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Ndas_3927 Ndas_3927 Ndas_0022 Ndas_0022 sucC sucC sucD sucD fumC fumC Ndas_0198 Ndas_0198 Ndas_0199 Ndas_0199 Ndas_0681 Ndas_0681 Ndas_0682 Ndas_0682 Ndas_0683 Ndas_0683 mdh mdh Ndas_0943 Ndas_0943 Ndas_0999 Ndas_0999 Ndas_1184 Ndas_1184 Ndas_1214 Ndas_1214 Ndas_1429 Ndas_1429 Ndas_1731 Ndas_1731 Ndas_1832 Ndas_1832 Ndas_1931 Ndas_1931 Ndas_2008 Ndas_2008 Ndas_2866 Ndas_2866 Ndas_3046 Ndas_3046 Ndas_3132 Ndas_3132 Ndas_3135 Ndas_3135 Ndas_3149 Ndas_3149 Ndas_3602 Ndas_3602 Ndas_3603 Ndas_3603 Ndas_3681 Ndas_3681 Ndas_3921 Ndas_3921 ppc ppc Ndas_3960 Ndas_3960 Ndas_4112 Ndas_4112 sucD-2 sucD-2 sucC-2 sucC-2 Ndas_4410 Ndas_4410 Ndas_4458 Ndas_4458 Ndas_4892 Ndas_4892 Ndas_4932 Ndas_4932 Ndas_5058 Ndas_5058 Ndas_5059 Ndas_5059 nuoH nuoH nuoI nuoI nuoK nuoK Ndas_5064 Ndas_5064 Ndas_5065 Ndas_5065 nuoN nuoN Ndas_5088 Ndas_5088 Ndas_5089 Ndas_5089 Ndas_5194 Ndas_5194
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Ndas_3927COGs: COG0479 Succinate dehydrogenase/fumarate reductase Fe-S protein subunit; InterProIPR001041:IPR006058:IPR012675:IPR012285:IPR 009051:IPR004489; KEGG: nfa:nfa56030 fumarate reductase iron-sulfur subunit; PFAM: ferredoxin; SPTR: C1YKS4 Succinate dehydrogenase subunit B; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: 2Fe-2S iron-sulfur cluster binding domain; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein. (263 aa)
Ndas_00224Fe-4S ferredoxin iron-sulfur binding domain protein; COGs: COG0437 Fe-S-cluster-containing hydrogenase components 1; InterPro IPR017900:IPR001450:IPR014603:IPR017896; KEGG: svi:Svir_19180 formate dehydrogenase beta subunit; PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; SPTR: C1YR75 Formate dehydrogenase beta subunit; PFAM: 4Fe-4S binding domain; TIGRFAM: formate dehydrogenase, beta subunit, Fe-S containing. (294 aa)
sucCsuccinyl-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. (393 aa)
sucDsuccinyl-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. (292 aa)
fumCFumarate 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. (462 aa)
Ndas_0198COGs: COG1294 Cytochrome bd-type quinol oxidase subunit 2; InterPro IPR003317; KEGG: tfu:Tfu_0637 cytochrome bd ubiquinol oxidase, subunit II; PFAM: cytochrome bd ubiquinol oxidase subunit II; SPTR: C1YHT0 Cytochrome d oxidase cyd, subunit II; TIGRFAM: cytochrome d ubiquinol oxidase, subunit II; PFAM: Cytochrome oxidase subunit II; TIGRFAM: cytochrome d oxidase, subunit II (cydB). (350 aa)
Ndas_0199COGs: COG1271 Cytochrome bd-type quinol oxidase subunit 1; InterPro IPR002585; KEGG: tfu:Tfu_0638 putative cytochrome oxidase subunit I; PFAM: cytochrome bd ubiquinol oxidase subunit I; SPTR: C1YHS9 Cytochrome bd-type quinol oxidase, subunit 1; PFAM: Bacterial Cytochrome Ubiquinol Oxidase. (481 aa)
Ndas_0681FAD linked oxidase domain protein; COGs: COG0277 FAD/FMN-containing dehydrogenase; InterPro IPR006094:IPR004113:IPR016166:IPR016168; KEGG: tcu:Tcur_3272 FAD linked oxidase domain protein; PFAM: FAD linked oxidase domain protein; SPTR: C1YNH9 FAD/FMN-dependent dehydrogenase; PFAM: FAD binding domain. (399 aa)
Ndas_0682D-lactate dehydrogenase (cytochrome); COGs: COG0277 FAD/FMN-containing dehydrogenase; InterProIPR016166:IPR016164:IPR016167:IPR006094:IPR 004113; KEGG: sen:SACE_6366 glycolate oxidase subunit; PFAM: FAD linked oxidase domain protein; PRIAM: D-lactate dehydrogenase (cytochrome); SPTR: C1YNH8 FAD/FMN-dependent dehydrogenase; PFAM: FAD binding domain; FAD linked oxidases, C-terminal domain; TIGRFAM: glycolate oxidase, subunit GlcD. (493 aa)
Ndas_0683COGs: COG2225 Malate synthase; InterPro IPR019830:IPR011076:IPR006252; KEGG: tfu:Tfu_0819 malate synthase; PFAM: Malate synthase family protein; PRIAM: Malate synthase; SPTR: C1YNH7 Malate synthase; TIGRFAM: malate synthase A; PFAM: Malate synthase; TIGRFAM: malate synthase A; Belongs to the malate synthase family. (534 aa)
mdhMalate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 2 family. (329 aa)
Ndas_0943COGs: COG0508 Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamide acyltransferase (E2) protein; InterProIPR014276:IPR000089:IPR004167:IPR001078:IPR 011053:IPR003016; KEGG: tfu:Tfu_0993 2-oxoglutarate dehydrogenase E2 component; PFAM: catalytic domain of components of various dehydrogenase complexes; biotin/lipoyl attachment domain-containing protein; E3 binding domain protein; SPTR: C1YQF3 2-oxoglutarate dehydrogenase E2 component; TIGRFAM: 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; PFAM: 2-oxoacid dehydrogenases acyltransferase (cataly [...] (600 aa)
Ndas_0999Aconitate hydratase domain protein; COGs: COG1048 Aconitase A; InterProIPR015931:IPR018136:IPR001030:IPR015932:IPR 000573:IPR015928; KEGG: ami:Amir_2132 aconitate hydratase 1; PFAM: aconitate hydratase domain protein; SPTR: C1YTQ9 Aconitase A; PFAM: Aconitase C-terminal domain; Aconitase family (aconitate hydratase); TIGRFAM: aconitate hydratase 1. (935 aa)
Ndas_1184FAD linked oxidase domain protein; COGs: COG0277 FAD/FMN-containing dehydrogenase; InterProIPR006094:IPR016166:IPR016164:IPR016167:IPR 016168:IPR016170; KEGG: plu:plu0950 hypothetical protein; PFAM: FAD linked oxidase domain protein; SPTR: C1YTL5 FAD/FMN-dependent dehydrogenase; PFAM: FAD binding domain. (482 aa)
Ndas_1214InterPro IPR006118; KEGG: hypothetical protein; SPTR: C1YTI6 Putative uncharacterized protein. (2922 aa)
Ndas_1429COGs: COG2224 Isocitrate lyase; InterPro IPR006254:IPR018523:IPR000918:IPR015813; KEGG: tfu:Tfu_1377 isocitrate lyase; PFAM: isocitrate lyase and phosphorylmutase; SPTR: C1YJE2 Isocitrate lyase; TIGRFAM: isocitrate lyase; PFAM: Isocitrate lyase family; TIGRFAM: isocitrate lyase. (432 aa)
Ndas_1731NADH/Ubiquinone/plastoquinone (complex I); COGs: COG0651 Formate hydrogenlyase subunit 3/Multisubunit Na+/H+ antiporter MnhD subunit; InterPro IPR003918:IPR001750; KEGG: jde:Jden_1915 NADH dehydrogenase (quinone); PFAM: NADH/Ubiquinone/plastoquinone (complex I); SPTR: C1YP02 Formate hydrogenlyase subunit 3/multisubunit Na+/H+ antiporter, MnhD subunit; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains. (505 aa)
Ndas_1832COGs: COG0372 Citrate synthase; InterPro IPR016141:IPR002020:IPR016142; KEGG: ami:Amir_4159 citrate synthase; PFAM: Citrate synthase; SPTR: C1YNP9 Citrate synthase; PFAM: Citrate synthase. (289 aa)
Ndas_1931Cytochrome c oxidase, subunit I; 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. (560 aa)
Ndas_2008FAD linked oxidase domain protein; COGs: COG0277 FAD/FMN-containing dehydrogenase; InterProIPR016166:IPR016164:IPR016167:IPR006094:IPR 004113; KEGG: sen:SACE_3889 FAD-binding oxidoreductase; PFAM: FAD linked oxidase domain protein; SPTR: C1YN20 FAD/FMN-dependent dehydrogenase; PFAM: FAD binding domain; FAD linked oxidases, C-terminal domain; TIGRFAM: glycolate oxidase, subunit GlcD. (460 aa)
Ndas_2866Aconitate hydratase 1; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (907 aa)
Ndas_3046FAD dependent oxidoreductase; COGs: COG0579 dehydrogenase; InterPro IPR006076; KEGG: sro:Sros_8880 hypothetical protein; PFAM: FAD dependent oxidoreductase; SPTR: C1YVF8 Predicted dehydrogenase; PFAM: FAD dependent oxidoreductase. (403 aa)
Ndas_3132Cytochrome b/b6 domain protein; COGs: COG1290 Cytochrome b subunit of the bc complex; InterPro IPR016174:IPR016175:IPR005797:IPR005798; KEGG: tfu:Tfu_1019 ubiquinol-cytochrome c reductase, cytochrome b subunit; PFAM: Cytochrome b/b6 domain; SPTR: C1YW48 Cytochrome b subunit of the bc complex; PFAM: Cytochrome b(N-terminal)/b6/petB. (551 aa)
Ndas_3135Cytochrome-c oxidase; COGs: COG1845 Heme/copper-type cytochrome/quinol oxidase subunit 3; InterPro IPR000298; KEGG: tfu:Tfu_1022 cytochrome c oxidase subunit III; PFAM: cytochrome c oxidase subunit III; PRIAM: Cytochrome-c oxidase; SPTR: C1YW45 Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III. (208 aa)
Ndas_3149Cytochrome c oxidase, subunit I; 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. (558 aa)
Ndas_3602COGs: COG1271 Cytochrome bd-type quinol oxidase subunit 1; InterPro IPR002585; KEGG: tfu:Tfu_0766 highly cytochrome d ubiquinol oxidase subunit I; PFAM: cytochrome bd ubiquinol oxidase subunit I; SPTR: C1YQX6 Cytochrome bd-type quinol oxidase, subunit 1; PFAM: Bacterial Cytochrome Ubiquinol Oxidase. (422 aa)
Ndas_3603COGs: COG1294 Cytochrome bd-type quinol oxidase subunit 2; InterPro IPR003317; KEGG: tfu:Tfu_0765 putative cytochrome d ubiquinol oxidase subunit II; PFAM: cytochrome bd ubiquinol oxidase subunit II; SPTR: C1YQX5 Cytochrome bd-type quinol oxidase, subunit 2; PFAM: Cytochrome oxidase subunit II. (307 aa)
Ndas_3681COGs: COG0567 2-oxoglutarate dehydrogenase complex dehydrogenase (E1); InterPro IPR011603:IPR001078:IPR001017:IPR005475; KEGG: tfu:Tfu_0566 alpha-ketoglutarate decarboxylase; PFAM: Transketolase central region; dehydrogenase E1 component; catalytic domain of components of various dehydrogenase complexes; SPTR: C1YU54 2-oxoglutarate dehydrogenase E1 component; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain); Dehydrogenase E1 component; Transketolase, pyrimidine binding domain; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 [...] (1219 aa)
Ndas_3921COGs: COG0479 Succinate dehydrogenase/fumarate reductase Fe-S protein subunit; InterProIPR001041:IPR009051:IPR004489:IPR001450:IPR 012675:IPR012285:IPR006058:IPR017900:IPR017896; KEGG: tfu:Tfu_2451 succinate dehydrogenase/fumarate reductase iron-sulfur subunit; PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; ferredoxin; SPTR: C1YKT0 Succinate dehydrogenase subunit B; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein. (248 aa)
ppcPhosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle; Belongs to the PEPCase type 1 family. (908 aa)
Ndas_3960Isocitrate dehydrogenase, NADP-dependent; COGs: COG0538 Isocitrate dehydrogenase; InterPro IPR004790:IPR019818:IPR001804; KEGG: tfu:Tfu_2568 isocitrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase; PRIAM: Isocitrate dehydrogenase (NADP(+)); SPTR: C1YKN9 Isocitrate dehydrogenase (NADP); TIGRFAM: isocitrate dehydrogenase, NADP-dependent; PFAM: Isocitrate/isopropylmalate dehydrogenase; TIGRFAM: isocitrate dehydrogenase, NADP-dependent, eukaryotic type; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (405 aa)
Ndas_4112Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; COGs: COG1894 NADH:ubiquinone oxidoreductase NADH-binding (51 kD) subunit; InterProIPR012335:IPR012336:IPR002023:IPR011538:IPR 019554:IPR019575:IPR001949; KEGG: sma:SAV_1835 NADH dehydrogenase I chain F; PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; NADH dehydrogenase (ubiquinone) 24 kDa subunit; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; SPTR: C1YSE4 NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit; PFAM: NADH-ubiquinone oxidoreductase-F iron [...] (656 aa)
sucD-2succinyl-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. (312 aa)
sucC-2succinyl-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. (395 aa)
Ndas_4410COGs: COG0372 Citrate synthase; InterProIPR016141:IPR002020:IPR016142:IPR010953:IPR 019810; KEGG: rop:ROP_50580 citrate synthase; PFAM: Citrate synthase; SPTR: C1YGF6 Citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; TIGRFAM: citrate synthase I (hexameric type); Belongs to the citrate synthase family. (429 aa)
Ndas_4458Metallophosphoesterase; InterPro IPR004843; KEGG: tfu:Tfu_2852 putative integral membrane protein; PFAM: metallophosphoesterase; SPTR: C1YGB0 Calcineurin-like phosphoesterase; PFAM: Calcineurin-like phosphoesterase. (514 aa)
Ndas_4892NADH/Ubiquinone/plastoquinone (complex I); COGs: COG0651 Formate hydrogenlyase subunit 3/Multisubunit Na+/H+ antiporter MnhD subunit; InterPro IPR003918:IPR001750; KEGG: tfu:Tfu_0348 putative monovalent cation/H+ antiporter subunit D; PFAM: NADH/Ubiquinone/plastoquinone (complex I); SPTR: C1YJ08 Formate hydrogenlyase subunit 3/multisubunit Na+/H+ antiporter, MnhD subunit; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains. (552 aa)
Ndas_4932Aconitate hydratase; COGs: COG1048 Aconitase A; InterProIPR015931:IPR006250:IPR001030:IPR015932:IPR 000573:IPR015928; KEGG: svi:Svir_23930 aconitase; PFAM: aconitate hydratase domain protein; SPTR: C1YIW8 Aconitase; TIGRFAM: aconitate hydratase; PFAM: Aconitase C-terminal domain; Aconitase family (aconitate hydratase); TIGRFAM: aconitate hydratase, putative, Aquifex type. (652 aa)
Ndas_5058NADH-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. (439 aa)
Ndas_5059NADH-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. (830 aa)
nuoHNADH 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. (457 aa)
nuoINADH-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. (185 aa)
nuoKNADH-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. (99 aa)
Ndas_5064Proton-translocating NADH-quinone oxidoreductase, chain L; COGs: COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter MnhA subunit; InterProIPR003945:IPR003916:IPR018393:IPR018486:IPR 001516:IPR001750; KEGG: tfu:Tfu_2684 NADH dehydrogenase subunit L; PFAM: NADH/Ubiquinone/plastoquinone (complex I); NADH-Ubiquinone oxidoreductase (complex I) chain 5/L domain protein; PRIAM: NADH dehydrogenase (quinone); SPTR: C1YIA1 NADH dehydrogenase subunit L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone/plastoquinone (c [...] (649 aa)
Ndas_5065Proton-translocating NADH-quinone oxidoreductase, chain M; COGs: COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M); InterPro IPR010227:IPR003918:IPR001750; KEGG: tfu:Tfu_2683 NADH dehydrogenase subunit M; PFAM: NADH/Ubiquinone/plastoquinone (complex I); SPTR: C1YIA0 NADH dehydrogenase subunit M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M. (555 aa)
nuoNProton-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. (550 aa)
Ndas_5088Thiamine pyrophosphate protein domain protein TPP-binding protein; COGs: COG1013 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductase beta subunit; InterPro IPR011766; KEGG: tfu:Tfu_2675 2-oxoglutarate ferredoxin oxidoreductase subunit beta; PFAM: thiamine pyrophosphate protein domain protein TPP-binding; SPTR: C1YI77 2-oxoacid:ferredoxin oxidoreductase, beta subunit; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain. (363 aa)
Ndas_5089Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; COGs: COG0674 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductase alpha subunit; InterPro IPR002869:IPR009014:IPR002880; KEGG: tfu:Tfu_2674 2-oxoglutarate ferredoxin oxidoreductase, alpha subunit; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; SPTR: C1YI76 2-oxoacid:ferredoxin oxidoreductase, alpha subunit; PFAM: domain; Pyruvate ferredoxin/flavodoxin oxidoreductase. (616 aa)
Ndas_5194Molybdopterin oxidoreductase; COGs: COG0243 Anaerobic dehydrogenase typically selenocysteine-containing; InterPro IPR006655:IPR009010:IPR006657:IPR006656; KEGG: tfu:Tfu_0340 trimethylamine-N-oxide reductase (cytochrome c); PFAM: molybdopterin oxidoreductase; molydopterin dinucleotide-binding region; SPTR: C1YI26 Anaerobic dehydrogenase, typically selenocysteine-containing; PFAM: Molybdopterin oxidoreductase; Molydopterin dinucleotide binding domain; TIGRFAM: molybdopterin guanine dinucleotide-containing S/N-oxide reductases; Belongs to the prokaryotic molybdopterin-containing oxidoredu [...] (845 aa)
Your Current Organism:
Nocardiopsis dassonvillei
NCBI taxonomy Id: 446468
Other names: N. dassonvillei subsp. dassonvillei DSM 43111, Nocardiopsis dassonvillei DSM 43111, Nocardiopsis dassonvillei subsp. dassonvillei DSM 43111, Nocardiopsis dassonvillei subsp. dassonvillei str. DSM 43111, Nocardiopsis dassonvillei subsp. dassonvillei strain DSM 43111
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