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
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[Homology]
Score
mcmAmethylmalonyl-CoA mutase; Radical enzyme that catalyzes the transformation of (2R)- methylmalonyl-CoA to succinyl-CoA. Is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation required for R.sphaeroides growth on acetate as sole carbon source. (709 aa)    
Predicted Functional Partners:
argK
IMG reference gene:2512953931; PFAM: ArgK protein; TIGRFAM: LAO/AO transport system ATPase.
  
 0.998
epi
methylmalonyl-CoA epimerase; Promiscuous isomerase that catalyzes epimerization of both ethylmalonyl-CoA and methylmalonyl-CoA. Has thus a dual role in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation required for R.sphaeroides growth on acetate as sole carbon source.
 
 
 0.997
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.
 
 
0.993
sucD
Succinyl-CoA synthetase, alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
  
 
 0.951
RSP_0029
IMG reference gene:2512955012; PFAM: Acetyl-CoA hydrolase/transferase N-terminal domain; Citrate lyase, alpha subunit (CitF); TIGRFAM: succinate CoA transferases.
  
 
 0.950
sucC
succinyl-CoA synthetase (ADP-forming) beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
  
 
 0.949
RSP_1041
malonyl-CoA synthase; IMG reference gene:2512956081; PFAM: AMP-binding enzyme.
  
 
 0.915
pycA
Pyruvate carboxylase; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
  
 
 0.898
mdh
Malate dehydrogenase (NAD); Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 3 family.
  
 
 0.884
pckA
Phosphoenolpyruvate carboxykinase; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
  
 
 0.876
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
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