SCOP 1.71: Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain

Lineage for Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (32 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.9: Metallo-dependent hydrolases [51556] (13 families)
   the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
   has transition metal ions bound inside the barrel

5. Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain [75073] (3 proteins)

Proteins:

1. D-hydantoinase [75074] (3 species)

   1. Species Bacillus stearothermophilus [TaxId:1422] [75076] (1 PDB entry)

   2. Species Burkholderia pickettii [TaxId:329] [89488] (1 PDB entry)

   3. Species Thermus sp. [TaxId:275] [75075] (2 PDB entries)

2. Dihydropyrimidinase related protein-1 [102084] (1 species)

   • Species Mouse (Mus musculus) [TaxId:10090] [102085] (1 PDB entry)

3. L-hydantoinase [75077] (1 species)

   • Species Arthrobacter aurescens [TaxId:43663] [75078] (1 PDB entry)

More info for Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain

Timeline for Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain:

• Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain first appeared in SCOP 1.61
  
• Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain appears in SCOP 1.69
  
• Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain appears in SCOP 1.73
  
• Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain appears in the current release, SCOPe 2.08