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nuoA1 nuoA1 nuoB1 nuoB1 nuoC1 nuoC1 nuoD1 nuoD1 nuoE1 nuoE1 nuoF1 nuoF1 nuoG1 nuoG1 nuoH1 nuoH1 nuoI1 nuoI1 nuoJ1 nuoJ1 nuoK1 nuoK1 nuoL1 nuoL1 nuoN1 nuoN1 STH1655 STH1655 STH1656 STH1656 STH1657 STH1657 STH1658 STH1658 STH1659 STH1659 STH1660 STH1660 STH1661 STH1661 STH1691 STH1691 STH1692 STH1692 ctaB ctaB STH2096 STH2096 STH2097 STH2097 STH2098 STH2098 STH2099 STH2099 STH2100 STH2100 nuoN2 nuoN2 nuoM2 nuoM2 nuoL2 nuoL2 nuoK2 nuoK2 nuoJ2 nuoJ2 nuoI2 nuoI2 nuoH2 nuoH2 nuoD2 nuoD2 nuoC2 nuoC2 nuoA2 nuoA2 nuoB2 nuoB2 STH2945 STH2945 STH3103 STH3103 STH3144 STH3144 STH3146 STH3146 STH3147 STH3147 STH3148 STH3148 STH3149 STH3149 STH3152 STH3152 STH3153 STH3153 STH3207 STH3207 STH3208 STH3208 STH3209 STH3209 STH548 STH548 STH634 STH634 STH642 STH642 STH643 STH643 STH929 STH929 STH934 STH934
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
nuoA1NADH dehydrogenase I subunit 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 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. (117 aa)
nuoB1NADH dehydrogenase I 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 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. (153 aa)
nuoC1NADH dehydrogenase I subunit C. (200 aa)
nuoD1NADH dehydrogenase I subunit 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 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. (404 aa)
nuoE1NADH dehydrogenase I subunit E. (274 aa)
nuoF1NADH dehydrogenase I 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. (425 aa)
nuoG1NADH dehydrogenase I 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. (817 aa)
nuoH1NADH dehydrogenase I subunit 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. (328 aa)
nuoI1NADH dehydrogenase I 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. (162 aa)
nuoJ1NADH dehydrogenase I subunit 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. (168 aa)
nuoK1NADH dehydrogenase I subunit 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 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. (102 aa)
nuoL1NADH dehydrogenase I subunit L. (640 aa)
nuoN1NADH dehydrogenase I 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 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. (491 aa)
STH1655Na+/H+ antiporter subunit. (754 aa)
STH1656Na+/H+ antiporter subunit. (164 aa)
STH1657Na+/H+ antiporter subunit. (127 aa)
STH1658Na+/H+ antiporter subunit. (494 aa)
STH1659Na+/H+ antiporter subunit. (159 aa)
STH1660Na+/H+ antiporter subunit. (116 aa)
STH1661Na+/H+ antiporter subunit. (116 aa)
STH1691Cytochrome D ubiquinol oxidase subunit II. (345 aa)
STH1692Cytochrome D ubiquinol oxidase subunit I. (420 aa)
ctaBPutative heme O synthase; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (298 aa)
STH2096Cytochrome 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). (342 aa)
STH2097Cytochrome 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. (628 aa)
STH2098Cytochrome C oxidase subunit III. (210 aa)
STH2099Conserved hypothetical protein. (78 aa)
STH2100Conserved hypothetical protein. (297 aa)
nuoN2NADH dehydrogenase I 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 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. (508 aa)
nuoM2NADH dehydrogenase I subunit M. (508 aa)
nuoL2NADH dehydrogenase I subunit L. (685 aa)
nuoK2NADH dehydrogenase I subunit 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 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. (107 aa)
nuoJ2NADH dehydrogenase I subunit 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. (176 aa)
nuoI2NADH dehydrogenase I 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. (240 aa)
nuoH2NADH dehydrogenase I subunit 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. (394 aa)
nuoD2NADH dehydrogenase I subunit 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 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. (384 aa)
nuoC2NADH dehydrogenase I subunit C; 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. (156 aa)
nuoA2NADH dehydrogenase I subunit 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 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. (119 aa)
nuoB2NADH dehydrogenase I 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 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. (182 aa)
STH2945Conserved hypothetical protein. (439 aa)
STH3103NADH dehydrogenase subunit. (394 aa)
STH3144Hypothetical protein. (312 aa)
STH3146Plastoquinol--plastocyanin reductase. (178 aa)
STH3147Putative menaquinol-cytochrome C reductase. (253 aa)
STH3148Menaquinol-cytochrome C reductase. (258 aa)
STH3149Putative ferredoxin. (408 aa)
STH3152Cytochrome C oxidase mono-heme subunit. (320 aa)
STH3153Cytochrome C oxidase heme b and copper-binding subunit. (467 aa)
STH3207Putative iron hydrogenase small subunit gamma. (186 aa)
STH3208Iron hydrogenase beta subunit. (618 aa)
STH3209Iron hydrogenase. (596 aa)
STH548ABC transporter ATP-binding protein. (351 aa)
STH634Alpha/beta hydrolase. (306 aa)
STH642Cytochrome D ubiquinol oxidase subunit I. (445 aa)
STH643Cytochrome D ubiquinol oxidase subunit II. (342 aa)
STH929Conserved hypothetical protein. (436 aa)
STH934Ferredoxin. (96 aa)
Your Current Organism:
Symbiobacterium thermophilum
NCBI taxonomy Id: 292459
Other names: S. thermophilum IAM 14863, Symbiobacterium thermophilum IAM 14863, Symbiobacterium thermophilum str. IAM 14863, Symbiobacterium thermophilum strain IAM 14863
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