SCOPe 2.08: Domain d1f1xc1: 1f1x C:4-147

Lineage for d1f1xc1 (1f1x C:4-147)

1. Root: SCOPe 2.08

2. Class d: Alpha and beta proteins (a+b) [53931] (396 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] (17 PDB entries)

8. Domain d1f1xc1: 1f1x C:4-147 [83212]
   complexed with fel

Details for d1f1xc1

PDB Entry: 1f1x, 1.6 Å

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

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

SCOPe Domain Sequences for d1f1xc1:

Sequence; same for both SEQRES and ATOM records:

>d1f1xc1 d.32.1.3 (C:4-147) Homoprotocatechuate 2,3-dioxygenase {Brevibacterium fuscum [TaxId: 47914]}
eipkpvapapdilrcayaelvvtdlaksrnfyvdvlglhvsyedenqiylrsfeefihhn
lvltkgpvaalkamafrvrtpedvdkaeayyqelgcrterrkdgfvkgigdalrvedplg
fpyefffetthverlhmrydlysa

Timeline for d1f1xc1:

• d1f1xc1 first appeared in SCOP 1.65
  
• d1f1xc1 appears in SCOPe 2.07