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ppk ppk atpA atpA atpH atpH yumB yumB ctaA ctaA yumB1 yumB1 ppa1 ppa1 sdhC sdhC nuoN nuoN nqo13 nqo13 nuoL nuoL nuoK nuoK ndhG ndhG nuoF2 nuoF2 nuoE nuoE ndh2 ndh2 AFE04066.1 AFE04066.1 ctaB ctaB sdhB sdhB sdhA sdhA nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD nuoG nuoG nuoH nuoH nuoI nuoI AFE06469.1 AFE06469.1 ppa ppa coxB coxB ctaD ctaD coxC coxC AFE07014.1 AFE07014.1 cydB cydB cydA cydA atpC atpC atpD atpD atpG atpG atpF atpF atpE atpE atpB atpB coxN coxN coxM coxM AFE07875.1 AFE07875.1 coxC1 coxC1 ctaD1 ctaD1 coxB1 coxB1
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
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:
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. (721 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. Belongs to the ATPase alpha/beta chains family. (515 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; Belongs to the ATPase delta chain family. (180 aa)
yumBNADH dehydrogenase. (442 aa)
ctaACytochrome oxidase assembly protein. (324 aa)
yumB1NADH dehydrogenase. (468 aa)
ppa1Inorganic pyrophosphatase. (179 aa)
sdhCSuccinate dehydrogenase cytochrome b558 subunit. (227 aa)
nuoNNADH 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 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. (520 aa)
nqo13NADH dehydrogenase I subunit M. (563 aa)
nuoLNADH dehydrogenase I subunit L. (742 aa)
nuoKNADH 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 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)
ndhGNADH 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)
nuoF2NADH 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. (447 aa)
nuoENADH dehydrogenase I subunit E. (162 aa)
ndh2Putative NADH dehydrogenase. (459 aa)
AFE04066.1Polyphosphate kinase 2. (266 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. (294 aa)
sdhBSuccinate dehydrogenase iron-sulfur subunit. (268 aa)
sdhASuccinate dehydrogenase flavoprotein subunit. (625 aa)
nuoAPutative NADH 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 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. (122 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. (187 aa)
nuoCNADH dehydrogenase I 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; Belongs to the complex I 30 kDa subunit family. (177 aa)
nuoDNADH 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 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 49 kDa subunit family. (419 aa)
nuoGPutative NADH dehydrogenase I subunit G. (630 aa)
nuoHPutative NADH 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. (481 aa)
nuoINADH 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. (252 aa)
AFE06469.1PPase family protein. (145 aa)
ppaInorganic pyrophosphatase. (241 aa)
coxBCytochrome c oxidase subunit II. (348 aa)
ctaDCytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (558 aa)
coxCCytochrome c oxidase subunit III. (220 aa)
AFE07014.1Putative cytochrome c oxidase subunit IV. (146 aa)
cydBCytochrome d ubiquinol oxidase subunit II. (343 aa)
cydACytochrome d ubiquinol oxidase subunit I. (448 aa)
atpCF0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (134 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; Belongs to the ATPase alpha/beta chains family. (481 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. (297 aa)
atpFATP synthase F0 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)
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. (76 aa)
atpBATP synthase F0 subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (351 aa)
coxNAlternative cytochrome c oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family. (577 aa)
coxMAlternative cytochrome c oxidase subunit 2. (278 aa)
AFE07875.1Putative cytochrome c oxidase subunit IV. (134 aa)
coxC1Cytochrome c oxidase subunit III. (209 aa)
ctaD1Cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (535 aa)
coxB1Cytochrome c oxidase subunit II. (336 aa)
Your Current Organism:
Corallococcus coralloides
NCBI taxonomy Id: 1144275
Other names: C. coralloides DSM 2259, Corallococcus coralloides ATCC 25202, Corallococcus coralloides DSM 2259, Corallococcus coralloides NBRC 100086, Corallococcus coralloides str. DSM 2259, Corallococcus coralloides strain DSM 2259
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