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
mchL-erythro-3-methylmalyl-CoA dehydratase; Involved in the ethylmalonyl-CoA pathway for acetate assimilation. Catalyzes the reversible hydration of mesaconyl-CoA (methylfumaryl-CoA) to yield beta-methylmalyl-CoA ((2R,3S)-beta- methylmalyl-CoA). (343 aa)    
Predicted Functional Partners:
RSP_1679
IMG reference gene:2512953583; PFAM: Acyl-CoA dehydrogenase, C-terminal domain; Acyl-CoA dehydrogenase, middle domain; Acyl-CoA dehydrogenase, N-terminal domain; extended by 7 aa.
 
 0.983
mcl1
beta-methylmalyl-CoA/L-malyl-CoA lyase; Involved in the ethylmalonyl-CoA pathway for acetate assimilation. Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to yield beta-methylmalyl-CoA. It is also able to catalyze the cleavage of (S)-citramalyl-CoA to yield acetyl-CoA and pyruvate, although this reaction is not involved in the ethylmalonyl- CoA pathway.
 
 
 0.980
mcl2
Putative citrate lyase beta chain; Catalyzes the hydrolysis of (3S)-malyl-CoA to (3S)-malate and free CoA. Inactive towards beta-methylmalyl-CoA and other CoA esters.
 
  
 0.967
MeaA
(R)-ethylmalonyl-CoA mutase; Radical enzyme that catalyzes the transformation of (2R)- ethylmalonyl-CoA to (2S)-methylsuccinyl-CoA. Is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation required for R.sphaeroides growth on acetate as sole carbon source. Is highly specific for its substrate, ethylmalonyl-CoA, and accepts methylmalonyl-CoA only at 0.2% relative activity.
 
  
 0.966
ccr
crotonyl-CoA carboxylase/reductase; Catalyzes the NADPH-dependent reductive carboxylation of crotonyl-CoA ((2E)-butenoyl-CoA) to (2S)-ethylmalonyl-CoA, in the presence of CO2. This is a key reaction in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation required for R.sphaeroides growth on acetate as sole carbon source. Is also able to accept acryloyl-CoA as an alternative substrate, yielding (2S)- methylmalonyl-CoA. To a lesser extent, when CO2 is absent, the enzyme also catalyzes the reduction of crotonyl-CoA to butanoyl-CoA.
 
 
 0.962
hbdA
IMG reference gene:2512953592; PFAM: 3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain.
  
 
 0.849
RSP_0972
Putative conserved small protein; IMG reference gene:2512956009; PFAM: Domain of unknown function (DUF1737).
  
    0.848
RSP_2196
3-hydroxyacyl-CoA dehydrogenase; IMG reference gene:2512954124; PFAM: Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain.
  
 0.847
RSP_0971
Putative membrane protein; IMG reference gene:2512956008; PFAM: NnrU protein.
 
    0.843
RSP_0398
Dehydrogenase; IMG reference gene:2512955407; PFAM: Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Glu/Leu/Phe/Val dehydrogenase, dimerisation domain; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
  
  
 0.690
Your Current Organism:
Rhodobacter sphaeroides 241
NCBI taxonomy Id: 272943
Other names: R. sphaeroides 2.4.1, Rhodobacter sphaeroides 2.4.1, Rhodobacter sphaeroides ATCC 17023, Rhodobacter sphaeroides ATH 2.4.1, Rhodobacter sphaeroides str. 2.4.1, Rhodobacter sphaeroides strain 2.4.1
Server load: low (14%) [HD]