STRINGSTRING
hyfA hyfA fdnH fdnH nuoI_1 nuoI_1 lutA lutA glpC_1 glpC_1 frdB_2 frdB_2 fdxA_1 fdxA_1 queG queG fdxA_2 fdxA_2 psaC psaC nuoI_2 nuoI_2
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:
hyfAHydrogenase-4 component A. (920 aa)
fdnHFormate dehydrogenase, nitrate-inducible, iron-sulfur subunit. (322 aa)
nuoI_1NADH-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. (189 aa)
lutALactate utilization protein A. (482 aa)
glpC_1Anaerobic glycerol-3-phosphate dehydrogenase subunit C. (1014 aa)
frdB_2Fumarate reductase iron-sulfur subunit. (250 aa)
fdxA_1Ferredoxin 1; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (103 aa)
queGEpoxyqueuosine reductase. (442 aa)
fdxA_2Ferredoxin-1; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (92 aa)
psaCPhotosystem I iron-sulfur center. (67 aa)
nuoI_2NADH-quinone oxidoreductase subunit I. (191 aa)
Your Current Organism:
Gemmata sp. SHPL17
NCBI taxonomy Id: 1630693
Other names: G. sp. SH-PL17, Gemmata sp. SH-PL17
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