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Mettu_2507 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2507" - TIGRFAM: 6-phosphogluconate dehydratase in Methylobacter tundripaludum
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second shell of interactors
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some 3D structure is known or predicted
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Known Interactions
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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_2507TIGRFAM- 6-phosphogluconate dehydratase; KEGG- pat-Patl_0972 phosphogluconate dehydratase; PFAM- Dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family (606 aa)    
Predicted Functional Partners:
Mettu_2508
2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase; TIGRFAM- KDPG/KHG aldolase; KEGG- pct-PC1_1833 keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; PFAM- KDPG/KHG aldolase (216 aa)
 
  0.999
Mettu_2028
TIGRFAM- 6-phosphogluconolactonase; KEGG- mei-Msip34_1095 6-phosphogluconolactonase; PFAM- Glucosamine/galactosamine-6-phosphate isomerase (227 aa)
 
 
  0.988
ilvC
Ketol-acid reductoisomerase (NADP(+)); Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol- acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3- dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3- hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate; Belongs to the ketol-acid reductoisomerase family (338 aa)
 
  0.968
Mettu_2506
Glucose-6-phosphate 1-dehydrogenase; Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone (495 aa)
 
 
  0.945
ilvE
Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family (308 aa)
   
  0.881
Mettu_2029
Glucose-6-phosphate 1-dehydrogenase; Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone (495 aa)
 
 
  0.873
Mettu_1418
Glyoxylate reductase; KEGG- mca-MCA1407 2-hydroxyacid dehydrogenase; PFAM- D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region (323 aa)
 
 
  0.841
Mettu_2397
TIGRFAM- Acetolactate synthase, large subunit, biosynthetic; KEGG- mca-MCA2270 acetolactate synthase, large subunit, biosynthetic type; PFAM- Thiamine pyrophosphate enzyme, N-terminal TPP binding region; Thiamine pyrophosphate enzyme, central region; Thiamine pyrophosphate enzyme, C-terminal TPP-binding (578 aa)
  0.840
Mettu_3921
PFAM- 3-hydroxyacyl-CoA dehydrogenase, NAD binding; 3-hydroxyacyl-CoA dehydrogenase, C-terminal; Crotonase, core; KEGG- rce-RC1_1947 3-hydroxyacyl-CoA dehydrogenase, putative (779 aa)
   
 
  0.826
Mettu_2030
6-phosphogluconate dehydrogenase, decarboxylating; Catalyzes the oxidative decarboxylation of 6- phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH; Belongs to the 6-phosphogluconate dehydrogenase family (481 aa)
         
  0.820
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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