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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
AEB82510.1TIGRFAM: Succinate CoA transferase; KEGG: ajs:Ajs_0046 acetyl-CoA hydrolase; PFAM: Acetyl-CoA hydrolase/transferase. (488 aa)    
Predicted Functional Partners:
AEB84840.1
TIGRFAM: Methylmalonyl-CoA mutase, alpha chain, catalytic; Methylmalonyl-CoA mutase, C-terminal; KEGG: dia:Dtpsy_1849 methylmalonyl-CoA mutase; PFAM: Methylmalonyl-CoA mutase, alpha/beta chain, catalytic; Cobalamin (vitamin B12)-binding.
 
 
 0.949
sucC
succinyl-CoA synthetase, 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.
   
 0.936
AEB83909.1
Acetate--CoA ligase; KEGG: bbr:BB0615 AMP-binding enzyme; PFAM: AMP-dependent synthetase/ligase.
  
 0.935
acsA
acetate/CoA ligase; 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.
  
 0.935
AEB86850.1
Acetate--CoA ligase; KEGG: bur:Bcep18194_C7155 AMP-dependent synthetase and ligase; PFAM: AMP-dependent synthetase/ligase.
  
 0.935
AEB86954.1
Acetate--CoA ligase; KEGG: gka:GK2759 acetyl-CoA synthetase (acetate-CoA ligase); PFAM: AMP-dependent synthetase/ligase.
  
 0.935
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.
   
 0.932
AEB84580.1
TIGRFAM: Succinate dehydrogenase/fumarate reductase iron-sulphur protein; KEGG: dac:Daci_2424 succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: Ferredoxin.
   
 
 0.923
AEB84780.1
Pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
   
 0.920
AEB84890.1
Dihydrolipoyllysine-residue acetyltransferase; KEGG: azo:azo3870 hypothetical protein; PFAM: 2-oxoacid dehydrogenase acyltransferase, catalytic domain.
   
 0.920
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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