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
EGW21281.1AIG2 family protein; PFAM: AIG2-like; KEGG: bja:bll7352 hypothetical protein. (134 aa)    
Predicted Functional Partners:
dtd
D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.
       0.778
EGW23755.1
TIGRFAM: Oxaloacetate decarboxylase, alpha subunit; KEGG: pmy:Pmen_2893 oxaloacetate decarboxylase; PFAM: Conserved carboxylase region; Pyruvate carboxyltransferase; Biotin/lipoyl attachment.
 
      0.595
metZ
O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.
     
 0.548
EGW22733.1
KEGG: mca:MCA0607 phosphoglucomutase; PFAM: Alpha-D-phosphohexomutase, alpha/beta/alpha domain I; Alpha-D-phosphohexomutase, alpha/beta/alpha domain II; Alpha-D-phosphohexomutase, alpha/beta/alpha domain III; Alpha-D-phosphohexomutase, C-terminal.
    
  0.490
EGW22051.1
TIGRFAM: Cysteine synthase B; Cysteine synthase K/M; KEGG: mca:MCA1899 cysteine synthase B; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; Belongs to the cysteine synthase/cystathionine beta- synthase family.
    
  0.469
EGW23422.1
TIGRFAM: Cysteine synthase A; Cysteine synthase K/M; KEGG: app:CAP2UW1_0445 cysteine synthase A; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; Belongs to the cysteine synthase/cystathionine beta- synthase family.
    
  0.469
pfp
Diphosphate--fructose-6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
       0.464
prs
Ribose-phosphate pyrophosphokinase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
   
  0.462
EGW22665.1
TIGRFAM: Phosphoribosyl pyrophosphokinase; KEGG: rfr:Rfer_2240 phosphoribosylpyrophosphate synthetase; PFAM: Phosphoribosyltransferase; Belongs to the ribose-phosphate pyrophosphokinase family.
   
  0.462
EGW20019.1
KEGG: mca:MCA1821 hypothetical protein.
  
     0.456
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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