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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
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second shell of interactors
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a 3D structure is known or predicted
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[Homology]
Score
AEB83174.1KEGG: dia:Dtpsy_0656 phosphoglycerate mutase; PFAM: Histidine phosphatase superfamily, clade-1; SMART: Histidine phosphatase superfamily, clade-1. (188 aa)    
Predicted Functional Partners:
cobS
Cobalamin-5-phosphate synthase CobS; 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.
 
 
 0.997
cobT
Nicotinate-nucleotide/dimethylbenzimidazole phosphoribosyltransferase; Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
 
 
 0.989
AEB83541.1
Adenosylcobinamide-phosphate guanylyltransferase; Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
 
  
 0.866
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. Belongs to the CobB/CobQ family. CobQ subfamily.
 
  
 0.860
gpmA
Phosphoglycerate mutase 1 family; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily.
   
 0.741
cobD
Cobalamin biosynthesis protein CobD; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
 
   
 0.740
AEB83540.1
PFAM: CobB/CobQ-like glutamine amidotransferase; Cobyrinic acid a,c-diamide synthase; KEGG: dia:Dtpsy_1013 CobB/CobQ domain protein glutamine amidotransferase.
 
  
 0.738
ilvA
Threonine dehydratase, biosynthetic; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
       0.608
AEB83545.1
cob(I)alamin adenosyltransferase; Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids.
 
   
 0.597
AEB86814.1
SMART: Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain; TIGRFAM: Glyceraldehyde-3-phosphate dehydrogenase, type I; KEGG: ajs:Ajs_3960 glyceraldehyde-3-phosphate dehydrogenase; PFAM: Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain; Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
    
 0.591
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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