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
mcl1beta-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. (318 aa)    
Predicted Functional Partners:
mch
L-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).
 
 
 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.
  
 
0.935
RSP_1255
Phosphate acetyltransferase; IMG reference gene:2512956299; PFAM: MaoC like domain; Phosphate acetyl/butaryl transferase.
  
 
 0.932
pccA
Biotin carboxyl carrier protein;biotin carboxylase; IMG reference gene:2512954118; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Biotin carboxylase C-terminal domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; Biotin-requiring enzyme; TIGRFAM: acetyl-CoA carboxylase, biotin carboxylase subunit; truncated by 29 aa.
  
 
 0.923
RSP_2313
2-hydroxyacid dehydrogenase; IMG reference gene:2512954247; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain.
 
 
 0.919
glcB
Malate synthase; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily.
    
 0.916
pccB
propionyl-CoA carboxylase carboxyltransferase subunit; IMG reference gene:2512954113; PFAM: Carboxyl transferase domain; Belongs to the AccD/PCCB family.
  
 
 0.916
acsA-2
Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family.
  
 
 0.915
RSP_0245
Serine-pyruvate aminotransferase/aspartate aminotransferase; IMG reference gene:2512955251; PFAM: Aminotransferase class-V.
  
 
 0.910
RSP_3366
IMG reference gene:2512956875; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain.
    
 0.906
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 (34%) [HD]