STRINGSTRING
dgk dgk BAG42728.1 BAG42728.1 fdsD fdsD fdhA fdhA BAG42829.1 BAG42829.1 fdhC fdhC BAG43035.1 BAG43035.1 BAG43070.1 BAG43070.1 BAG43115.1 BAG43115.1 BAG43117.1 BAG43117.1 cyoD cyoD cyoC cyoC cyoB cyoB cyoA cyoA nuoM nuoM nuoN nuoN nuoM-2 nuoM-2 nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoD nuoD nuoC nuoC nuoB nuoB nuoA nuoA BAG44639.1 BAG44639.1 cyoE cyoE cox1 cox1 BAG44680.1 BAG44680.1 BAG44681.1 BAG44681.1 coxC coxC cox1-2 cox1-2 coxA coxA coxB coxB cyt1 cyt1 cytB cytB rip1 rip1 BAG45150.1 BAG45150.1 BAG45328.1 BAG45328.1 cccA-3 cccA-3 nirK nirK BAG46396.1 BAG46396.1 BAG46961.1 BAG46961.1 estC estC BAG47362.1 BAG47362.1 ndhF ndhF BAG47499.1 BAG47499.1 coxB-2 coxB-2 coxA-2 coxA-2 asoB asoB coxB-3 coxB-3 cyoB-2 cyoB-2
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:
dgkCOG1428: Deoxynucleoside kinases, Ralstonia solanacearum; KEGG, K00904. (228 aa)
BAG42728.1Lysophospholipase-like protein; COG2267: Lysophospholipase, Ralstonia solanacearum. (325 aa)
fdsDFormate dehydrogenase delta subunit; KEGG, K00126. (83 aa)
fdhAFormate dehydrogenase alpha subunit; COG3383: Uncharacterized anaerobic dehydrogenase, Sinorhizobium meliloti; KEGG, K00123. (983 aa)
BAG42829.1COG1894: NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit, Sinorhizobium meliloti; KEGG, K05903. (525 aa)
fdhCFormate dehydrogenase gamma subunit; COG1905: NADH:ubiquinone oxidoreductase 24 kD subunit, Sinorhizobium meliloti; KEGG, K00127. (166 aa)
BAG43035.1Conserved hypothetical protein. (147 aa)
BAG43070.1COG0702: Predicted nucleoside-diphosphate-sugar epimerases, Listeria innocua. (209 aa)
BAG43115.1Lysophospholipase-like protein; COG2267: Lysophospholipase, Ralstonia solanacearum; KEGG, K07024. (325 aa)
BAG43117.1Hypothetical protein; COG0702: Predicted nucleoside-diphosphate-sugar epimerases, Ralstonia solanacearum. (209 aa)
cyoDCOG3125: Heme/copper-type cytochrome/quinol oxidase, subunit 4, Ralstonia solanacearum; CyoD protein; KEGG, K02300. (110 aa)
cyoCCOG1845: Heme/copper-type cytochrome/quinol oxidase, subunit 3, Pseudomonas aeruginosa; KEGG, K02299. (202 aa)
cyoBCOG0843: Heme/copper-type cytochrome/quinol oxidases, subunit 1, Ralstonia solanacearum; KEGG, K02298; Belongs to the heme-copper respiratory oxidase family. (668 aa)
cyoACOG1622: Heme/copper-type cytochrome/quinol oxidases, subunit 2, Ralstonia solanacearum; KEGG, K02297. (295 aa)
nuoMCOG1008: NADH:ubiquinone oxidoreductase subunit 4 (chain M), Ralstonia solanacearum; KEGG, K00342. (509 aa)
nuoNNADH dehydrogenase I 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. (491 aa)
nuoM-2COG1008: NADH:ubiquinone oxidoreductase subunit 4 (chain M), Ralstonia solanacearum; KEGG, K00342. (496 aa)
nuoLCOG1009: NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit, Ralstonia solanacearum; KEGG, K00341. (684 aa)
nuoKNADH dehydrogenase I chain 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. (101 aa)
nuoJNADH 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. (216 aa)
nuoINADH dehydrogenase I chain 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)
nuoHNADH 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. (355 aa)
nuoGNADH dehydrogenase I 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. (776 aa)
nuoFNADH dehydrogenase I 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. (436 aa)
nuoECOG1905: NADH:ubiquinone oxidoreductase 24 kD subunit, Ralstonia solanacearum; KEGG, K00334. (161 aa)
nuoDNADH dehydrogenase I chain 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. (417 aa)
nuoCNADH dehydrogenase I 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. (200 aa)
nuoBNADH dehydrogenase I 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). (173 aa)
nuoANADH dehydrogenase I 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. (119 aa)
BAG44639.1COG1145: Ferredoxin, Ralstonia solanacearum. (87 aa)
cyoEProtoheme 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. (300 aa)
cox1COG1612: Uncharacterized protein required for cytochrome oxidase assembly, Ralstonia solanacearum; KEGG, K02259. (370 aa)
BAG44680.1Putative membrane protein. (210 aa)
BAG44681.1Putative membrane protein; COG3346: Uncharacterized conserved protein, Ralstonia solanacearum. (236 aa)
coxCCOG1845: Heme/copper-type cytochrome/quinol oxidase, subunit 3, Ralstonia solanacearum; KEGG, K02276. (285 aa)
cox1-2COG3175: Cytochrome oxidase assembly factor, Ralstonia solanacearum; KEGG, K02258. (203 aa)
coxACytochrome 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. (535 aa)
coxBCytochrome 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). (532 aa)
cyt1COG2857: Cytochrome c1, Ralstonia solanacearum; KEGG, K00413. (252 aa)
cytBUbiquinol-cytochrome c reductase cytochrome b 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. (459 aa)
rip1Ubiquinol-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. (206 aa)
BAG45150.1COG0702: Predicted nucleoside-diphosphate-sugar epimerases, Mesorhizobium loti. (293 aa)
BAG45328.1COG0446: Uncharacterized NAD(FAD)-dependent dehydrogenases, Mesorhizobium loti. (115 aa)
cccA-3COG2010: Cytochrome c, mono- and diheme variants, Ralstonia solanacearum. (280 aa)
nirKNO-forming nitrite reductase; KEGG, K00368. (166 aa)
BAG46396.1Fusion protein of NAD-dependent epimerase/dehydratase and GCN5-related N-acetyltransferase; COG0702: Predicted nucleoside-diphosphate-sugar epimerases, Mesorhizobium loti. (402 aa)
BAG46961.1COG0702: Predicted nucleoside-diphosphate-sugar epimerases, Mesorhizobium loti. (288 aa)
estCPutative esterase. (294 aa)
BAG47362.1Uncharacterized NAD(FAD)-dependent dehydrogenase. (99 aa)
ndhFCOG1009: NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit, Vibrio cholerae; KEGG, K05577. (532 aa)
BAG47499.1COG0657: Esterase/lipase, Caulobacter vibrioides. (319 aa)
coxB-2COG1622: Heme/copper-type cytochrome/quinol oxidases, subunit 2, Bacillus halodurans; KEGG, K02275. (195 aa)
coxA-2COG0843: Heme/copper-type cytochrome/quinol oxidases, subunit 1, Bacillus halodurans; KEGG, K02274. (541 aa)
asoBArsenite oxidase small subunit; COG0723: Rieske Fe-S protein, Aeropyrum pernix; KEGG, K08355. (172 aa)
coxB-3COG1622: Heme/copper-type cytochrome/quinol oxidases, subunit 2, Sinorhizobium meliloti; KEGG, K02275. (339 aa)
cyoB-2COG0843: Heme/copper-type cytochrome/quinol oxidases, subunit 1, Mesorhizobium loti; CyoB2 protein. (878 aa)
Your Current Organism:
Burkholderia multivorans
NCBI taxonomy Id: 395019
Other names: B. multivorans ATCC 17616, Burkholderia multivorans ATCC 17616, Burkholderia multivorans str. ATCC 17616, Burkholderia multivorans strain ATCC 17616
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.