SCOPe 2.02: Domain d2igaa2: 2iga A:148-322

Lineage for d2igaa2 (2iga A:148-322)

1. Root: SCOPe 2.02

2. Class d: Alpha and beta proteins (a+b) [53931] (376 folds)

3. Fold d.32: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase [54592] (1 superfamily)
   beta-alpha-beta(3); 2 layers: alpha/beta

4. Superfamily d.32.1: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase [54593] (11 families)

5. Family d.32.1.3: Extradiol dioxygenases [54602] (4 proteins)
   duplication: consists of 2 similar domains with 2 repeats in each
   Similar to the Methylmalonyl-CoA epimerase dimer

6. Protein Homoprotocatechuate 2,3-dioxygenase [89886] (2 species)

7. Species Brevibacterium fuscum [TaxId:47914] [89888] (8 PDB entries)

8. Domain d2igaa2: 2iga A:148-322 [137361]
   automatically matched to d1f1xa2
   complexed with ca, cl, fe2, gol, oxy, xx2, xx3, xxp

Details for d2igaa2

PDB Entry: 2iga, 1.95 Å

PDB Description: Structure of Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in complex with reactive intermediates formed via in crystallo reaction with 4-nitrocatechol at low oxygen concentrations.

PDB Compounds: (A:) homoprotocatechuate 2,3-dioxygenase

SCOPe Domain Sequences for d2igaa2:

Sequence; same for both SEQRES and ATOM records:

>d2igaa2 d.32.1.3 (A:148-322) Homoprotocatechuate 2,3-dioxygenase {Brevibacterium fuscum [TaxId: 47914]}
gelvrldhfnqvtpdvprgrkyledlgfrvtediqddegttyaawmhrkgtvhdtaltgg
ngprlhhvafsthekhniiqicdkmgalrisdriergpgrhgvsnafylyildpdnhrie
iytqdyytgdpdnptitwnvhdnqrrdwwgnpvvpswyteaskvldldgnvqeii

Timeline for d2igaa2:

• d2igaa2 first appeared in SCOP 1.73
  
• d2igaa2 appears in SCOPe 2.01
  
• d2igaa2 appears in SCOPe 2.03
  
• d2igaa2 appears in the current release, SCOPe 2.08