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GDI3312 GDI3312 cycB cycB GDI1876 GDI1876 fdxA fdxA cyoD cyoD cyoC cyoC cyoB cyoB cyoA cyoA adhA adhA adhB adhB petC petC petB petB ccp ccp ctaD ctaD msrQ msrQ adhB-2 adhB-2 nuoN nuoN nuoM-2 nuoM-2 nuoL nuoL nuoJ nuoJ nuoG nuoG nuoF nuoF nuoCD nuoCD nuoB nuoB nuoA nuoA ccp-2 ccp-2 ctaE ctaE ctaD-2 ctaD-2 ctaC ctaC GDI2617 GDI2617 GDI2618 GDI2618 GDI2621 GDI2621 GDI2761 GDI2761 nouN nouN nouL nouL nouJ nouJ nouG nouG nouF nouF nouC nouC nuoB-2 nuoB-2 nouA nouA petA petA adhB-3 adhB-3 GDI3310 GDI3310 cycA cycA GDI3316 GDI3316 GDI3621 GDI3621 acpD acpD GDI3651 GDI3651 GDI0274 GDI0274 fixA fixA fixB fixB cybB cybB cydA cydA nuoM nuoM GDI0649 GDI0649 GDI0856 GDI0856 GDI0860 GDI0860 GDI1142 GDI1142 etfD etfD etfB etfB etfA etfA sdhB sdhB sdhC sdhC GDI1482 GDI1482 GDI1787 GDI1787
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:
GDI3312Conserved hypothetical protein. (459 aa)
cycBPutative cytochrome c-552. (166 aa)
GDI1876Putative cytochrome c homolog. (175 aa)
fdxAPutative ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (110 aa)
cyoDPutative cytochrome o ubiquinol oxidase protein cyoD. (110 aa)
cyoCPutative cytochrome o ubiquinol oxidase subunit 3. (201 aa)
cyoBUbiquinol oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family. (664 aa)
cyoAUbiquinol oxidase subunit 2 precursor. (315 aa)
adhAAlcohol dehydrogenase [acceptor] precursor. (736 aa)
adhBPutative alcohol dehydrogenase cytochrome c subunit precursor. (470 aa)
petCPutative cytochrome c. (253 aa)
petBPutative cytochrome b; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (417 aa)
ccpPutative cytochrome c551 peroxidase precursor. (452 aa)
ctaDPutative cytochrome c oxidase subunit 1. (470 aa)
msrQPutative membrane protein; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, usin [...] (207 aa)
adhB-2Putative alcohol dehydrogenase cytochrome c subunit. (139 aa)
nuoNPutative 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 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. (493 aa)
nuoM-2Putative NADH-quinone oxidoreductase chain M. (493 aa)
nuoLPutative NADH-quinone oxidoreductase chain L. (625 aa)
nuoJPutative NADH-quinone oxidoreductase 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. (168 aa)
nuoGPutative NADH-quinone oxidoreductase chain 3; Belongs to the complex I 75 kDa subunit family. (896 aa)
nuoFPutative NADH-quinone oxidoreductase chain F. (428 aa)
nuoCDPutative ADH-quinone oxidoreductase chain C/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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (601 aa)
nuoBPutative NADH-quinone oxidoreductase chain 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. (211 aa)
nuoAPutative NADH-quinone oxidoreductase 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. (147 aa)
ccp-2Putative cytochrome c peroxidase. (451 aa)
ctaEPutative cytochrome c oxidase subunit 3. (225 aa)
ctaD-2Putative cytochrome c oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family. (540 aa)
ctaCPutative cytochrome c oxidase subunit 2 precursor. (326 aa)
GDI2617Conserved hypothetical protein. (169 aa)
GDI2618Putative membrane protein. (172 aa)
GDI2621Putative chaperone protein HtpG. (217 aa)
GDI2761Putative membrane protein. (187 aa)
nouNPutative 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 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. (475 aa)
nouLPutative NADH-quinone oxidoreductase chain L. (626 aa)
nouJPutative NADH-quinone oxidoreductase 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. (253 aa)
nouGNADH-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. (689 aa)
nouFNADH-quinone oxidoreductase chain 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. (441 aa)
nouCNADH-quinone oxidoreductase chain 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. (213 aa)
nuoB-2NADH-quinone oxidoreductase chain B; 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 (By similarity). (191 aa)
nouAPutative NADH-ubiquinone oxidoreductase chain 3; 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. (121 aa)
petAPutative ubiquinol-cytochrome c reductase iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (227 aa)
adhB-3Putative alcohol dehydrogenase cytochrome c subunit precursor. (442 aa)
GDI3310Putative NADH-quinone oxidoreductase chain B. (166 aa)
cycAPutative cytochrome c-552. (153 aa)
GDI3316Putative membrane protein. (772 aa)
GDI3621Putative membrane protein. (207 aa)
acpDPutative acyl carrier protein phosphodiesterase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (201 aa)
GDI3651Putative cytochrome B561. (185 aa)
GDI0274Conserved hypothetical protein. (170 aa)
fixAProtein fixA. (284 aa)
fixBfixB. (364 aa)
cybBPutative cytochrome protein. (191 aa)
cydAPutative cytochrome d ubiquinol oxidase subunit 1. (466 aa)
nuoMPutative NADH-quinone oxidoreductase chain M. (524 aa)
GDI0649Putative exported protein. (117 aa)
GDI0856Putative gluconate 2-dehydrogenase cytochrome c subunit precursor. (448 aa)
GDI0860Puative alcohol dehydrogenase cytochrome c subunit precursor. (466 aa)
GDI1142Putative membrane protein. (208 aa)
etfDElectron transfer flavoprotein-ubiquinone oxidoreductase; Accepts electrons from ETF and reduces ubiquinone. (545 aa)
etfBElectron transfer flavoprotein subunit beta. (249 aa)
etfAElectron transfer flavoprotein subunit alpha. (311 aa)
sdhBSuccinate dehydrogenase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (260 aa)
sdhCPutative Succinate dehydrogenase cytochrome b556 subunit. (153 aa)
GDI1482Putative Cytochrome b561. (203 aa)
GDI1787Alcohol dehydrogenase cytochrome c subunit precursor. (420 aa)
Your Current Organism:
Gluconacetobacter diazotrophicus
NCBI taxonomy Id: 272568
Other names: G. diazotrophicus PA1 5, Gluconacetobacter diazotrophicus ATCC 49037, Gluconacetobacter diazotrophicus BR 11281, Gluconacetobacter diazotrophicus CCUG 37298, Gluconacetobacter diazotrophicus CIP 103539, Gluconacetobacter diazotrophicus DSM 5601, Gluconacetobacter diazotrophicus LMG 7603, Gluconacetobacter diazotrophicus NCCB 89154, Gluconacetobacter diazotrophicus PA1 5, Gluconacetobacter diazotrophicus str. PA1 5, Gluconacetobacter diazotrophicus strain PA1 5
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