SCOPe 2.08: Domain d2fzma2: 2fzm A:262-610

Lineage for d2fzma2 (2fzm A:262-610)

1. Root: SCOPe 2.08

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

3. Fold c.1: TIM beta/alpha-barrel [51350] (34 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.23: FAD-linked oxidoreductase [51730] (3 families)
   distinct cofactor-binding mode from both FMN- and NAD(P)-linked TIM-barrel oxidoreductases; families are related by a circular permutation

5. Family c.1.23.2: Proline dehydrohenase domain of bifunctional PutA protein [82279] (2 proteins)
   automatically mapped to Pfam PF01619

6. Protein Proline dehydrohenase domain of bifunctional PutA protein [82280] (2 species)

7. Species Escherichia coli [TaxId:562] [82281] (7 PDB entries)
   Uniprot P09546 87-610

8. Domain d2fzma2: 2fzm A:262-610 [134459]
   Other proteins in same PDB: d2fzma1
   automated match to d1tj1a2
   complexed with fad, so2

Details for d2fzma2

PDB Entry: 2fzm, 2.3 Å

PDB Description: structure of the e. coli puta proline dehydrogenase domain reduced by dithionite and complexed with so2

PDB Compounds: (A:) Bifunctional protein putA, Proline dehydrogenase (EC 1.5.99.8) (Proline oxidase)

SCOPe Domain Sequences for d2fzma2:

Sequence; same for both SEQRES and ATOM records:

>d2fzma2 c.1.23.2 (A:262-610) Proline dehydrohenase domain of bifunctional PutA protein {Escherichia coli [TaxId: 562]}
getiaealanarkleekgfrysydmlgeaaltaadaqaymvsyqqaihaigkasngrgiy
egpgisiklsalhprysraqydrvmeelyprlksltllarqydiginidaeesdrleisl
dlleklcfepelagwngigfviqayqkrcplvidylidlatrsrrrlmirlvkgaywdse
ikraqmdglegypvytrkvytdvsylacakkllavpnliypqfathnahtlaaiyqlagq
nyypgqyefqclhgmgeplyeqvtgkvadgklnrpcriyapvgthetllaylvrrlleng
antsfvnriadtslpldelvadpvtaveklaqqegqtglphpkiplprd

Timeline for d2fzma2:

• d2fzma2 first appeared in SCOP 1.73
  
• d2fzma2 appears in SCOPe 2.07