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STRINGSTRING
Mettu_1748 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_1748" - PFAM: Aminotransferase, class I/II in Methylobacter tundripaludum
Nodes:
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Mettu_1748PFAM- Aminotransferase, class I/II; KEGG- sua-Saut_0088 class I/II aminotransferase (339 aa)    
Predicted Functional Partners:
cobQ
Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation (483 aa)
 
  0.984
cobD
Cobalamin biosynthesis protein CobD; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group (298 aa)
 
 
  0.976
hisF
Imidazole glycerol phosphate synthase subunit HisF; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (257 aa)
  0.959
cobS
Adenosylcobinamide-GDP ribazoletransferase; Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5’-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5’-phosphate; Belongs to the CobS family (301 aa)
 
   
  0.952
Mettu_2825
KEGG- alv-Alvin_2084 chorismate mutase; TIGRFAM- Gamma/beta/epsilon proteobacterial P-protein, chorismate mutase domain; PFAM- Prephenate dehydratase; Chorismate mutase, type II; Amino acid-binding ACT (361 aa)
   
  0.933
Mettu_1747
Alpha-ribazole phosphatase; KEGG- mfa-Mfla_0100 phosphoglycerate mutase; TIGRFAM- Alpha-ribazole phosphatase, CobC; PFAM- Phosphoglycerate mutase (187 aa)
 
   
  0.918
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine (436 aa)
  0.916
hisI
Phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP (130 aa)
 
 
  0.905
aroA
3-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3- phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate (733 aa)
   
 
  0.878
hisB
HAMAP- Imidazoleglycerol-phosphate dehydratase; KEGG- psa-PST_4090 imidazoleglycerol-phosphate dehydratase; PFAM- Imidazoleglycerol-phosphate dehydratase (208 aa)
 
  0.861
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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