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Pmen_0142 Pmen_0142 Pmen_0143 Pmen_0143 Pmen_0144 Pmen_0144 Pmen_0145 Pmen_0145 Pmen_0147 Pmen_0147 Pmen_0148 Pmen_0148 Pmen_0149 Pmen_0149 cyoE cyoE Pmen_0151 Pmen_0151 Pmen_0903 Pmen_0903 Pmen_0904 Pmen_0904 Pmen_0905 Pmen_0905 Pmen_1494 Pmen_1494 Pmen_1512 Pmen_1512 Pmen_2266 Pmen_2266 Pmen_2267 Pmen_2267 nuoA nuoA nuoB nuoB nuoC nuoC Pmen_2415 Pmen_2415 Pmen_2416 Pmen_2416 Pmen_2417 Pmen_2417 nuoH nuoH nuoI nuoI Pmen_2420 Pmen_2420 nuoK nuoK Pmen_2422 Pmen_2422 Pmen_2423 Pmen_2423 nuoN nuoN Pmen_2984 Pmen_2984 Pmen_3812 Pmen_3812 Pmen_4192 Pmen_4192 Pmen_4357 Pmen_4357
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:
Pmen_0142Cytochrome 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). (374 aa)
Pmen_0143Cytochrome-c oxidase; 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. (527 aa)
Pmen_0144PFAM: cytochrome c oxidase assembly protein CtaG/Cox11. (182 aa)
Pmen_0145PFAM: cytochrome c oxidase, subunit III. (298 aa)
Pmen_0147Conserved hypothetical protein. (243 aa)
Pmen_0148Hypothetical protein. (193 aa)
Pmen_0149PFAM: cytochrome oxidase assembly. (345 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. (299 aa)
Pmen_0151Electron transport protein SCO1/SenC; PFAM: alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen; electron transport protein SCO1/SenC. (210 aa)
Pmen_0903Ubiquinol-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)
Pmen_0904Cytochrome b/b6, N-terminal domain protein; 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. (403 aa)
Pmen_0905Cytochrome c1-like protein. (259 aa)
Pmen_1494PFAM: alpha/beta hydrolase fold. (326 aa)
Pmen_1512Lysophospholipase-like protein. (481 aa)
Pmen_2266TIGRFAM: cytochrome c, monohaem; PFAM: cytochrome c oxidase, subunit II. (336 aa)
Pmen_2267PFAM: cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family. (843 aa)
nuoANADH dehydrogenase 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)
nuoBNADH dehydrogenase 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)
nuoCNADH dehydrogenase subunit D / NADH dehydrogenase subunit 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (593 aa)
Pmen_2415TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone), 24 kDa subunit. (170 aa)
Pmen_2416NADH dehydrogenase 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)
Pmen_2417NADH dehydrogenase 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)
nuoHNADH dehydrogenase 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)
nuoINADH dehydrogenase 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)
Pmen_2420NADH dehydrogenase 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. (169 aa)
nuoKNADH dehydrogenase 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)
Pmen_2422TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone oxidoreductase (complex I), chain 5/L domain protein; NADH/Ubiquinone/plastoquinone (complex I). (616 aa)
Pmen_2423TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (509 aa)
nuoNNADH dehydrogenase 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. (494 aa)
Pmen_2984PFAM: alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen; Redoxin domain protein. (152 aa)
Pmen_3812PFAM: NAD-dependent epimerase/dehydratase. (213 aa)
Pmen_4192PFAM: 4Fe-4S ferredoxin, iron-sulfur binding domain protein. (83 aa)
Pmen_4357PFAM: Tannase and feruloyl esterase. (570 aa)
Your Current Organism:
Pseudomonas mendocina ymp
NCBI taxonomy Id: 399739
Other names: P. mendocina ymp, Pseudomonas mendocina str. ymp, Pseudomonas mendocina strain ymp
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