STRINGSTRING
coxB coxB coxA coxA coxG coxG coxC coxC BAN45787.1 BAN45787.1 BAN45789.1 BAN45789.1 cyoE cyoE BAN45988.1 BAN45988.1 BAN45996.1 BAN45996.1 BAN45997.1 BAN45997.1 BAN46227.1 BAN46227.1 oprG oprG dmpR dmpR ccoN2 ccoN2 BAN46627.1 BAN46627.1 BAN46628.1 BAN46628.1 petA petA petB petB petC petC BAN47049.1 BAN47049.1 BAN47134.1 BAN47134.1 BAN47135.1 BAN47135.1 BAN47136.1 BAN47136.1 BAN47192.1 BAN47192.1 BAN48048.1 BAN48048.1 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 BAN48273.1 BAN48273.1 BAN48274.1 BAN48274.1 coxM coxM coxN coxN coxO coxO coxP coxP coxQ coxQ BAN48440.1 BAN48440.1 BAN48441.1 BAN48441.1 BAN48498.1 BAN48498.1 coxB-2 coxB-2 coxA-2 coxA-2 BAN48724.1 BAN48724.1 BAN48854.1 BAN48854.1 BAN48855.1 BAN48855.1 BAN48856.1 BAN48856.1 BAN48896.1 BAN48896.1 BAN48897.1 BAN48897.1 BAN48898.1 BAN48898.1 BAN48899.1 BAN48899.1 BAN48900.1 BAN48900.1 BAN48989.1 BAN48989.1 BAN49015.1 BAN49015.1 BAN49016.1 BAN49016.1 BAN49293.1 BAN49293.1 BAN49294.1 BAN49294.1 ccoN1 ccoN1 ccoO1 ccoO1 ccoQ2 ccoQ2 ccoP1 ccoP1 ccoN2-2 ccoN2-2 ccoO2 ccoO2 ccoQ2-2 ccoQ2-2 ccoP2 ccoP2 BAN49574.1 BAN49574.1 BAN49575.1 BAN49575.1 BAN49576.1 BAN49576.1 ccoS ccoS BAN49578.1 BAN49578.1 BAN49789.1 BAN49789.1 BAN50895.1 BAN50895.1 BAN50896.1 BAN50896.1 BAN50897.1 BAN50897.1
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:
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). (367 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. (540 aa)
coxGCytochrome c oxidase assembly protein. (183 aa)
coxCCytochrome c oxidase subunit III. (295 aa)
BAN45787.1Hypothetical protein. (242 aa)
BAN45789.1Hypothetical protein. (361 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. (301 aa)
BAN45988.1Putative 4Fe-4S ferredoxin. (83 aa)
BAN45996.1Hypothetical protein. (493 aa)
BAN45997.1M16 family peptidase. (441 aa)
BAN46227.1Hypothetical protein. (290 aa)
oprGOuter membrane protein OprG. (223 aa)
dmpRRegulatory protein DmpR. (567 aa)
ccoN2Cbb3-type cytochrome c oxidase subunit CcoN2; Belongs to the heme-copper respiratory oxidase family. (491 aa)
BAN46627.1Hypothetical protein. (81 aa)
BAN46628.1Hypothetical protein. (92 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. (197 aa)
petBUbiquinol--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. (404 aa)
petCUbiquinol--cytochrome c reductase cytochrome c1 subunit. (260 aa)
BAN47049.1Hypothetical protein. (495 aa)
BAN47134.1Cytochrome c family protein. (323 aa)
BAN47135.1Hypothetical protein. (909 aa)
BAN47136.1Hypothetical protein. (55 aa)
BAN47192.1Hypothetical protein. (528 aa)
BAN48048.1Hypothetical protein. (125 aa)
nuoNNADH-quinone oxidoreductase 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. (486 aa)
nuoMNADH-quinone oxidoreductase subunit M. (508 aa)
nuoLNADH-quinone oxidoreductase subunit L. (615 aa)
nuoKNADH-quinone oxidoreductase 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. (102 aa)
nuoJNADH-quinone oxidoreductase 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. (166 aa)
nuoINADH-quinone oxidoreductase 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. (182 aa)
nuoHNADH-quinone oxidoreductase 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. (330 aa)
nuoGNADH-quinone oxidoreductase subunit 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. (902 aa)
nuoFNADH-quinone oxidoreductase 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. (448 aa)
nuoENADH-quinone oxidoreductase subunit E. (164 aa)
nuoCNADH-quinone oxidoreductase subunit 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 C-terminal section; belongs to the complex I 49 kDa subunit family. (593 aa)
nuoBNADH-quinone oxidoreductase 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. (225 aa)
nuoANADH-quinone oxidoreductase 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. (137 aa)
BAN48273.1Hypothetical protein. (517 aa)
BAN48274.1Hypothetical protein. (207 aa)
coxMCytochrome c oxidase subunit II CoxM. (479 aa)
coxNCytochrome c oxidase subunit I CoxN; 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. (589 aa)
coxOCytochrome c oxidase subunit III CoxO. (224 aa)
coxPCytochrome c oxidase subunit III CoxP. (222 aa)
coxQPutative cytochrome oxidase subunit IV. (105 aa)
BAN48440.1Putative cytochrome c. (197 aa)
BAN48441.1Cytochrome c family protein. (349 aa)
BAN48498.1Hypothetical protein. (249 aa)
coxB-2Cytochrome c oxidase subunit II. (278 aa)
coxA-2Cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (843 aa)
BAN48724.1Cytochrome c. (123 aa)
BAN48854.1Hypothetical protein. (744 aa)
BAN48855.1Cytochrome c family protein. (319 aa)
BAN48856.1Hypothetical protein. (164 aa)
BAN48896.1Hypothetical protein. (184 aa)
BAN48897.1Hypothetical protein. (593 aa)
BAN48898.1Hypothetical protein. (213 aa)
BAN48899.1Hypothetical protein. (60 aa)
BAN48900.1Hypothetical protein. (196 aa)
BAN48989.1Hypothetical protein. (130 aa)
BAN49015.1Hypothetical protein. (635 aa)
BAN49016.1Hypothetical protein. (222 aa)
BAN49293.1Hypothetical protein. (202 aa)
BAN49294.1Hypothetical protein. (620 aa)
ccoN1Cbb3-type cytochrome c oxidase subunit CcoN1; Belongs to the heme-copper respiratory oxidase family. (474 aa)
ccoO1Cbb3-type cytochrome c oxidase subunit CcoO1. (203 aa)
ccoQ2Cbb3-type cytochrome c oxidase subunit CcoQ2. (55 aa)
ccoP1Cbb3-type cytochrome c oxidase subunit CcoP1; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (311 aa)
ccoN2-2Cbb3-type cytochrome c oxidase subunit CcoN2; Belongs to the heme-copper respiratory oxidase family. (450 aa)
ccoO2Cbb3-type cytochrome c oxidase subunit CcoO2. (203 aa)
ccoQ2-2Cbb3-type cytochrome c oxidase subunit CcoQ2. (62 aa)
ccoP2Cbb3-type cytochrome c oxidase subunit CcoP2; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (324 aa)
BAN49574.1Putative 4Fe-4S ferredoxin. (471 aa)
BAN49575.1Hypothetical protein. (166 aa)
BAN49576.1Cation-transporting P-type ATPase. (799 aa)
ccoSCbb3-type cytochrome c oxidase maturation protein. (73 aa)
BAN49578.1Hypothetical protein. (241 aa)
BAN49789.1Hypothetical protein. (3429 aa)
BAN50895.1Hypothetical protein. (369 aa)
BAN50896.1Hypothetical protein. (411 aa)
BAN50897.1Hypothetical protein. (765 aa)
Your Current Organism:
Pseudomonas resinovorans NBRC106553
NCBI taxonomy Id: 1245471
Other names: P. resinovorans NBRC 106553, Pseudomonas resinovorans NBRC 106553
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