SCOPe 2.06: Domain d2ylsa1: 2yls A:11-154,A:390-542

Lineage for d2ylsa1 (2yls A:11-154,A:390-542)

1. Root: SCOPe 2.06

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.3: FAD/NAD(P)-binding domain [51904] (1 superfamily)
   core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander

4. Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families)

5. Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (15 proteins)
   duplication: both domains have similar folds and functions
   most members of the family contain common C-terminal alpha+beta domain

6. Protein Phenylacetone monooxygenase [110440] (1 species)

7. Species Thermobifida fusca [TaxId:2021] [110441] (6 PDB entries)
   Uniprot Q5YS95 # 55% sequence identity; Nocardia farcinica TaxID:37329

8. Domain d2ylsa1: 2yls A:11-154,A:390-542 [207665]
   automated match to d1w4xa1
   complexed with fad, nap

Details for d2ylsa1

PDB Entry: 2yls, 2.26 Å

PDB Description: snapshots of enzymatic baeyer-villiger catalysis: oxygen activation and intermediate stabilization: reduced enzyme bound to nadp

PDB Compounds: (A:) phenylacetone monooxygenase

SCOPe Domain Sequences for d2ylsa1:

Sequence; same for both SEQRES and ATOM records:

>d2ylsa1 c.3.1.5 (A:11-154,A:390-542) Phenylacetone monooxygenase {Thermobifida fusca [TaxId: 2021]}
rqppeevdvlvvgagfsglyalyrlrelgrsvhvietagdvggvwywnrypgarcdiesi
eycysfseevlqewnwteryasqpeilryinfvadkfdlrsgitfhttvtaaafdeatnt
wtvdtnhgdrirarylimasgqlsXdaltgalfkidirgvgnvalkekwaagprtylgls
tagfpnlffiagpgspsalsnmlvsieqhvewvtdhiaymfkngltrseavlekedewve
hvneiadetlypmtaswytganvpgkprvfmlyvggfhryrqicdevaakgyegfvlt

Timeline for d2ylsa1:

• d2ylsa1 first appeared in SCOPe 2.03
  
• d2ylsa1 appears in SCOPe 2.05
  
• d2ylsa1 appears in SCOPe 2.07
  
• d2ylsa1 appears in the current release, SCOPe 2.08