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D782_0228 D782_0228 ppk ppk nuoA nuoA nuoB nuoB nuoC nuoC D782_1386 D782_1386 D782_1387 D782_1387 D782_1388 D782_1388 nuoH nuoH nuoI nuoI D782_1391 D782_1391 nuoK nuoK D782_1393 D782_1393 D782_1394 D782_1394 nuoN nuoN D782_1666 D782_1666 D782_1995 D782_1995 D782_2283 D782_2283 D782_2284 D782_2284 D782_3120 D782_3120 D782_3121 D782_3121 D782_3122 D782_3122 D782_3132 D782_3132 D782_3133 D782_3133 D782_3134 D782_3134 D782_3135 D782_3135 D782_3295 D782_3295 D782_3407 D782_3407 D782_3408 D782_3408 D782_3409 D782_3409 D782_3410 D782_3410 cyoE cyoE ppa ppa D782_4104 D782_4104 D782_4105 D782_4105 frdC frdC frdD frdD atpB atpB atpE atpE atpF atpF atpH atpH atpA atpA atpG atpG atpD atpD atpC atpC
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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D782_0228NADH dehydrogenase, FAD-containing subunit; PFAM: Pyridine nucleotide-disulphide oxidoreductase. (400 aa)
ppkPolyphosphate kinase 1; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family. (686 aa)
nuoANADH:ubiquinone oxidoreductase subunit 3 (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. (146 aa)
nuoBNADH dehydrogenase subunit 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. (224 aa)
nuoCNADH/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 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 C-terminal section; belongs to the complex I 49 kDa subunit family. (601 aa)
D782_1386PFAM: Respiratory-chain NADH dehydrogenase 24 Kd subunit; TIGRFAM: NADH-quinone oxidoreductase, E subunit. (166 aa)
D782_1387NADH dehydrogenase subunit 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)
D782_1388NADH dehydrogenase subunit 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. (908 aa)
nuoHNADH:ubiquinone oxidoreductase subunit 1 (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)
nuoINADH dehydrogenase subunit 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)
D782_1391NADH:ubiquinone oxidoreductase subunit 6 (chain J); 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. (184 aa)
nuoKNADH:ubiquinone oxidoreductase subunit 11 or 4L (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)
D782_1393PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L. (613 aa)
D782_1394PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M. (509 aa)
nuoNNADH dehydrogenase subunit 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. (485 aa)
D782_1666Flavocytochrome c; PFAM: FAD binding domain; NADH:flavin oxidoreductase / NADH oxidase family; FMN-binding domain; TIGRFAM: flavocytochrome c. (927 aa)
D782_1995NADH dehydrogenase, FAD-containing subunit; PFAM: Pyridine nucleotide-disulphide oxidoreductase. (434 aa)
D782_2283Cytochrome bd-type quinol oxidase, subunit 1; PFAM: Bacterial Cytochrome Ubiquinol Oxidase. (465 aa)
D782_2284PFAM: Cytochrome oxidase subunit II; TIGRFAM: cytochrome d oxidase, subunit II (cydB). (336 aa)
D782_3120PFAM: Membrane bound YbgT-like protein; TIGRFAM: cyd operon protein YbgT. (36 aa)
D782_3121PFAM: Cytochrome oxidase subunit II; TIGRFAM: cytochrome d oxidase, subunit II (cydB). (379 aa)
D782_3122Cytochrome bd-type quinol oxidase, subunit 1; PFAM: Bacterial Cytochrome Ubiquinol Oxidase. (522 aa)
D782_3132Succinate dehydrogenase subunit B; PFAM: 2Fe-2S iron-sulfur cluster binding domain; 4Fe-4S dicluster domain; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (238 aa)
D782_3133PFAM: FAD binding domain; Fumarate reductase flavoprotein C-term; TIGRFAM: succinate dehydrogenase, flavoprotein subunit, E. coli/mitochondrial subgroup; succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (588 aa)
D782_3134Succinate dehydrogenase, hydrophobic membrane anchor protein; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (115 aa)
D782_3135PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit; TIGRFAM: succinate dehydrogenase, cytochrome b556 subunit. (134 aa)
D782_3295Inorganic pyrophosphatase/exopolyphosphatase; PFAM: DHH family; DHHA2 domain. (300 aa)
D782_3407PFAM: COX Aromatic Rich Motif; Cytochrome C oxidase subunit II, periplasmic domain; TIGRFAM: cytochrome o ubiquinol oxidase subunit II. (315 aa)
D782_3408Cytochrome bo3 quinol oxidase subunit 1 apoprotein; PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome o ubiquinol oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family. (663 aa)
D782_3409PFAM: Cytochrome c oxidase subunit III; TIGRFAM: cytochrome o ubiquinol oxidase, subunit III. (203 aa)
D782_3410PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: cytochrome o ubiquinol oxidase subunit IV. (109 aa)
cyoEProtoheme IX farnesyltransferase; 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)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (175 aa)
D782_4104Succinate dehydrogenase subunit A; PFAM: FAD binding domain; Fumarate reductase flavoprotein C-term; TIGRFAM: fumarate reductase, flavoprotein subunit; succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup. (596 aa)
D782_4105PFAM: 2Fe-2S iron-sulfur cluster binding domain; 4Fe-4S dicluster domain; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (244 aa)
frdCFumarate reductase subunit C; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. (131 aa)
frdDFumarate reductase subunit D; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. (119 aa)
atpBF0F1-type ATP synthase, alpha subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (271 aa)
atpEATP synthase, F0 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)
atpFATP synthase F0 subcomplex B subunit; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. (156 aa)
atpHATP synthase, F1 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)
atpAProton translocating ATP synthase, F1 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)
atpGATP synthase F1 subcomplex 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. (287 aa)
atpDATP synthase F1 subcomplex 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)
atpCATP synthase, F1 epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (139 aa)
Your Current Organism:
Enterobacteriaceae bacterium strain
NCBI taxonomy Id: 693444
Other names: E. bacterium strain FGI 57, Enterobacteriaceae bacterium strain FGI 57
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