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Desaf_1085 Desaf_1085 Desaf_0581 Desaf_0581 Desaf_1616 Desaf_1616 Desaf_0580 Desaf_0580 Desaf_2186 Desaf_2186 nuoB nuoB
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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
Desaf_1085PFAM: 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; KEGG: dsa:Desal_3826 4Fe-4S ferredoxin iron-sulfur binding domain protein. (82 aa)
Desaf_0581NADH dehydrogenase (quinone); KEGG: dsa:Desal_3237 NADH-ubiquinone oxidoreductase chain 49kDa; PFAM: NADH-quinone oxidoreductase, subunit D; Nickel-dependent hydrogenase, large subunit. (358 aa)
Desaf_1616TIGRFAM: NADH-quinone oxidoreductase, chain M; KEGG: proton-translocating NADH-quinone oxidoreductase subunit M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase. (523 aa)
Desaf_0580PFAM: 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; KEGG: hypothetical protein. (140 aa)
Desaf_2186TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate/ketoisovalerate oxidoreductase; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding protein. (1232 aa)
nuoBNAD(P)H-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. (179 aa)
Your Current Organism:
Desulfocurvibacter africanus
NCBI taxonomy Id: 690850
Other names: D. africanus subsp. africanus str. Walvis Bay, Desulfocurvibacter africanus str. Walvis Bay, Desulfocurvibacter africanus subsp. africanus str. Walvis Bay, Desulfovibrio africanus ATCC 19997, Desulfovibrio africanus str. Walvis Bay, Desulfovibrio africanus strain Walvis Bay
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