SCOP 1.75: Domain d3ecka2: 3eck A:148-322

Lineage for d3ecka2 (3eck A:148-322)

1. Root: SCOP 1.75

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] (10 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 d3ecka2: 3eck A:148-322 [158109]
   automatically matched to d1f1xa2
   complexed with ca, cl, fe2, gol, xxg; mutant

Details for d3ecka2

PDB Entry: 3eck, 1.6 Å

PDB Description: structure of e323l homoprotocatechuate 2,3-dioxygenase from brevibacterium fuscum in complex with putative o-o bond cleavage intermediate formed via in crystallo reaction with 4-sulfonyl catechol at low oxygen concentrations

PDB Compounds: (A:) PROTEIN (Homoprotocatechuate 2,3-dioxygenase)

SCOP Domain Sequences for d3ecka2:

Sequence; same for both SEQRES and ATOM records:

>d3ecka2 d.32.1.3 (A:148-322) Homoprotocatechuate 2,3-dioxygenase {Brevibacterium fuscum [TaxId: 47914]}
gelvrldhfnqvtpdvprgrkyledlgfrvtediqddegttyaawmhrkgtvhdtaltgg
ngprlhhvafsthekhniiqicdkmgalrisdriergpgrhgvsnafylyildpdnhrie
iytqdyytgdpdnptitwnvhdnqrrdwwgnpvvpswyteaskvldldgnvqeii

Timeline for d3ecka2:

• d3ecka2 is new in SCOP 1.75
  
• d3ecka2 appears in SCOPe 2.01
  
• d3ecka2 appears in the current release, SCOPe 2.08