouridylase complex [GO:0002144] | flavin adenine dinucleotide binding [GO:0050660]; protein homodimerization activity [GO:0042803] | PF01134;PF13932;PF21680; | 3.50.50.60;1.10.150.570;1.10.10.1800; | MnmG family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17062623}. | null | null | null | null | null | FUNCTION: NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000269|PubMed:11544186, ECO:0000269|PubMed:17062623, ECO:0000269|PubMed:9603884}. | Escherichia coli (strain K12) |
P0A6U5 | RSMG_ECOLI | MLNKLSLLLKDAGISLTDHQKNQLIAYVNMLHKWNKAYNLTSVRDPNEMLVRHILDSIVVAPYLQGERFIDVGTGPGLPGIPLSIVRPEAHFTLLDSLGKRVRFLRQVQHELKLENIEPVQSRVEEFPSEPPFDGVISRAFASLNDMVSWCHHLPGEQGRFYALKGQMPEDEIALLPEEYQVESVVKLQVPALDGERHLVVIKANKI | 2.1.1.170 | null | rRNA base methylation [GO:0070475] | cytosol [GO:0005829] | rRNA (guanine-N7-)-methyltransferase activity [GO:0070043] | PF02527; | 3.40.50.150; | Methyltransferase superfamily, RNA methyltransferase RsmG family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00074}. | CATALYTIC ACTIVITY: Reaction=guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42732, Rhea:RHEA-COMP:10209, Rhea:RHEA-COMP:10210, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74480; EC=2.1.1.170; Evidence={ECO... | null | null | null | null | FUNCTION: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. Requires the intact 30S subunit for methylation. {ECO:0000255|HAMAP-Rule:MF_00074, ECO:0000269|PubMed:17238915}. | Escherichia coli (strain K12) |
P0A6V1 | GLGC_ECOLI | MVSLEKNDHLMLARQLPLKSVALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEEMNEFVDLLPAQQRMKGENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPIEEASAFGVMAVDENDKIIEFVEKPANPPSMPNDPSKSLASMGIYVFDADYLYELLEEDDRDENSSHDFGKDLIPKITEAGLAYAHPFPLSCVQSDPDAEPYWRDVGTLEAYWKANLDLASVVPELDMYDRNWPIRTYNESLPPAKFVQ... | 2.7.7.27 | null | glycogen biosynthetic process [GO:0005978]; protein homotetramerization [GO:0051289] | glucose-1-phosphate adenylyltransferase complex [GO:0010170] | AMP binding [GO:0016208]; ATP binding [GO:0005524]; glucose-1-phosphate adenylyltransferase activity [GO:0008878]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287] | PF00483; | 2.160.10.10; | Bacterial/plant glucose-1-phosphate adenylyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498, ChEBI:CHEBI:58601; EC=2.7.7.27; Evidence={ECO:0000269|PubMed:1648099}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for alpha-D-glucose 1-phosphate {ECO:0000269|PubMed:1648099}; KM=120 uM for diphosphate {ECO:0000269|PubMed:1648099}; Vmax=133 umol/min/mg enzyme toward alpha-D-glucose 1-phosphate {ECO:0000269|PubMed:1648099}; Vmax=97 umol/min/mg enzyme toward diphosphate {E... | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc. {ECO:0000269|PubMed:1648099}. | Escherichia coli (strain K12) |
P0A6W3 | MRAY_ECOLI | MLVWLAEHLVKYYSGFNVFSYLTFRAIVSLLTALFISLWMGPRMIAHLQKLSFGQVVRNDGPESHFSKRGTPTMGGIMILTAIVISVLLWAYPSNPYVWCVLVVLVGYGVIGFVDDYRKVVRKDTKGLIARWKYFWMSVIALGVAFALYLAGKDTPATQLVVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAGGFALVAWATGNMNFASYLHIPYLRHAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQEFLLVIMGGVFVVETLSVILQVGSFKLRGQRIFR... | 2.7.8.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000269|PubMed:215212}; Note=Replacement of Mg(2+) by Mn(2+) restores only 10% of the activity. {ECO:0000269|PubMed:215212}; | cell cycle [GO:0007049]; cell division [GO:0051301]; cell wall macromolecule biosynthetic process [GO:0044038]; cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | membrane [GO:0016020]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; phospho-N-acetylmuramoyl-pentapeptide-transferase activity [GO:0008963]; UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity [GO:0051992] | PF00953;PF10555; | null | Glycosyltransferase 4 family, MraY subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000269|PubMed:15919996}. | CATALYTIC ACTIVITY: Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP; Xref=Rhe... | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000305|PubMed:215212}. | null | null | FUNCTION: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known ... | Escherichia coli (strain K12) |
P0A6X1 | HEM1_ECOLI | MTLLALGINHKTAPVSLRERVSFSPDKLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLNEEDLRKSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHMKASELERMFQKSFSVAKRVRTETDIGASAVSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQILADEVGAEVIALSDIDERLREADIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRKAAAVE... | 1.2.1.70 | null | protoporphyrinogen IX biosynthetic process from glutamate [GO:0019353] | null | glutamyl-tRNA reductase activity [GO:0008883]; identical protein binding [GO:0042802]; NADP binding [GO:0050661] | PF00745;PF05201;PF01488; | 3.30.460.30;3.40.50.720; | Glutamyl-tRNA reductase family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH; Xref=Rhea:RHEA:12344, Rhea:RHEA-COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57501, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520; EC=1.2.1.70; Evidence={E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=24 uM for L-glutamyl-tRNA(Glu) {ECO:0000269|PubMed:12370189}; KM=39 uM for NADPH {ECO:0000269|PubMed:12370189}; | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. | null | null | FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA. {ECO:0000269|PubMed:12370189, ECO:0000269|PubMed:1569081}. | Escherichia coli (strain K12) |
P0A6X3 | HFQ_ECOLI | MAKGQSLQDPFLNALRRERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVSHHSNNAGGGTSSNYHHGSSAQNTSAQQDSEETE | null | null | positive regulation of translation, ncRNA-mediated [GO:0045975]; regulation of DNA-templated transcription [GO:0006355]; regulation of RNA stability [GO:0043487]; regulation of translation, ncRNA-mediated [GO:0045974]; sRNA-mediated post-transcriptional gene silencing [GO:0040033] | cytosol [GO:0005829] | bent DNA binding [GO:0003681]; DNA binding [GO:0003677]; RNA binding [GO:0003723]; RNA folding chaperone [GO:0140691] | PF17209; | 2.30.30.100; | Hfq family | null | null | null | null | null | null | null | FUNCTION: RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Involved in the regulation of stress responses mediated by the sigma factors RpoS, sigma-E and sigma-32 (Pu... | Escherichia coli (strain K12) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.