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Mettu_4177 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_4177" - 8-amino-7-oxononanoate synthase in Methylobacter tundripaludum
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
Mettu_41778-amino-7-oxononanoate synthase; KEGG- sat-SYN_00565 2-amino-3-ketobutyrate coenzyme A ligase; PFAM- Aminotransferase, class I/II (407 aa)    
Predicted Functional Partners:
bioA
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase; 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 (450 aa)
 
  0.966
Mettu_4176
KEGG- sat-SYN_00564 L-threonine 3-dehydrogenase; PFAM- NAD-dependent epimerase/dehydratase (310 aa)
 
 
  0.951
bioC
Malonyl-[acyl-carrier protein] O-methyltransferase; Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl- L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway (257 aa)
 
  0.845
gcvP
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; Belongs to the GcvP family (963 aa)
   
 
  0.845
Mettu_2658
CoA-binding domain protein; PFAM- CoA-binding; GCN5-related N-acetyltransferase; KEGG- gca-Galf_1381 CoA-binding domain-containing protein (893 aa)
   
  0.843
bioB
Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical- based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family (322 aa)
 
  0.823
bioD
ATP-dependent dethiobiotin synthetase BioD; 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 (219 aa)
 
 
  0.810
Mettu_0134
Carboxylesterase; KEGG- mca-MCA1127 BioH protein; PFAM- Alpha/beta hydrolase fold-1 (287 aa)
     
  0.789
Mettu_2540
KEGG- mca-MCA2793 delta-aminolevulinic acid dehydratase; PFAM- Tetrapyrrole biosynthesis, porphobilinogen synthase; Belongs to the ALAD family (334 aa)
   
 
  0.745
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 (417 aa)
   
 
  0.727
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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