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
pcaI3-oxoadipate CoA-transferase subunit A; Identified by similarity to protein SP:Q01103 (Pseudomonas putida). Catalyses the following reaction : succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA. (223 aa)    
Predicted Functional Partners:
pcaJ
3-oxoadipate CoA-transferase subunit B; Identified by similarity to protein SP: P0A102 (Pseudomonas putida). Catalyses the following reaction : succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA.
 0.999
scoB
3-oxoacid CoA-transferase catalyses the following reaction: succinyl-CoA + a 3-oxo acid <=> succinate + a 3-oxoacyl-CoA. Acetoacetate or, more slowly, 3-oxopropanoate, 3-oxopentanoate, 3-oxo-4-methylpentanoate or 3-oxohexanoate can act as acceptor.
 
 0.997
pcaD
3-oxoadipate enol-lactonase catalyses the formation of 3-oxoadipate from 3-oxoadipate enol-lactone. It is involved in aromatic acids catabolism.
  
 
 0.920
fadA
Fatty acid oxidation complex subunit beta; Also named acetyl-CoA C-acyltransferase. Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids. Part of the FadAB fatty acid oxidation complex; Belongs to the thiolase-like superfamily. Thiolase family.
 
 
 0.918
AARI_04450
acetyl-CoA C-acyltransferase (also named 3-ketoacyl-CoA thiolase or thiolase I) has a broad chain-length specificity for its substrates and is involved in degradative pathways such as fatty acid beta-oxidation; Belongs to the thiolase-like superfamily. Thiolase family.
 
 
 0.879
AARI_04480
IclR-family transcriptional regulator; Identified by match to PF09339: IclR helix-turn-helix domain. This family of bacterial transcriptional regulators groups several proteins, including gylR, a possible activator protein for the gylABX glycerol operon in Streptomyces, and iclR, the repressor of the acetate operon (also known as glyoxylate bypass operon) in Escherichia coli and Salmonella typhimurium.
  
  
 0.729
pcaH
Protocatechuate 3,4-dioxygenase subunit beta; Catalyses the following reaction: 3,4-dihydroxybenzoate + O(2) <=> 3-carboxy-cis,cis-muconate.
  
  
 0.494
AARI_04440
Hypothetical secreted protein; Signal peptide predicted by SignalP 3.0 HMM (probability: 1.000) with cleavage site probability 0.321 between position 26 and 27.
       0.427
fadB
Fatty acid oxidation complex subunit alpha; Identified by similarity to protein SP: P21177 (Escherichia coli). Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities. Involved in the aerobic and anaerobic degradation of long-chain fatty acids. Part of the FadAB fatty acid oxidation complex.
  
  
 0.403
AARI_32560
Putative citrate lyase beta subunit; Citrate lyase catalyses the formation of acetate and oxaloacetate from citrate; Belongs to the HpcH/HpaI aldolase family.
     
 0.403
Your Current Organism:
Glutamicibacter arilaitensis
NCBI taxonomy Id: 861360
Other names: Arthrobacter arilaitensis CIP 108037, Arthrobacter arilaitensis Re117, G. arilaitensis Re117, Glutamicibacter arilaitensis Re117
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.