STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ANS85098.1Anaerobic dimethyl sulfoxide reductase chain; Electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. Contains 3 4Fe-4S ferredoxin-type domains. (205 aa)    
Predicted Functional Partners:
dmsA
Dimethylsulfoxide reductase; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E. coli to grow anaerobically on DMSO as respiratory oxidant; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family; Contains 1 4Fe-4S Mo/W bis-MGD-type domain; KEGG: yel:LC20_03833 anaerobic dimethyl sulfoxide reductase subunit A.
 0.998
ANS85099.1
Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. DmsC anchors the DmsAB dimer to the membrane and stabilizes it. To E. coli YnfH.
 
 
 0.994
torA
Trimethylamine-N-oxide reductase (cytochrome c); Reduces trimethylamine-N-oxide (TMAO) into trimethylamin; an anaerobic reaction coupled to energy-yielding reactions; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family; KEGG: vch:VC1692 trimethylamine-N-oxide reductase (cytochrome c).
 
 
 0.921
ANS85473.1
Formate dehydrogenase; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family; Contains 1 4Fe-4S Mo/W bis-MGD-type domain; KEGG: vcf:IR04_12795 formate dehydrogenase major subunit.
 
 0.858
ANS85471.1
Hypothetical protein.
 
 
 0.844
napA
Nitrate reductase; Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
 
 
 0.833
ANS85096.1
Putative Tat proofreading chaperone DmsD; Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein; Belongs to the TorD/DmsD family. DmsD subfamily.
 
  
 0.828
fdoG
Formate dehydrogenase; Contains 4 4Fe-4S ferredoxin-type domains; KEGG: vvu:VV2_1360 formate dehydrogenase major subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
  
 0.780
coxB
Cytochrome-c oxidase; 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).
  
 
 0.744
tuf
Elongation factor Tu-A; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.
  
 
 0.720
Your Current Organism:
Vibrio scophthalmi
NCBI taxonomy Id: 45658
Other names: CAIM 75, CECT 4638, CIP 105211, LMG 19158, LMG:19158, V. scophthalmi, strain A089
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