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A7J50_3051 A7J50_3051 A7J50_0023 A7J50_0023 A7J50_0579 A7J50_0579 A7J50_0812 A7J50_0812 A7J50_1050 A7J50_1050 A7J50_2048 A7J50_2048 A7J50_2064 A7J50_2064 A7J50_2202 A7J50_2202 A7J50_2416 A7J50_2416 A7J50_2650 A7J50_2650 azoR-2 azoR-2 nuoB nuoB nuoC nuoC A7J50_3457 A7J50_3457 A7J50_3458 A7J50_3458 nuoH nuoH nuoI nuoI A7J50_3461 A7J50_3461 nuoK nuoK A7J50_3463 A7J50_3463 A7J50_3464 A7J50_3464 nuoN nuoN A7J50_3522 A7J50_3522 azoR-3 azoR-3 A7J50_4896 A7J50_4896 A7J50_4929 A7J50_4929 A7J50_5181 A7J50_5181 A7J50_5361 A7J50_5361 A7J50_5590 A7J50_5590 A7J50_5622 A7J50_5622 A7J50_3295 A7J50_3295 A7J50_3418 A7J50_3418 nuoA nuoA
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.
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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:
A7J50_3051Pfam:pfam03358 NADPH-dependent FMN reductase. (228 aa)
A7J50_0023Quinone oxidoreductase; Pfam:pfam00107 Zinc-binding dehydrogenase. (325 aa)
A7J50_0579Peptidase; Pfam:pfam13172 PepSY-associated TM helix. (460 aa)
A7J50_0812Flavodoxin; Pfam:pfam00258 Flavodoxin. (841 aa)
A7J50_1050Peptidase; Pfam:pfam13703 PepSY-associated TM helix. (524 aa)
A7J50_2048Peptidase; Pfam:pfam13703 PepSY-associated TM helix. (405 aa)
A7J50_2064FMN reductase; Pfam:pfam03358 NADPH-dependent FMN reductase. (187 aa)
A7J50_2202Ribosyldihydronicotinamide dehydrogenase; Pfam:pfam02525 Flavodoxin-like fold. (233 aa)
A7J50_2416ACP phosphodiesterase; Pfam:pfam03358 NADPH-dependent FMN reductase. (185 aa)
A7J50_2650NAD(P)H dehydrogenase; Pfam:pfam02525 Flavodoxin-like fold. (199 aa)
azoR-2FMN-dependent NADH-azoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (203 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. (224 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. (594 aa)
A7J50_3457NADH 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. (451 aa)
A7J50_3458NADH-quinone oxidoreductase; 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. (904 aa)
nuoHNADH:ubiquinone 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. (335 aa)
nuoINADH dehydrogenase; 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)
A7J50_3461NADH-quinone oxidoreductase, 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. (167 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)
A7J50_3463NADH:ubiquinone oxidoreductase subunit L; Pfam:pfam00361 NADH-Ubiquinone/plastoquinone (complex I), various chains. (617 aa)
A7J50_3464NADH:ubiquinone oxidoreductase subunit M; Pfam:pfam00361 NADH-Ubiquinone/plastoquinone (complex I), various chains. (510 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. (487 aa)
A7J50_3522Monovalent cation/H+ antiporter subunit D; Pfam:pfam00361 NADH-Ubiquinone/plastoquinone (complex I), various chains. (560 aa)
azoR-3FMN-dependent NADH-azoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (200 aa)
A7J50_4896Flavodoxin; Pfam:pfam00258 Flavodoxin. (151 aa)
A7J50_4929NADPH quinone reductase MdaB; Pfam:pfam02525 Flavodoxin-like fold. (196 aa)
A7J50_5181NAD(P)H dehydrogenase; Pfam:pfam02525 Flavodoxin-like fold. (214 aa)
A7J50_5361Peptidase; Pfam:pfam13703 PepSY-associated TM helix. (367 aa)
A7J50_5590Pfam:pfam03358 NADPH-dependent FMN reductase. (197 aa)
A7J50_5622NADPH:quinone oxidoreductase; Pfam:pfam00107 Zinc-binding dehydrogenase. (325 aa)
A7J50_3295Ferredoxin; Pfam:pfam13510 2Fe-2S iron-sulfur cluster binding domain. (96 aa)
A7J50_3418NAD(P)H quinone oxidoreductase; Pfam:pfam03358 NADPH-dependent FMN reductase; Belongs to the WrbA family. (204 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)
Your Current Organism:
Pseudomonas antarctica
NCBI taxonomy Id: 219572
Other names: CCUG 49625, DSM 15318, LMG 22709, LMG:22709, MTCC 4992, Pseudomonas antarctica Reddy et al. 2004, strain CMS 35
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