STRINGSTRING
cyoE cyoE cyoD cyoD cyoC cyoC cyoB cyoB cyoA cyoA cydA cydA cydB cydB cydC cydC cydD cydD hyaA hyaA hyaB hyaB hyaC hyaC hyaD hyaD hyaE hyaE hyaF hyaF appC appC appB appB ndh ndh ydbK ydbK nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoC nuoC nuoB nuoB nuoA nuoA hyfA hyfA hyfB hyfB hyfC hyfC hyfD hyfD hyfE hyfE hyfF hyfF hyfG hyfG hyfH hyfH hyfI hyfI hyfJ hyfJ hyfR hyfR focB focB yfhL yfhL hypF hypF hydN hydN hycI hycI hycH hycH hycG hycG hycF hycF hycE hycE hycD hycD hycC hycC hycB hycB hycA hycA hypA hypA hypB hypB hypC hypC hypD hypD hypE hypE fhlA fhlA CAR14223.1 CAR14223.1 ygfS ygfS hybG hybG hybF hybF hybE hybE hybD hybD hybC hybC hybB hybB hybA hybA hybO hybO CAR14639.1 CAR14639.1 yghW yghW yhjA yhjA fdhF fdhF
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:
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. (296 aa)
cyoDCytochrome o ubiquinol oxidase subunit IV; Function experimentally demonstrated in the studied species; carrier. (109 aa)
cyoCCytochrome o ubiquinol oxidase subunit III; Function experimentally demonstrated in the studied species; carrier. (204 aa)
cyoBCytochrome o ubiquinol oxidase subunit I; Function experimentally demonstrated in the studied species; carrier; Belongs to the heme-copper respiratory oxidase family. (663 aa)
cyoACytochrome o ubiquinol oxidase subunit II; Function experimentally demonstrated in the studied species; carrier. (315 aa)
cydACytochrome d terminal oxidase, subunit I; Function experimentally demonstrated in the studied species; carrier. (522 aa)
cydBCytochrome d terminal oxidase, subunit II; Function experimentally demonstrated in the studied species; carrier. (379 aa)
cydCFused cysteine transporter subunits of ABC superfamily: membrane component; Function experimentally demonstrated in the studied species; transporter. (573 aa)
cydDFused cysteine transporter subunits of ABC superfamily: membrane component; Function experimentally demonstrated in the studied species; transporter. (588 aa)
hyaAHydrogenase 1, small subunit; Function experimentally demonstrated in the studied species; enzyme. (372 aa)
hyaBHydrogenase 1, large subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. (597 aa)
hyaCHydrogenase 1, b-type cytochrome subunit; Function experimentally demonstrated in the studied species; carrier. (235 aa)
hyaDProtein involved in processing of HyaA and HyaB proteins; Function experimentally demonstrated in the studied species; factor. (195 aa)
hyaEProtein involved in processing of HyaA and HyaB proteins; Function experimentally demonstrated in the studied species; factor. (132 aa)
hyaFProtein involved in nickel incorporation into hydrogenase-1 proteins; Function experimentally demonstrated in the studied species; factor. (285 aa)
appCCytochrome bd-II oxidase, subunit I; Function experimentally demonstrated in the studied species; carrier. (514 aa)
appBCytochrome bd-II oxidase, subunit II; Function experimentally demonstrated in the studied species; carrier. (378 aa)
ndhRespiratory NADH dehydrogenase 2/cupric reductase; Function experimentally demonstrated in the studied species; enzyme. (434 aa)
ydbKPutative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (1174 aa)
nuoNNADH:ubiquinone oxidoreductase, membrane 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. (425 aa)
nuoMNADH:ubiquinone oxidoreductase, membrane subunit M; Function experimentally demonstrated in the studied species; membrane component. (509 aa)
nuoLNADH:ubiquinone oxidoreductase, membrane subunit L; Function experimentally demonstrated in the studied species; membrane component. (613 aa)
nuoKNADH:ubiquinone oxidoreductase, membrane 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)
nuoJNADH:ubiquinone oxidoreductase, membrane 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. (184 aa)
nuoINADH:ubiquinone oxidoreductase, 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. (180 aa)
nuoHNADH:ubiquinone oxidoreductase, membrane 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. (325 aa)
nuoGNADH:ubiquinone 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. (910 aa)
nuoFNADH:ubiquinone 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. (445 aa)
nuoENADH:ubiquinone oxidoreductase, chain E; Function experimentally demonstrated in the studied species; carrier. (166 aa)
nuoCNADH:ubiquinone 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. (600 aa)
nuoBNADH:ubiquinone 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. (220 aa)
nuoANADH:ubiquinone oxidoreductase, membrane 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. (147 aa)
hyfAHydrogenase 4, 4Fe-4S subunit; Function experimentally demonstrated in the studied species; carrier. (205 aa)
hyfBHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (672 aa)
hyfCHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (315 aa)
hyfDHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (479 aa)
hyfEHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (216 aa)
hyfFHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (526 aa)
hyfGHydrogenase 4, subunit; Function experimentally demonstrated in the studied species; carrier. (555 aa)
hyfHHydrogenase 4, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (181 aa)
hyfIHydrogenase 4, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (252 aa)
hyfJPutative processing element hydrogenase 4; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor. (137 aa)
hyfRDNA-binding transcriptional activator, formate sensing; Function experimentally demonstrated in the studied species; regulator. (670 aa)
focBPutative formate transporter; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. (282 aa)
yfhLFerredoxin (4Fe-4S cluster-containing protein) (fdx-like); Function of strongly homologous gene; carrier. (86 aa)
hypFCarbamoyl phosphate phosphatase and maturation protein for [NiFe] hydrogenases; Involved in the maturation of [NiFe] hydrogenases. Along with HypE, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase using carbamoylphosphate as a substrate and transferring the carboxamido moiety in an ATP-dependent reaction to the thiolate of the C-terminal cysteine of HypE yielding a protein-S-carboxamide. (770 aa)
hydNFormate dehydrogenase-H, [4Fe-4S] ferredoxin subunit; Function experimentally demonstrated in the studied species; carrier. (175 aa)
hycIProtease involved in processing C-terminal end of HycE; Function experimentally demonstrated in the studied species; enzyme. (156 aa)
hycHProtein required for maturation of hydrogenase 3; Function experimentally demonstrated in the studied species; factor. (136 aa)
hycGHydrogenase 3 and formate hydrogenase complex, HycG subunit; Function experimentally demonstrated in the studied species; enzyme. (255 aa)
hycFFormate hydrogenlyase complex iron-sulfur protein; Function experimentally demonstrated in the studied species; carrier. (180 aa)
hycEHydrogenase 3, large subunit; Function experimentally demonstrated in the studied species; enzyme. (569 aa)
hycDHydrogenase 3, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (307 aa)
hycCHydrogenase 3, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (608 aa)
hycBHydrogenase 3, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (203 aa)
hycARegulator of the transcriptional regulator FhlA; Function experimentally demonstrated in the studied species; regulator. (153 aa)
hypAProtein involved in nickel insertion into hydrogenases 3; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. (116 aa)
hypBGTP hydrolase involved in nickel liganding into hydrogenases; Function experimentally demonstrated in the studied species; enzyme. (290 aa)
hypCProtein required for maturation of hydrogenases 1 and 3; Function experimentally demonstrated in the studied species; factor. (90 aa)
hypDProtein required for maturation of hydrogenases; Function experimentally demonstrated in the studied species; factor; Belongs to the HypD family. (373 aa)
hypECarbamoyl phosphate phosphatase, hydrogenase 3 maturation protein; Function experimentally demonstrated in the studied species; enzyme. (322 aa)
fhlADNA-binding transcriptional activator; Function experimentally demonstrated in the studied species; regulator. (692 aa)
CAR14223.1Putative molybdenum-pterin-binding-protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (155 aa)
ygfSPutative oxidoreductase, 4Fe-4S ferredoxin-type subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (162 aa)
hybGHydrogenase 2 accessory protein; Function experimentally demonstrated in the studied species; putative factor. (82 aa)
hybFProtein involved with the maturation of hydrogenases 1 and 2; Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. (113 aa)
hybEHydrogenase 2-specific chaperone; Function experimentally demonstrated in the studied species; factor. (162 aa)
hybDMaturation element for hydrogenase 2; Function of strongly homologous gene; factor. (164 aa)
hybCHydrogenase 2, large subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. (567 aa)
hybBFunction of strongly homologous gene; carrier. (392 aa)
hybAHydrogenase 2 4Fe-4S ferredoxin-type component; Function experimentally demonstrated in the studied species; putative carrier. (328 aa)
hybOHydrogenase 2, small subunit; Function experimentally demonstrated in the studied species; enzyme. (372 aa)
CAR14639.1Conserved hypothetical protein; Doubtful CDS. (61 aa)
yghWConserved hypothetical protein; Homologs of previously reported genes of unknown function. (95 aa)
yhjACytochrome C peroxidase (cpp-like); Function experimentally demonstrated in the studied species; enzyme. (465 aa)
fdhFFormate dehydrogenase-H, selenopolypeptide subunit; Function experimentally demonstrated in the studied genus; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (715 aa)
Your Current Organism:
Escherichia coli UMN026
NCBI taxonomy Id: 585056
Other names: E. coli UMN026
Server load: low (20%) [HD]