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| | nuoD1 | NADH dehydrogenase I, D subunit; 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 a menaquinone. 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 49 kDa subunit family. (441 aa) |
| | Sare_0003 | TIGRFAM: 6-phosphogluconate dehydrogenase, decarboxylating; PFAM: 6-phosphogluconate dehydrogenase domain protein; 6-phosphogluconate dehydrogenase NAD-binding; KEGG: stp:Strop_0004 6-phosphogluconate dehydrogenase, decarboxylating. (290 aa) |
| | Sare_0107 | PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: stp:Strop_0107 catalytic domain of components of various dehydrogenase complexes. (490 aa) |
| | Sare_0135 | Fructose-bisphosphate aldolase, class II; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis; Belongs to the class II fructose-bisphosphate aldolase family. (340 aa) |
| | Sare_0188 | PFAM: Vitamin K epoxide reductase; KEGG: stp:Strop_0174 vitamin K epoxide reductase. (211 aa) |
| | Sare_0316 | PFAM: FAD linked oxidase domain protein; KEGG: stp:Strop_0273 FAD linked oxidase domain protein. (464 aa) |
| | Sare_0377 | PFAM: protein of unknown function DUF849; KEGG: stp:Strop_0314 protein of unknown function DUF849. (280 aa) |
| | gpmA | Phosphoglycerate mutase 1 family; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. (255 aa) |
| | nuoB1 | NADH-quinone oxidoreductase, B subunit; 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 a menaquinone. 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. (188 aa) |
| | Sare_0463 | NADH dehydrogenase (ubiquinone) 30 kDa subunit; 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 30 kDa subunit family. (235 aa) |
| | nuoH | NADH dehydrogenase (quinone); 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. (320 aa) |
| | nuoI | 4Fe-4S ferredoxin iron-sulfur binding domain protein; 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. (216 aa) |
| | Sare_0469 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. (200 aa) |
| | nuoK | NADH-ubiquinone oxidoreductase chain 4L; 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 a menaquinone. 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. (118 aa) |
| | Sare_0471 | KEGG: stp:Strop_0403 proton-translocating NADH-quinone oxidoreductase, chain L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (646 aa) |
| | Sare_0472 | KEGG: stp:Strop_0404 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (503 aa) |
| | nuoN | NADH dehydrogenase (quinone); 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 a menaquinone. 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. (514 aa) |
| | Sare_0511 | PFAM: Citrate synthase; KEGG: stp:Strop_0423 citrate (Si)-synthase; Belongs to the citrate synthase family. (368 aa) |
| | Sare_0556 | KEGG: stp:Strop_2698 hypothetical protein. (345 aa) |
| | Sare_0645 | PFAM: thiamine pyrophosphate protein domain protein TPP-binding; KEGG: stp:Strop_0698 thiamine pyrophosphate enzyme domain protein TPP-binding. (344 aa) |
| | Sare_0646 | PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; KEGG: stp:Strop_0699 pyruvate flavodoxin/ferredoxin oxidoreductase domain protein. (615 aa) |
| | Sare_0648 | NADH-ubiquinone/plastoquinone oxidoreductase chain 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (125 aa) |
| | Sare_0708 | NADH-ubiquinone/plastoquinone oxidoreductase chain 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (114 aa) |
| | Sare_0710 | PFAM: respiratory-chain NADH dehydrogenase subunit 1; KEGG: stp:Strop_0768 respiratory-chain NADH dehydrogenase, subunit 1. (309 aa) |
| | Sare_0711 | Conserved hypothetical protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. (187 aa) |
| | nuoK-2 | NADH-ubiquinone oxidoreductase chain 4L; 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 a menaquinone. 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) |
| | Sare_0713 | NADH dehydrogenase (quinone); PFAM: NADH/Ubiquinone/plastoquinone (complex I); KEGG: stp:Strop_0771 NADH dehydrogenase (quinone). (621 aa) |
| | Sare_0714 | KEGG: stp:Strop_0772 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (496 aa) |
| | nuoN-2 | NADH dehydrogenase (quinone); 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 a menaquinone. 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. (462 aa) |
| | ppc | Phosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle; Belongs to the PEPCase type 1 family. (928 aa) |
| | eno | Phosphopyruvate hydratase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. (427 aa) |
| | Sare_0983 | Cytochrome c oxidase subunit I type; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (585 aa) |
| | Sare_1027 | PFAM: MmgE/PrpD family protein; KEGG: stp:Strop_4385 MmgE/PrpD family protein. (458 aa) |
| | Sare_1103 | PFAM: Electron transfer flavoprotein alpha/beta-subunit; KEGG: stp:Strop_1210 electron transfer flavoprotein beta-subunit. (259 aa) |
| | Sare_1104 | PFAM: Electron transfer flavoprotein alpha/beta-subunit; Electron transfer flavoprotein alpha subunit; KEGG: stp:Strop_1211 electron transfer flavoprotein, alpha subunit. (319 aa) |
| | Sare_1114 | Transketolase domain protein; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (785 aa) |
| | Sare_1132 | KEGG: stp:Strop_1242 hypothetical protein. (152 aa) |
| | Sare_1640 | PFAM: Rieske [2Fe-2S] domain protein; KEGG: stp:Strop_1655 Rieske (2Fe-2S) domain protein. (204 aa) |
| | Sare_1660 | PFAM: glucose-6-phosphate dehydrogenase; KEGG: stp:Strop_1668 glucose-6-phosphate dehydrogenase. (481 aa) |
| | Sare_1705 | TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: stp:Strop_1708 succinate dehydrogenase and fumarate reductase iron-sulfur protein. (251 aa) |
| | Sare_1706 | KEGG: stp:Strop_1709 succinate dehydrogenase or fumarate reductase, flavoprotein subunit; TIGRFAM: succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein. (643 aa) |
| | Sare_1734 | KEGG: stp:Strop_1749 hypothetical protein. (192 aa) |
| | Sare_1865 | PFAM: ribulose-phosphate 3-epimerase; KEGG: stp:Strop_1872 ribulose-phosphate 3-epimerase; Belongs to the ribulose-phosphate 3-epimerase family. (226 aa) |
| | Sare_2178 | KEGG: stp:Strop_2698 hypothetical protein. (320 aa) |
| | Sare_2219 | PFAM: ferredoxin; oxidoreductase FAD/NAD(P)-binding domain protein; Oxidoreductase FAD-binding domain protein; KEGG: stp:Strop_2076 oxidoreductase FAD-binding domain protein. (363 aa) |
| | Sare_2240 | PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: stp:Strop_2099 catalytic domain of components of various dehydrogenase complexes. (430 aa) |
| | Sare_2284 | KEGG: stp:Strop_2136 citrate synthase I; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; Belongs to the citrate synthase family. (427 aa) |
| | Sare_2295 | Cytochrome c oxidase subunit I type; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (666 aa) |
| | Sare_2330 | KEGG: cvi:CV_3273 VioB - polyketide synthase. (1069 aa) |
| | Sare_2357 | KEGG: stp:Strop_2240 hypothetical protein. (97 aa) |
| | Sare_2381 | Lysine 2,3-aminomutase; PFAM: Radical SAM domain protein; KEGG: stp:Strop_2262 radical SAM domain protein. (467 aa) |
| | Sare_2384 | PFAM: D-Lysine 56-aminomutase alpha subunit; KEGG: stp:Strop_2265 hypothetical protein. (520 aa) |
| | Sare_2481 | KEGG: stp:Strop_2338 cytochrome d ubiquinol oxidase, subunit II; TIGRFAM: cytochrome d ubiquinol oxidase, subunit II; PFAM: cytochrome bd ubiquinol oxidase subunit II. (332 aa) |
| | Sare_2482 | PFAM: cytochrome bd ubiquinol oxidase subunit I; KEGG: stp:Strop_2339 cytochrome bd ubiquinol oxidase, subunit I. (470 aa) |
| | Sare_2537 | KEGG: stp:Strop_1338 protein of unknown function DUF1271. (68 aa) |
| | Sare_2952 | PFAM: methylaspartate mutase E subunit; KEGG: hal:VNG2288G MamB. (471 aa) |
| | Sare_3163 | Ferredoxin; KEGG: sco:SCO7676 ferredoxin. (71 aa) |
| | Sare_3183 | PFAM: flavodoxin/nitric oxide synthase; KEGG: stp:Strop_1973 flavodoxin/nitric oxide synthase; Belongs to the WrbA family. (205 aa) |
| | Sare_3242 | KEGG: mjl:Mjls_3780 putative ferredoxin. (64 aa) |
| | Sare_3289 | TIGRFAM: aconitate hydratase 1; PFAM: aconitate hydratase domain protein; KEGG: stp:Strop_3062 aconitate hydratase 1. (948 aa) |
| | Sare_3316 | TIGRFAM: transketolase; PFAM: Transketolase domain protein; Transketolase central region; KEGG: stp:Strop_3089 transketolase; Belongs to the transketolase family. (712 aa) |
| | tal | Transaldolase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway; Belongs to the transaldolase family. Type 2 subfamily. (392 aa) |
| | Sare_3318 | PFAM: phosphoglucose isomerase (PGI); KEGG: stp:Strop_3091 phosphoglucose isomerase (PGI); Belongs to the GPI family. (559 aa) |
| | zwf | Glucose-6-phosphate 1-dehydrogenase; Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone. (505 aa) |
| | pgl | 6-phosphogluconolactonase; Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. (256 aa) |
| | tpiA | Triose-phosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (263 aa) |
| | pgk | PFAM: phosphoglycerate kinase; KEGG: stp:Strop_3097 phosphoglycerate kinase; Belongs to the phosphoglycerate kinase family. (399 aa) |
| | Sare_3325 | KEGG: stp:Strop_3098 glyceraldehyde-3-phosphate dehydrogenase, type I; TIGRFAM: glyceraldehyde-3-phosphate dehydrogenase, type I; PFAM: glyceraldehyde 3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. (334 aa) |
| | Sare_3385 | KEGG: stp:Strop_3160 pyruvate kinase; TIGRFAM: pyruvate kinase; PFAM: Pyruvate kinase barrel; Pyruvate kinase alpha/beta; Belongs to the pyruvate kinase family. (482 aa) |
| | Sare_3408 | KEGG: stp:Strop_3182 hypothetical protein. (209 aa) |
| | Sare_3455 | PFAM: NADH/Ubiquinone/plastoquinone (complex I); KEGG: stp:Strop_3229 NADH/ubiquinone/plastoquinone (complex I). (488 aa) |
| | pfp | Diphosphate--fructose-6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. (342 aa) |
| | Sare_3524 | PFAM: Cytochrome b/b6 domain; KEGG: stp:Strop_3292 cytochrome b/b6, N-terminal domain. (536 aa) |
| | Sare_3525 | PFAM: Rieske [2Fe-2S] domain protein; KEGG: stp:Strop_3293 Rieske (2Fe-2S) domain protein. (361 aa) |
| | Sare_3526 | PFAM: cytochrome c class I; KEGG: stp:Strop_3294 cytochrome c, class I. (277 aa) |
| | Sare_3527 | PFAM: cytochrome c oxidase subunit III; KEGG: stp:Strop_3295 cytochrome c oxidase, subunit III. (199 aa) |
| | Sare_3531 | Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. (141 aa) |
| | Sare_4958 | PFAM: MmgE/PrpD family protein; KEGG: stp:Strop_4443 MmgE/PrpD family protein. (464 aa) |
| | nuoD2 | NADH dehydrogenase (quinone); 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 a menaquinone. 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 49 kDa subunit family. (385 aa) |
| | fumC | Fumarate lyase; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (466 aa) |
| | nuoA | NADH-ubiquinone/plastoquinone oxidoreductase chain 3; 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 a menaquinone. 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. (121 aa) |
| | nuoB2 | NADH-quinone oxidoreductase, B subunit; 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 a menaquinone. 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. (226 aa) |
| | nuoC | NADH (or F420H2) dehydrogenase, subunit C; 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 a menaquinone. 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 30 kDa subunit family. (245 aa) |
| | Sare_4459 | TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; KEGG: stp:Strop_4061 NADH-quinone oxidoreductase, E subunit. (305 aa) |
| | Sare_4458 | NADH-quinone oxidoreductase, F subunit; 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. (443 aa) |
| | Sare_4457 | NADH-quinone oxidoreductase, chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family. (839 aa) |
| | nuoH-2 | NADH dehydrogenase (quinone); 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. (448 aa) |
| | nuoI-2 | NADH-quinone oxidoreductase, 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. (211 aa) |
| | Sare_4454 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. (256 aa) |
| | nuoK-3 | NADH-ubiquinone oxidoreductase chain 4L; 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 a menaquinone. 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. (105 aa) |
| | Sare_4452 | KEGG: stp:Strop_4054 proton-translocating NADH-quinone oxidoreductase, chain L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone oxidoreductase (complex I) chain 5/L domain protein; NADH/Ubiquinone/plastoquinone (complex I). (651 aa) |
| | Sare_4451 | KEGG: stp:Strop_4053 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (510 aa) |
| | nuoN-3 | Proton-translocating NADH-quinone oxidoreductase, 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 a menaquinone. 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. (517 aa) |
| | Sare_4259 | PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; BFD domain protein [2Fe-2S]-binding domain protein; KEGG: stp:Strop_3868 FAD-dependent pyridine nucleotide-disulphide oxidoreductase. (478 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. (392 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. (295 aa) |
| | Sare_4200 | KEGG: stp:Strop_3810 hypothetical protein. (422 aa) |
| | Sare_4174 | Lactate/malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. (316 aa) |
| | Sare_4173 | KEGG: stp:Strop_3793 isocitrate dehydrogenase, NADP-dependent; TIGRFAM: isocitrate dehydrogenase, NADP-dependent; PFAM: isocitrate/isopropylmalate dehydrogenase; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (404 aa) |
| | Sare_4159 | PFAM: protein of unknown function DUF405; protein of unknown function DUF418; KEGG: stp:Strop_3780 protein of unknown function DUF418. (401 aa) |
| | Sare_4151 | TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: ferredoxin; KEGG: stp:Strop_3769 succinate dehydrogenase and fumarate reductase iron-sulfur protein. (366 aa) |
| | Sare_4150 | PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; FAD dependent oxidoreductase; KEGG: stp:Strop_3768 succinate dehydrogenase. (637 aa) |
| | Sare_4141 | 4Fe-4S ferredoxin iron-sulfur binding domain protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (108 aa) |
| | Sare_4070 | TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase central region; KEGG: stp:Strop_3690 2-oxoglutarate dehydrogenase, E1 subunit. (1237 aa) |
| | Sare_3976 | KEGG: stp:Strop_3595 hypothetical protein. (353 aa) |
| | Sare_3964 | PFAM: metallophosphoesterase; KEGG: stp:Strop_3584 metallophosphoesterase. (258 aa) |
| | Sare_3893 | KEGG: stp:Strop_3518 hypothetical protein. (137 aa) |
| | Sare_3824 | 6-phosphogluconate dehydrogenase, decarboxylating; Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. (478 aa) |
| | Sare_3797 | KEGG: stp:Strop_3420 hypothetical protein. (140 aa) |
| | Sare_3613 | 2-oxo-acid dehydrogenase E1 subunit, homodimeric type; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (912 aa) |
| | Sare_3552 | 2-oxoglutarate dehydrogenase E2 component; KEGG: stp:Strop_3320 dihydrolipoyllysine-residue succinyltransferase; TIGRFAM: 2-oxoglutarate dehydrogenase E2 component; PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein. (590 aa) |
| | Sare_3532 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (323 aa) |
