STRINGSTRING
dfa1 protein (Synechocystis sp. PCC6803) - STRING interaction network
"dfa1" - Diflavin flavoprotein A 1 in Synechocystis sp. PCC6803
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
dfa1Diflavin flavoprotein A 1; Mediates electron transfer from NADH to oxygen, reducing it to water. This modular protein has 3 redox cofactors, in other organisms the same activity requires 2 or 3 proteins; In the N-terminal section; belongs to the zinc metallo-hydrolase group 3 family (573 aa)    
Predicted Functional Partners:
blaOXA-3
annotation not available (304 aa)
           
  0.825
isiB
Flavodoxin; Low-potential electron donor to a number of redox enzymes (170 aa)
         
  0.773
ama
annotation not available (416 aa)
   
   
  0.718
sll0100
annotation not available (393 aa)
   
   
  0.718
slr0876
annotation not available (409 aa)
   
 
  0.717
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. Could be involved in hydrogenase-linked redox processes (By similarity) (115 aa)
 
   
  0.694
ndhJ
NAD(P)H-quinone oxidoreductase subunit J; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon- concentration (179 aa)
           
  0.689
sll1384
annotation not available (314 aa)
         
  0.648
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3’-5’ and 5’-3’ exonuclease activity (986 aa)
         
  0.633
fmt
Methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus (330 aa)
           
  0.599
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
Server load: low (11%) [HD]