SCOP 1.75: Domain d2qmwa2: 2qmw A:185-264

Lineage for d2qmwa2 (2qmw A:185-264)

1. Root: SCOP 1.75

2. Class d: Alpha and beta proteins (a+b) [53931] (376 folds)

3. Fold d.58: Ferredoxin-like [54861] (59 superfamilies)
   alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2

4. Superfamily d.58.18: ACT-like [55021] (14 families)
   regulatory domain linked to a wide range of metabolic enzymes

5. Family d.58.18.3: Phenylalanine metabolism regulatory domain [55028] (2 proteins)

6. Protein Prephenate dehydratase C-terminal domain [160320] (1 species)

7. Species Staphylococcus aureus [TaxId:1280] [160321] (1 PDB entry)
   Uniprot Q99SX2 185-264

8. Domain d2qmwa2: 2qmw A:185-264 [150900]
   Other proteins in same PDB: d2qmwa1, d2qmwb1
   complexed with act, edo, na, peg

Details for d2qmwa2

PDB Entry: 2qmw, 2.3 Å

PDB Description: The crystal structure of the prephenate dehydratase (PDT) from Staphylococcus aureus subsp. aureus Mu50

PDB Compounds: (A:) Prephenate dehydratase

SCOP Domain Sequences for d2qmwa2:

Sequence; same for both SEQRES and ATOM records:

>d2qmwa2 d.58.18.3 (A:185-264) Prephenate dehydratase C-terminal domain {Staphylococcus aureus [TaxId: 1280]}
slmflitpmhdkpgllasvlntfalfninlswiesrplktqlgmyrffvqadsaittdik
kviailetldfkvemigafn

Timeline for d2qmwa2:

• d2qmwa2 is new in SCOP 1.75
  
• d2qmwa2 appears in SCOPe 2.01
  
• d2qmwa2 appears in the current release, SCOPe 2.08