SCOPe 2.02: Domain d1ynya2: 1yny A:53-384

Lineage for d1ynya2 (1yny A:53-384)

1. Root: SCOPe 2.02

2. Class c: Alpha and beta proteins (a/b) [51349] (147 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 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] (19 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] (5 proteins)

6. Protein D-hydantoinase [75074] (4 species)

7. Species Bacillus sp. AR9 [TaxId:301298] [141802] (1 PDB entry)
   Uniprot Q5DLU2 2-460

8. Domain d1ynya2: 1yny A:53-384 [123765]
   Other proteins in same PDB: d1ynya1, d1ynyb1
   complexed with mn

Details for d1ynya2

PDB Entry: 1yny, 2.3 Å

PDB Description: molecular structure of d-hydantoinase from a bacillus sp. ar9: evidence for mercury inhibition

PDB Compounds: (A:) D-hydantoinase

SCOPe Domain Sequences for d1ynya2:

Sequence; same for both SEQRES and ATOM records:

>d1ynya2 c.1.9.6 (A:53-384) D-hydantoinase {Bacillus sp. AR9 [TaxId: 301298]}
ggidphthldmpfggtvtaddfftgtraaafggttsivdfcltkkgeslksaiatwheka
rgkavidygfhlmiaeandqvleelesvissegitslkvfmayknvfqaddetlfktlvk
akelgalvqvhaengdvldyltkkalaegntdpiyhaytrppeaegeatgraialtalag
sqlyvvhvscasavqriaearekgwnvygetcpqylaldvsimdqpdfegakyvwspplr
ekwnqevlwsalkngilqtvgsdhcpfnfrgqkelgrgdftkipnggpliedrltilyse
gvrqgrislnqfvdisstkaaklfgmfprkgt

Timeline for d1ynya2:

• d1ynya2 first appeared in SCOP 1.73
  
• d1ynya2 appears in SCOPe 2.01
  
• d1ynya2 appears in SCOPe 2.03
  
• d1ynya2 appears in the current release, SCOPe 2.08