SCOP 1.75: Domain d2puza2: 2puz A:80-380

Lineage for d2puza2 (2puz A:80-380)

1. Root: SCOP 1.75

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] (18 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.1.9.17: Imidazolonepropionase-like [159400] (3 proteins)

6. Protein Imidazolonepropionase [159405] (2 species)

7. Species Agrobacterium tumefaciens [TaxId:358] [159407] (2 PDB entries)
   Uniprot Q8U8Z6 78-378

8. Domain d2puza2: 2puz A:80-380 [149874]
   Other proteins in same PDB: d2puza1, d2puzb1
   complexed with cl, fe, mg, nig

Details for d2puza2

PDB Entry: 2puz, 1.83 Å

PDB Description: crystal structure of imidazolonepropionase from agrobacterium tumefaciens with bound product n-formimino-l-glutamate

PDB Compounds: (A:) Imidazolonepropionase

SCOP Domain Sequences for d2puza2:

Sequence; same for both SEQRES and ATOM records:

>d2puza2 c.1.9.17 (A:80-380) Imidazolonepropionase {Agrobacterium tumefaciens [TaxId: 358]}
palidchthlvfggnramefemrlngatyeeiakagggivssvrdtralsdevlvaqalp
rldtllsegvstieiksgygldietelkmlrvarrletlrpvrivtsylaahatpadykg
rnadyitdvvlpglekahaegladavdgfcegiafsvkeidrvfaaaqqrglpvklhaeq
lsnlggaelaasynalsadhleyldetgakalakagtvavllpgafyalrekqlppvqal
rdagaeialatdcnpgtspltsllltmnmgatlfrmtveecltattrnaakalgllaetg
t

Timeline for d2puza2:

• d2puza2 is new in SCOP 1.75
  
• d2puza2 appears in SCOPe 2.01
  
• d2puza2 appears in the current release, SCOPe 2.08