SCOPe 2.05: Domain d2igac1: 2iga C:4-147

Lineage for d2igac1 (2iga C:4-147)

1. Root: SCOPe 2.05

2. Class d: Alpha and beta proteins (a+b) [53931] (381 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] (5 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] (15 PDB entries)

8. Domain d2igac1: 2iga C:4-147 [137364]
   automated match to d1q0oa1
   complexed with ca, cl, fe2, gol, oxy, xx2, xx3, xxp

Details for d2igac1

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: (C:) homoprotocatechuate 2,3-dioxygenase

SCOPe Domain Sequences for d2igac1:

Sequence; same for both SEQRES and ATOM records:

>d2igac1 d.32.1.3 (C:4-147) Homoprotocatechuate 2,3-dioxygenase {Brevibacterium fuscum [TaxId: 47914]}
eipkpvapapdilrcayaelvvtdlaksrnfyvdvlglhvsyedenqiylrsfeefihhn
lvltkgpvaalkamafrvrtpedvdkaeayyqelgcrterrkdgfvkgigdalrvedplg
fpyefffetthverlhmrydlysa

Timeline for d2igac1:

• d2igac1 first appeared in SCOP 1.73
  
• d2igac1 appears in SCOPe 2.04
  
• d2igac1 appears in SCOPe 2.06
  
• d2igac1 appears in the current release, SCOPe 2.08