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
Rvan_0033KEGG: azc:AZC_4245 glycine cleavage system T protein; TIGRFAM: glycine cleavage system T protein; PFAM: glycine cleavage T protein (aminomethyl transferase); Glycine cleavage T-protein barrel. (383 aa)    
Predicted Functional Partners:
Rvan_0030
KEGG: bid:Bind_0736 glycine dehydrogenase subunit 2.
 0.999
gcvPA
Glycine dehydrogenase (decarboxylating); 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.
 
 0.999
gcvH
Glycine cleavage system H protein; 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.
 0.999
glyA
Glycine 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.
 
 0.997
folD
Methylenetetrahydrofolate dehydrogenase (NADP(+)); Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
  
 
 0.971
Rvan_0653
KEGG: bbt:BBta_0398 dihydrolipoamide dehydrogenase; TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region.
 
 0.956
Rvan_1330
KEGG: rce:RC1_0122 dihydrolipoamide dehydrogenase; TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region.
 
 0.956
purH
SMART: AICARFT/IMPCHase bienzyme formylation region; TIGRFAM: phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; KEGG: met:M446_2965 phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PFAM: AICARFT/IMPCHase bienzyme formylation region; MGS domain protein.
   
 
 0.953
Rvan_0865
PFAM: FAD dependent oxidoreductase; KEGG: rpd:RPD_3428 glycine oxidase ThiO.
  
 
 0.952
Rvan_0018
TIGRFAM: 5,10-methylenetetrahydrofolate reductase; KEGG: mno:Mnod_4919 5,10-methylenetetrahydrofolate reductase; PFAM: methylenetetrahydrofolate reductase; Belongs to the methylenetetrahydrofolate reductase family.
  
 
 0.949
Your Current Organism:
Rhodomicrobium vannielii
NCBI taxonomy Id: 648757
Other names: R. vannielii ATCC 17100, Rhodomicrobium vannielii ATCC 17100, Rhodomicrobium vannielii NCIMB 10020, Rhodomicrobium vannielii str. ATCC 17100, Rhodomicrobium vannielii strain ATCC 17100
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.