SCOP 1.67: Domain d1f1xc2: 1f1x C:148-322

Lineage for d1f1xc2 (1f1x C:148-322)

1. Root: SCOP 1.67

2. Class d: Alpha and beta proteins (a+b) [53931] (260 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] (5 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] (3 PDB entries)

8. Domain d1f1xc2: 1f1x C:148-322 [83213]

Details for d1f1xc2

PDB Entry: 1f1x, 1.6 Å

PDB Description: crystal structure of homoprotocatechuate 2,3-dioxygenase from brevibacterium fuscum

SCOP Domain Sequences for d1f1xc2:

Sequence; same for both SEQRES and ATOM records:

>d1f1xc2 d.32.1.3 (C:148-322) Homoprotocatechuate 2,3-dioxygenase {Brevibacterium fuscum}
gelvrldhfnqvtpdvprgrkyledlgfrvtediqddegttyaawmhrkgtvhdtaltgg
ngprlhhvafsthekhniiqicdkmgalrisdriergpgrhgvsnafylyildpdnhrie
iytqdyytgdpdnptitwnvhdnqrrdwwgnpvvpswyteaskvldldgnvqeii

Timeline for d1f1xc2:

• d1f1xc2 first appeared in SCOP 1.65
  
• d1f1xc2 appears in SCOP 1.69
  
• d1f1xc2 appears in the current release, SCOPe 2.08