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
cyfCytochrome c-553; Natural electron acceptor for a formate dehydrogenase. (103 aa)    
Predicted Functional Partners:
hydA
Periplasmic [Fe] hydrogenase, large subunit; May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme.
    
   0.900
hydB
Periplasmic [Fe] hydrogenase, small subunit; May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme.
    
   0.900
DVU_1968
Oxidoreductase, putative.
   
 
 0.827
DVU_3212
Pyridine nucleotide-disulfide oxidoreductase; Identified by match to protein family HMM PF00070; match to protein family HMM PF02852.
   
 
 0.794
hmcA
High-molecular-weight cytochrome C; HMWC (high-molecular-weight cytochrome c), ORF2, ORF3, ORF4, ORF5 and ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates.
  
 
 
 0.784
qrcD
Molybdopterin oxidoreductase, transmembrane subunit, putative; Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration. Is likely essential for growth on H(2) or formate since the periplasmic hydrogenases and/or formate dehydrogenases act as primary electron donors for the Qrc complex. The QrcD subunit anchors the protein complex to the membrane and likely interacts with the quinone pool.
  
  
 0.740
DVU_3195
Lipoprotein, putative; Identified by similarity to OMNI:NTL01CJ01286.
  
   
 0.731
rdl
Identified by match to protein family HMM PF00301; Belongs to the rubredoxin family.
   
  
 0.639
qrcC
Molybdopterin oxidoreductase, iron-sulfur cluster-binding subunit, putative; Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration. Is likely essential for growth on H(2) or formate since the periplasmic hydrogenases and/or formate dehydrogenases act as primary electron donors for the Qrc complex. QrcC is an electron- transferring subunit; its cubane iron sulfur clusters form a pathway for electron transfer between the he [...]
  
  
 0.610
rub
Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
   
  
 0.600
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 str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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