SCOPe 2.08: Domain d1gkrd2: 1gkr D:55-379

Lineage for d1gkrd2 (1gkr D:55-379)

1. Root: SCOPe 2.08

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (34 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 d1gkrd2: 1gkr D:55-379 [70258]
   Other proteins in same PDB: d1gkra1, d1gkrb1, d1gkrc1, d1gkrd1
   complexed with zn

Details for d1gkrd2

PDB Entry: 1gkr, 2.6 Å

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

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

SCOPe Domain Sequences for d1gkrd2:

Sequence; same for both SEQRES and ATOM records:

>d1gkrd2 c.1.9.6 (D:55-379) L-hydantoinase {Arthrobacter aurescens [TaxId: 43663]}
gvvdehvhiidmdlknrygrfeldsesaavggittiiempitfpptttldaflekkkqag
qrlkvdfalygggvpgnlpeirkmhdagavgfksmmaasvpgmfdavsdgelfeifqeia
acgsvivvhaenetiiqalqkqikaaggkdmaayeasqpvfqeneaiqralllqkeagcr
livlhvsnpdgvelihqaqsegqdvhcesgpqylnittddaerigpymkvappvrsaemn
irlweqlenglidtlgsdhgghpvedkepgwkdvwkagngalgletslpmmltngvnkgr
lslerlvevmcekpaklfgiypqkg

Timeline for d1gkrd2:

• d1gkrd2 first appeared in SCOP 1.61
  
• d1gkrd2 appears in SCOPe 2.07