STRINGSTRING
AGS67041.1 AGS67041.1 AGS67043.1 AGS67043.1 AGS67307.1 AGS67307.1 AGS67664.1 AGS67664.1 AGS68827.1 AGS68827.1 ctaB ctaB AGS69071.1 AGS69071.1 AGS69072.1 AGS69072.1 AGS69073.1 AGS69073.1 AGS69074.1 AGS69074.1 AGS69078.1 AGS69078.1 AGS69079.1 AGS69079.1 AGS70028.1 AGS70028.1 ppk ppk AGS70457.1 AGS70457.1 AGS70589.1 AGS70589.1 AGS70590.1 AGS70590.1 ppa ppa nuoD nuoD AGS71055.1 AGS71055.1 AGS71056.1 AGS71056.1 nuoA nuoA nuoB nuoB nuoC nuoC nuoD-2 nuoD-2 AGS71114.1 AGS71114.1 AGS71115.1 AGS71115.1 AGS71116.1 AGS71116.1 nuoH nuoH nuoI nuoI AGS71119.1 AGS71119.1 nuoK nuoK AGS71121.1 AGS71121.1 AGS71122.1 AGS71122.1 nuoN nuoN AGS71146.1 AGS71146.1 nuoB-2 nuoB-2 nuoH-2 nuoH-2 nuoI-2 nuoI-2 AGS71151.1 AGS71151.1 nuoK-2 nuoK-2 AGS71153.1 AGS71153.1 AGS71154.1 AGS71154.1 nuoN-2 nuoN-2 sdhB sdhB sdhA1 sdhA1 AGS71369.1 AGS71369.1 AGS71370.1 AGS71370.1 AGS71600.1 AGS71600.1 sdhA2 sdhA2 atpB atpB atpE atpE atpF atpF atpH atpH atpA atpA atpG atpG atpD atpD atpC atpC AGS72784.1 AGS72784.1 AGS73116.1 AGS73116.1 AGS73117.1 AGS73117.1 AGS73192.1 AGS73192.1 sdhA3 sdhA3 AGS73194.1 AGS73194.1 AGS73348.1 AGS73348.1 AGS73350.1 AGS73350.1 AGS73371.1 AGS73371.1 AGS73388.1 AGS73388.1
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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:
AGS67041.1FAD-dependent pyridine nucleotide-disulfide oxidoreductase; COG1252 NADH dehydrogenase, FAD-containing subunit. (400 aa)
AGS67043.1Oxidoreductase; COG1252 NADH dehydrogenase, FAD-containing subunit. (402 aa)
AGS67307.1Cytochrome 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. (574 aa)
AGS67664.1Oxidoreductase; COG1252 NADH dehydrogenase, FAD-containing subunit. (459 aa)
AGS68827.1COG1612 Uncharacterized protein required for cytochrome oxidase assembly. (336 aa)
ctaBProtoheme 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. (306 aa)
AGS69071.1COG1290 Cytochrome b subunit of the bc complex. (543 aa)
AGS69072.1Ubiquinol-cytochrome c reductase iron-sulfur 'Rieske' subunit; COG0723 Rieske Fe-S protein. (331 aa)
AGS69073.1COG2010 Cytochrome c, mono- and diheme variants. (270 aa)
AGS69074.1COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. (206 aa)
AGS69078.1Cytochrome 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. (577 aa)
AGS69079.1COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. (276 aa)
AGS70028.1FAD-dependent pyridine nucleotide-disulfide oxidoreductase; COG1252 NADH dehydrogenase, FAD-containing subunit. (460 aa)
ppkPolyphosphate kinase; 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. (716 aa)
AGS70457.1COG1252 NADH dehydrogenase, FAD-containing subunit. (459 aa)
AGS70589.1COG1294 Cytochrome bd-type quinol oxidase, subunit 2. (339 aa)
AGS70590.1COG1271 Cytochrome bd-type quinol oxidase, subunit 1. (502 aa)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (163 aa)
nuoDNADH dehydrogenase subunit NuoD2; 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. (382 aa)
AGS71055.1COG1271 Cytochrome bd-type quinol oxidase, subunit 1. (486 aa)
AGS71056.1COG1294 Cytochrome bd-type quinol oxidase, subunit 2. (346 aa)
nuoANADH dehydrogenase 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)
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 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. (184 aa)
nuoCNADH 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. (254 aa)
nuoD-2NADH dehydrogenase 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. (446 aa)
AGS71114.1COG1905 NADH:ubiquinone oxidoreductase 24 kD subunit. (288 aa)
AGS71115.1NADH 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. (448 aa)
AGS71116.1NADH 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. (834 aa)
nuoHNADH:ubiquinone oxidoreductase 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. (459 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. (216 aa)
AGS71119.1NADH:ubiquinone oxidoreductase 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. (282 aa)
nuoKNADH:ubiquinone oxidoreductase 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. (99 aa)
AGS71121.1COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit. (648 aa)
AGS71122.1COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). (523 aa)
nuoNNADH:ubiquinone oxidoreductase 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. (549 aa)
AGS71146.1NADH dehydrogenase I subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (139 aa)
nuoB-2NADH 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. (206 aa)
nuoH-2NADH 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. (322 aa)
nuoI-2NADH 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. (184 aa)
AGS71151.1NADH dehydrogenase I 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. (221 aa)
nuoK-2NADH dehydrogenase subunit NuoK2; 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. (128 aa)
AGS71153.1COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit. (664 aa)
AGS71154.1COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). (524 aa)
nuoN-2NADH 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. (511 aa)
sdhBCOG0479 Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (259 aa)
sdhA1COG1053 Succinate dehydrogenase/fumarate reductase, flavoprotein subunit. (584 aa)
AGS71369.1COG2142 Succinate dehydrogenase, hydrophobic anchor subunit. (160 aa)
AGS71370.1COG2009 Succinate dehydrogenase/fumarate reductase, cytochrome b subunit. (126 aa)
AGS71600.1COG0479 Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit. (256 aa)
sdhA2COG1053 Succinate dehydrogenase/fumarate reductase, flavoprotein subunit. (643 aa)
atpBF0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. (256 aa)
atpEATP synthase 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)
atpFF0F1 ATP synthase subunit B; 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. (182 aa)
atpHF0F1 ATP synthase subunit delta; 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. (271 aa)
atpAF0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (530 aa)
atpGF0F1 ATP synthase subunit gamma; 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. (305 aa)
atpDF0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (478 aa)
atpCF0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (125 aa)
AGS72784.1COG1252 NADH dehydrogenase, FAD-containing subunit. (511 aa)
AGS73116.1COG1271 Cytochrome bd-type quinol oxidase, subunit 1. (471 aa)
AGS73117.1COG1294 Cytochrome bd-type quinol oxidase, subunit 2. (329 aa)
AGS73192.1Cytochrome b subunit; COG0642 Signal transduction histidine kinase. (223 aa)
sdhA3COG1053 Succinate dehydrogenase/fumarate reductase, flavoprotein subunit. (649 aa)
AGS73194.1COG0479 Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit. (249 aa)
AGS73348.1COG1290 Cytochrome b subunit of the bc complex. (497 aa)
AGS73350.1Cytochrome C oxidase polypeptide 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. (554 aa)
AGS73371.1RNA polymerase sigma foactor. (341 aa)
AGS73388.1Cytochrome 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. (564 aa)
Your Current Organism:
Streptomyces collinus
NCBI taxonomy Id: 1214242
Other names: S. collinus Tu 365, Streptomyces collinus Tu 365
Server load: low (20%) [HD]