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| | acnB | Aconitate hydrase B; Residues 1 to 865 of 865 are 99.88 pct identical to residues 1 to 865 of 865 from Escherichia coli K-12 Strain MG1655: B0118; Belongs to the aconitase/IPM isomerase family. (865 aa) |
| | yafV | Putative EC 3.5. amidase-type enzyme; Residues 1 to 255 of 256 are 98.82 pct identical to residues 1 to 255 of 256 from Escherichia coli K-12 Strain MG1655: B0219. (256 aa) |
| | cyoE | Protoheme IX farnesyltransferase (haeme O biosynthesis); Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (296 aa) |
| | cyoD | Cytochrome o ubiquinol oxidase subunit IV; Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity). (109 aa) |
| | cyoC | Cytochrome o ubiquinol oxidase subunit III; Residues 1 to 204 of 204 are 99.50 pct identical to residues 1 to 204 of 204 from Escherichia coli K-12 Strain MG1655: B0430. (204 aa) |
| | cyoB | Cytochrome o ubiquinol oxidase subunit I; Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity). (663 aa) |
| | cyoA | Cytochrome o ubiquinol oxidase subunit II; Residues 1 to 315 of 315 are 99.04 pct identical to residues 1 to 315 of 315 from Escherichia coli K-12 Strain MG1655: B0432. (315 aa) |
| | gltA | Citrate synthase; Residues 1 to 426 of 427 are 99.76 pct identical to residues 1 to 426 of 427 from Escherichia coli K-12 Strain MG1655: B0720; Belongs to the citrate synthase family. (427 aa) |
| | sdhC | Succinate dehydrogenase, cytochrome b556; Membrane-anchoring subunit of succinate dehydrogenase (SDH). Belongs to the cytochrome b560 family. (129 aa) |
| | sdhD | Succinate dehydrogenase, hydrophobic subunit; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (115 aa) |
| | sdhA | Succinate dehydrogenase, flavoprotein subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (588 aa) |
| | sdhB | Succinate dehydrogenase, iron sulfur protein; Residues 1 to 238 of 238 are 99.57 pct identical to residues 1 to 238 of 238 from Escherichia coli K-12 Strain MG1655: B0724; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (238 aa) |
| | sucA | 2-oxoglutarate dehydrogenase (decarboxylase component); E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). (933 aa) |
| | sucB | 2-oxoglutarate dehydrogenase (dihydrolipoyltranssuccinase E2 component); E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). (405 aa) |
| | sucC | succinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (388 aa) |
| | sucD | succinyl-CoA synthetase, alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. (289 aa) |
| | fumA-2 | Putative fumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (550 aa) |
| | cydA | Cytochrome d terminal oxidase, polypeptide subunit I; Residues 1 to 523 of 523 are 100.00 pct identical to residues 1 to 523 of 523 from Escherichia coli K-12 Strain MG1655: B0733. (523 aa) |
| | cydB | Cytochrome d terminal oxidase polypeptide subunit II; A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. (379 aa) |
| | ybhJ | Putative enzyme; Residues 1 to 761 of 761 are 99.21 pct identical to residues 1 to 761 of 761 from Escherichia coli K-12 Strain MG1655: B0771. (761 aa) |
| | cydC | ATP-binding component of cytochrome-related transport; Residues 1 to 573 of 573 are 98.95 pct identical to residues 1 to 573 of 573 from Escherichia coli K-12 Strain MG1655: B0886. (573 aa) |
| | cydD | ATP-binding component of cytochrome-related transport, Zn sensitive; Residues 1 to 588 of 588 are 99.31 pct identical to residues 1 to 588 of 588 from Escherichia coli K-12 Strain MG1655: B0887. (588 aa) |
| | appC | Probable third cytochrome oxidase, subunit I; Residues 1 to 514 of 514 are 99.22 pct identical to residues 1 to 514 of 514 from Escherichia coli K-12 Strain MG1655: B0978. (514 aa) |
| | appB | Probable third cytochrome oxidase, subunit II; Residues 1 to 378 of 378 are 99.47 pct identical to residues 1 to 378 of 378 from Escherichia coli K-12 Strain MG1655: B0979. (378 aa) |
| | icdA | Isocitrate dehydrogenase, specific for NADP+; Residues 1 to 416 of 416 are 99.27 pct identical to residues 1 to 416 of 416 from Escherichia coli K-12 Strain MG1655: B1136. (416 aa) |
| | sfcA | NAD-linked malate dehydrogenase (malic enzyme); Residues 1 to 574 of 574 are 99.47 pct identical to residues 1 to 574 of 574 from Escherichia coli K-12 Strain MG1655: B1479; Belongs to the malic enzymes family. (574 aa) |
| | ydbK | Putative oxidoreductase, Fe-S subunit; Residues 1 to 1174 of 1174 are 99.57 pct identical to residues 1 to 1174 of 1174 from Escherichia coli K-12 Strain MG1655: B1378. (1174 aa) |
| | acnA | Aconitate hydrase 1; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (891 aa) |
| | fumC | Fumarase C= fumarate hydratase Class II; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (467 aa) |
| | fumA | Fumarase A = fumarate hydratase Class I; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate. (548 aa) |
| | fumD | Orf, hypothetical protein; In vitro catalyzes the addition of water to fumarate, forming malate. Cannot catalyze the reverse reaction. Cannot use the cis-isomer maleate as substrate; Belongs to the FumD family. (69 aa) |
| | yojH | Orf, hypothetical protein; Residues 1 to 548 of 548 are 99.63 pct identical to residues 1 to 548 of 548 from Escherichia coli K-12 Strain MG1655: B2210. (548 aa) |
| | nuoN | NADH dehydrogenase I chain N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. (425 aa) |
| | nuoM | NADH dehydrogenase I chain M; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity); Belongs to the complex I subunit 4 family. (509 aa) |
| | nuoL | NADH dehydrogenase I chain L; Residues 1 to 613 of 613 are 99.83 pct identical to residues 1 to 613 of 613 from Escherichia coli K-12 Strain MG1655: B2278. (613 aa) |
| | nuoK | NADH dehydrogenase I chain K; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family. (100 aa) |
| | nuoJ | NADH dehydrogenase I chain J; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity); Belongs to the complex I subunit 6 family. (184 aa) |
| | nuoI | NADH dehydrogenase I chain I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (180 aa) |
| | nuoH | NADH dehydrogenase I chain H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. (325 aa) |
| | nuoG | NADH dehydrogenase I chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). (910 aa) |
| | nuoF | NADH dehydrogenase I chain F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (445 aa) |
| | nuoE | NADH dehydrogenase I chain E; Residues 1 to 166 of 166 are 99.39 pct identical to residues 1 to 166 of 166 from Escherichia coli K-12 Strain MG1655: B2285. (166 aa) |
| | nuoC | NADH dehydrogenase I chain C, D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (600 aa) |
| | nuoB | NADH dehydrogenase I chain B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (220 aa) |
| | nuoA | NADH dehydrogenase I chain A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. (147 aa) |
| | alaA | Putative aminotransferase; Residues 1 to 405 of 405 are 99.75 pct identical to residues 1 to 405 of 405 from Escherichia coli K-12 Strain MG1655: B2290. (405 aa) |
| | maeB | Putative multimodular enzyme; Residues 1 to 759 of 759 are 99.86 pct identical to residues 1 to 759 of 759 from Escherichia coli K-12 Strain MG1655: B2463. (759 aa) |
| | yfhL | Orf, hypothetical protein; Residues 1 to 86 of 86 are 98.83 pct identical to residues 1 to 86 of 86 from Escherichia coli K-12 Strain MG1655: B2562. (86 aa) |
| | yggD | Putative transcriptional regulator; Residues 1 to 169 of 169 are 94.67 pct identical to residues 1 to 169 of 169 from Escherichia coli K-12 Strain MG1655: B2929. (169 aa) |
| | ygiP | Putative transcriptional regulator LYSR-type; Positive regulator required for L-tartrate-dependent anaerobic growth on glycerol. Induces expression of the ttdA-ttdB-ygjE operon (By similarity). (310 aa) |
| | ttdA | L-tartrate dehydratase, subunit A; Residues 1 to 303 of 303 are 99.00 pct identical to residues 1 to 303 of 303 from Escherichia coli K-12 Strain MG1655: B3061; Belongs to the class-I fumarase family. (303 aa) |
| | ttdB | L-tartrate dehydratase, subunit B; Residues 1 to 201 of 201 are 99.00 pct identical to residues 1 to 201 of 201 from Escherichia coli K-12 Strain MG1655: B3062. (201 aa) |
| | ygjE | Orf, hypothetical protein; Catalyzes the uptake of tartrate in exchange for intracellular succinate. Essential for anaerobic L-tartrate fermentation (By similarity). (487 aa) |
| | mdh | Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa) |
| | avtA | Alanine-alpha-ketoisovalerate (or valine-pyruvate) transaminase, transaminase C; Residues 1 to 417 of 417 are 99.04 pct identical to residues 1 to 417 of 417 from Escherichia coli K-12 Strain MG1655: B3572. (417 aa) |
| | atpC | Membrane-bound ATP synthase, F1 sector, epsilon-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (139 aa) |
| | atpD | Membrane-bound ATP synthase, F1 sector, beta-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. (460 aa) |
| | atpG | Membrane-bound ATP synthase, F1 sector, gamma-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex (By similarity). (287 aa) |
| | atpA | Membrane-bound ATP synthase, F1 sector, alpha-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family. (513 aa) |
| | atpH | Membrane-bound ATP synthase, F1 sector, delta-subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. (177 aa) |
| | atpF | Membrane-bound ATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (156 aa) |
| | atpE | Membrane-bound ATP synthase, F0 sector, subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (79 aa) |
| | atpB | Membrane-bound ATP synthase, F0 sector, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (271 aa) |
| | aceK | Isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. (578 aa) |
| | fumB | Fumarase B= fumarate hydratase Class I; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (548 aa) |
| | frdD | Fumarate reductase, anaerobic, membrane anchor polypeptide; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. (119 aa) |
| | frdC | Fumarate reductase, anaerobic, membrane anchor polypeptide; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. (131 aa) |
| | frdB | Fumarate reductase, anaerobic, iron-sulfur protein subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (244 aa) |
| | frdA | Fumarate reductase, anaerobic, flavoprotein subunit; Residues 1 to 602 of 602 are 99.83 pct identical to residues 1 to 602 of 602 from Escherichia coli K-12 Strain MG1655: B4154. (602 aa) |
| | ppa | Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (176 aa) |
