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
kblGlycine C-acetyltransferase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. (399 aa)    
Predicted Functional Partners:
tdh
L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family.
 
 0.998
gcvP
Glycine dehydrogenase (aminomethyl-transferring); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
  
 
 0.950
glyA
Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
  
 
 0.918
AND13055.1
Threonine aldolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.913
AND13027.1
NAD(P)-dependent oxidoreductase; NADP(+)-dependent; catalyzes the formation of 3-hydroxypropionate from the toxic malonic semialdehyde, catalyzes the formation of 2-aminomalonate-semialdehyde from L-serine; can also use 3-hydroxybutyrate, 3-hydroxy-isobutyrate, D-threonine, L-allo-threonine,D-serine; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
    
  0.902
coaD
Pantetheine-phosphate adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family.
     
 0.825
bioA
Adenosylmethionine--8-amino-7-oxononanoate transaminase; Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
  
 0.795
yiaY
L-threonine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.780
bioD-2
Dethiobiotin synthase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. Belongs to the dethiobiotin synthetase family.
  
 0.766
AND13406.1
Malonyl CoA-acyl carrier protein transacylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.759
Your Current Organism:
Proteus mirabilis
NCBI taxonomy Id: 584
Other names: ATCC 29906, CCUG 26767, CIP 103181, DSM 4479, LMG 3257, LMG:3257, NCTC 11938, P. mirabilis
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