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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
pucGVitamin B6-dependent (S)-ureidoglycine glyoxylate aminotransferase; Catalyzes the transamination between an unstable intermediate ((S)-ureidoglycine) and the end product of purine catabolism (glyoxylate) to yield oxalurate and glycine. Glyoxylate is the preferred substrate, but other amino-group acceptors can be used. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. (416 aa)    
Predicted Functional Partners:
pucF
Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S- ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 (By similarity).
 
 
  0.991
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 (By similarity); Belongs to the SHMT family.
  
 0.861
pucL
Urate oxidase with peroxide reductase N-terminal domain; Catalyzes two steps in the degradation of uric acid, i.e. the oxidation of uric acid to 5-hydroxyisourate (HIU) and the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5- ureidoimidazoline (OHCU) to (S)-allantoin.
 
  
 0.841
gcvPB
Glycine decarboxylase (subunit 2) (glycine cleavage system protein P); 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 (By similarity); Belongs to the GcvP family. C-terminal subunit subfamily.
  
 
 0.839
kbl
2-amino-3-ketobutyrate CoA ligase (glycine acetyl transferase); Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
    
 0.828
pucH
Allantoinase; Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.
    0.809
gcvPA
Glycine decarboxylase (subunit 1) (glycine cleavage system protein P); 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 (By similarity).
  
 
 0.808
pucM
5-hydroxyisourate hydrolase; Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
 
    0.721
alaS
alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
  
  
 0.715
purD
Phosphoribosylglycinamide synthetase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
  
    0.700
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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