SCOP 1.71: Domain d1tj0a2: 1tj0 A:262-610

Lineage for d1tj0a2 (1tj0 A:262-610)

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (32 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] (2 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] (1 protein)

6. Protein Proline dehydrohenase domain of bifunctional PutA protein [82280] (1 species)

7. Species Escherichia coli [TaxId:562] [82281] (5 PDB entries)

8. Domain d1tj0a2: 1tj0 A:262-610 [112433]
   Other proteins in same PDB: d1tj0a1
   complexed with fad, lac

Details for d1tj0a2

PDB Entry: 1tj0, 2.1 Å

PDB Description: Crystal structure of E. coli PutA proline dehydrogenase domain (residues 86-669) co-crystallized with L-lactate

SCOP Domain Sequences for d1tj0a2:

Sequence; same for both SEQRES and ATOM records:

>d1tj0a2 c.1.23.2 (A:262-610) Proline dehydrohenase domain of bifunctional PutA protein {Escherichia coli}
getiaealanarkleekgfrysydmlgeaaltaadaqaymvsyqqaihaigkasngrgiy
egpgisiklsalhprysraqydrvmeelyprlksltllarqydiginidaeesdrleisl
dlleklcfepelagwngigfviqayqkrcplvidylidlatrsrrrlmirlvkgaywdse
ikraqmdglegypvytrkvytdvsylacakkllavpnliypqfathnahtlaaiyqlagq
nyypgqyefqclhgmgeplyeqvtgkvadgklnrpcriyapvgthetllaylvrrlleng
antsfvnriadtslpldelvadpvtaveklaqqegqtglphpkiplprd

Timeline for d1tj0a2:

• d1tj0a2 is new in SCOP 1.71
  
• d1tj0a2 appears in SCOP 1.73
  
• d1tj0a2 appears in the current release, SCOPe 2.08