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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
AF_0366acetyl-CoA synthetase (acs-2); Similar to PID:1001216 PID:1001254 percent identity: 47.28; identified by sequence similarity; putative. (681 aa)    
Predicted Functional Partners:
AF_1340
Citrate synthase (citZ); Similar to GB:U05257 SP:P39120 PID:487433 PID:2293267 GB:AL009126 percent identity: 50.27; identified by sequence similarity; putative.
  
 0.963
AF_1938
Conserved hypothetical protein; Catalyzes the reversible conversion of a variety of acids to the corresponding acyl-CoA esters. Shows the highest activity with the aryl acids, indoleacetate and phenylacetate, as compared to acetate. In the reverse direction, phenylacetyl-CoA is the best substrate. Seems to be involved primarily in the degradation of aryl-CoA esters to the corresponding acids. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. In the C-terminal section; belongs to the acetate CoA ligase alpha subunit family.
    
 0.958
cdhE
acetyl-CoA decarbonylase/synthase, subunit gamma (cdhE); Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2).
   
 
 0.951
AF_1211
Conserved hypothetical protein; Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters; In the C-terminal section; belongs to the acetate CoA ligase beta subunit family.
    
 0.948
AF_1699
Pyruvate ferredoxin oxidoreductase, subunit gamma (porG); Similar to PID:1197358 percent identity: 50.84; identified by sequence similarity; putative.
  
 
 0.947
korB
2-ketoglutarate ferredoxin oxidoreductase, subunit beta (korB); Similar to GB:L77117 PID:1591241 percent identity: 51.38; identified by sequence similarity; putative.
  
 
 0.946
korA
2-ketoglutarate ferredoxin oxidoreductase, subunit alpha (korA); Similar to GB:L77117 PID:1592279 percent identity: 52.34; identified by sequence similarity; putative.
  
 
 0.933
AF_1701
Pyruvate ferredoxin oxidoreductase, subunit alpha (porA); Similar to PID:1590995 percent identity: 50.27; identified by sequence similarity; putative.
  
 
 0.922
AF_2053
2-ketoisovalerate ferredoxin oxidoreductase, subunit alpha (vorA); Similar to PID:1197363 percent identity: 41.16; identified by sequence similarity; putative.
  
 
 0.922
leuA
2-isopropylmalate synthase (leuA-2); Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate).
  
 
 0.921
Your Current Organism:
Archaeoglobus fulgidus
NCBI taxonomy Id: 224325
Other names: A. fulgidus DSM 4304, Archaeoglobus fulgidus DSM 4304, Archaeoglobus fulgidus VC-16, Archaeoglobus fulgidus str. DSM 4304, Archaeoglobus fulgidus strain DSM 4304
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.