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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene co-occurrence
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[Homology]
Score
glyA-2Serine 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. (431 aa)    
Predicted Functional Partners:
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.
  
 
 0.997
gcvH
Glycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
  
 
 0.994
gcvT
Glycine cleavage system protein T; Catalyzes the transfer of a methylene carbon from the methylamine-loaded GcvH protein to tetrahydrofolate, causing the release of ammonia and the generation of reduced GcvH protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.990
folD
Bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
 
 0.988
purH
Bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.972
fhs
Formate--tetrahydrofolate ligase; Catalyzes the formation of 10-formyltetrahydrofolate from formate and tetrahydrofolate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the formate--tetrahydrofolate ligase family.
  
 0.968
ANQ24145.1
Low-specificity L-threonine aldolase; Low- specificity; catalyzes the formation of acetaldehyde and glycine from L-threonine; acts on L-threonine, L-allo-threonine, L-threo-phenylserine, and L-erythro-phenylserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.961
ANQ24440.1
Sarcosine oxidase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GcvT family.
  
 0.961
ANQ21938.1
L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family.
  
 
 0.958
ANQ23529.1
L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family.
  
 
 0.958
Your Current Organism:
Vibrio natriegens
NCBI taxonomy Id: 691
Other names: ATCC 14048, Beneckea natriegens, CAIM 12, CCUG 16371, CCUG 4980 A, CIP 103193, DSM 759, IFO 15636, LMG 10935, LMG:10935, NBRC 15636, NCCB 73019, NCMB 857, NCMB:857, NCTC 11319, Pseudomonas natriegens, V. natriegens
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