Known metabolic pathways, protein complexes, signal transduction pathways, etc ... from curated databases.
Genes that are sometimes fused into single open reading frames.
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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.
colored nodes: query proteins and first shell of interactors
white nodes: second shell of interactors
empty nodes: proteins of unknown 3D structure
filled nodes: some 3D structure is known or predicted
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 each other.
from curated databases
Ferredoxin, 4Fe-4S, putative; Identified by similarity to SP-P33393; match to protein family HMM PF00037; match to protein family HMM PF02754 (439 aa)
Predicted Functional Partners:
Uncharacterized protein; Identified by Glimmer2; putative (408 aa)
annotation not available (219 aa)
Acidic cytochrome c3; Identified by similarity to SP-P94690 (126 aa)
Pyridine nucleotide-disulfide oxidoreductase; Identified by match to protein family HMM PF00070 (673 aa)
Hydrogenase, CooM subunit, putative; Identified by similarity to GP-1515466; match to protein family HMM PF00361 (1253 aa)
Oxidoreductase, FAD/iron-sulfur cluster-binding domain protein; Identified by match to protein family HMM PF00037; match to protein family HMM PF01565; match to protein family HMM PF02913 (941 aa)
Identified by match to protein family HMM PF00582; Belongs to the universal stress protein A family (308 aa)
Pyruvate synthase; Identified by similarity to GP-1770208; match to protein family HMM PF00037; match to protein family HMM PF01558; match to protein family HMM PF01855 (1215 aa)
Uncharacterized protein; Identified by Glimmer2; putative (51 aa)
Sulfite reductase, dissimilatory-type subunit alpha; Part of the complex that catalyzes the reduction of sulfite to sulfide. The alpha and beta subunits may have arisen by gene duplication. They both bind 2 iron-sulfur clusters, but the alpha subunit seems to be catalytically inactive, due to substitutions along the putative substrate access channel, and because it binds sirohydrochlorin (the dematallated form of siroheme) instead of siroheme (437 aa)
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882 Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough