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SVI_0004 SVI_0004 coxN coxN SVI_0006 SVI_0006 SVI_0007 SVI_0007 cytcB cytcB SVI_0181 SVI_0181 cyoE-1 cyoE-1 SVI_0183 SVI_0183 SVI_0184 SVI_0184 SVI_0185 SVI_0185 SVI_0188 SVI_0188 coxG coxG SVI_0190 SVI_0190 SVI_0191 SVI_0191 SVI_0236 SVI_0236 SVI_0237 SVI_0237 SVI_0386 SVI_0386 petA petA petB petB petC petC SVI_0566 SVI_0566 SVI_0567 SVI_0567 nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoCD nuoCD nuoB nuoB nuoA nuoA SVI_3153 SVI_3153 SVI_3232 SVI_3232 SVI_3550 SVI_3550 cytcA cytcA cyoE-2 cyoE-2 cyoD cyoD cyoC cyoC cyoB cyoB cyoA cyoA
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:
SVI_0004Cytochrome c oxidase, subunit II. (492 aa)
coxNAlternative cytochrome c oxidase polypeptide I; Belongs to the heme-copper respiratory oxidase family. (604 aa)
SVI_0006Cytochrome c oxidase subunit III. (231 aa)
SVI_0007Cytochrome c oxidase subunit III. (230 aa)
cytcBSoluble cytochrome cB. (206 aa)
SVI_0181SCO1/SenC family protein. (230 aa)
cyoE-1Protoheme 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. (304 aa)
SVI_0183Cytochrome oxidase assembly protein, putative. (327 aa)
SVI_0184Conserved hypothetical protein. (181 aa)
SVI_0185Conserved hypothetical protein. (278 aa)
SVI_0188Cytochrome c oxidase subunit III. (291 aa)
coxGCytochrome c oxidase assembly protein coxG. (189 aa)
SVI_0190Cytochrome 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. (531 aa)
SVI_0191Cytochrome 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). (373 aa)
SVI_0236Peptidase, M16 family. (442 aa)
SVI_0237Peptidase, M16 family. (481 aa)
SVI_0386Conserved hypothetical protein. (218 aa)
petAUbiquinol-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. (196 aa)
petBUbiquinol-cytochrome c reductase, 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. (404 aa)
petCUbiquinol-cytochrome c reductase, cytochrome c1. (232 aa)
SVI_0566Peptidase M16 inactive domain family. (525 aa)
SVI_0567Peptidase, M16 family. (479 aa)
nuoNNADH dehydrogenase I, N subunit; 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. (460 aa)
nuoMNADH dehydrogenase I, M subunit. (525 aa)
nuoLNADH dehydrogenase I, L subunit. (624 aa)
nuoKNADH dehydrogenase I, K subunit; 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)
nuoJNADH dehydrogenase I, J subunit; 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. (294 aa)
nuoINADH dehydrogenase I, I subunit; 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)
nuoHNADH dehydrogenase I, H subunit; 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. (318 aa)
nuoGNADH dehydrogenase I, G subunit; 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. (976 aa)
nuoFNADH dehydrogenase I, F subunit; 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. (456 aa)
nuoENADH dehydrogenase I, E subunit. (228 aa)
nuoCDNADH dehydrogenase I, C/D subunits; 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. (596 aa)
nuoBNADH dehydrogenase I, B subunit; 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. (219 aa)
nuoANADH dehydrogenase I, A subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (123 aa)
SVI_3153Peptidase, M16 family. (944 aa)
SVI_3232Ferredoxin, 4Fe-4S. (84 aa)
SVI_3550Hydrolase, alpha/beta fold family. (268 aa)
cytcASoluble cytochrome cA. (107 aa)
cyoE-2Protoheme 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. (299 aa)
cyoDCytochrome o ubiquinol oxidase, subunit IV. (111 aa)
cyoCCytochrome o ubiquinol oxidase, subunit III. (207 aa)
cyoBCytochrome o ubiquinol oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family. (661 aa)
cyoACytochrome o ubiquinol oxidase, subunit II. (300 aa)
Your Current Organism:
Shewanella violacea
NCBI taxonomy Id: 637905
Other names: S. violacea DSS12, Shewanella violacea DSS12, Shewanella violacea JCM 10179, Shewanella violacea str. DSS12, Shewanella violacea strain DSS12
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