SCOPe 2.05: Domain d1gkrc2: 1gkr C:55-379

Lineage for d1gkrc2 (1gkr C:55-379)

1. Root: SCOPe 2.05

2. Class c: Alpha and beta proteins (a/b) [51349] (148 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)
   automatically mapped to Pfam PF13147

6. Protein L-hydantoinase [75077] (1 species)

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

8. Domain d1gkrc2: 1gkr C:55-379 [70256]
   Other proteins in same PDB: d1gkra1, d1gkrb1, d1gkrc1, d1gkrd1
   complexed with zn

Details for d1gkrc2

PDB Entry: 1gkr, 2.6 Å

PDB Description: l-hydantoinase (dihydropyrimidinase) from arthrobacter aurescens

PDB Compounds: (C:) non-ATP dependent l-selective hydantoinase

SCOPe Domain Sequences for d1gkrc2:

Sequence; same for both SEQRES and ATOM records:

>d1gkrc2 c.1.9.6 (C:55-379) L-hydantoinase {Arthrobacter aurescens [TaxId: 43663]}
gvvdehvhiidmdlknrygrfeldsesaavggittiiempitfpptttldaflekkkqag
qrlkvdfalygggvpgnlpeirkmhdagavgfksmmaasvpgmfdavsdgelfeifqeia
acgsvivvhaenetiiqalqkqikaaggkdmaayeasqpvfqeneaiqralllqkeagcr
livlhvsnpdgvelihqaqsegqdvhcesgpqylnittddaerigpymkvappvrsaemn
irlweqlenglidtlgsdhgghpvedkepgwkdvwkagngalgletslpmmltngvnkgr
lslerlvevmcekpaklfgiypqkg

Timeline for d1gkrc2:

• d1gkrc2 first appeared in SCOP 1.61
  
• d1gkrc2 appears in SCOPe 2.04
  
• d1gkrc2 appears in SCOPe 2.06
  
• d1gkrc2 appears in the current release, SCOPe 2.08