SCOPe 2.08: Domain d2pdaa1: 2pda A:2-258

Lineage for d2pdaa1 (2pda A:2-258)

1. Root: SCOPe 2.08

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

3. Fold c.36: Thiamin diphosphate-binding fold (THDP-binding) [52517] (1 superfamily)
   3 layers: a/b/a; parallel beta-sheet of 6 strands, order 213465

4. Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (9 families)
   there are two different functional modules of this fold: pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules
   two Pyr and two PP modules assemble together in a conserved heterotetrameric core that binds two THDP coenzyme molecules

5. Family c.36.1.8: PFOR Pyr module [88746] (1 protein)
   domains VI, I and II are arranged in the same way as the TK PP, Pyr and C domains
   automatically mapped to Pfam PF01855

6. Protein Pyruvate-ferredoxin oxidoreductase, PFOR, domain I [88747] (1 species)

7. Species Desulfovibrio africanus [TaxId:873] [88748] (10 PDB entries)

8. Domain d2pdaa1: 2pda A:2-258 [31835]
   Other proteins in same PDB: d2pdaa2, d2pdaa3, d2pdaa4, d2pdaa5, d2pdab2, d2pdab3, d2pdab4, d2pdab5
   complexed with ca, mg, pyr, sf4, tpp

Details for d2pdaa1

PDB Entry: 2pda, 3 Å

PDB Description: crystal structure of the complex between pyruvate-ferredoxin oxidoreductase from desulfovibrio africanus and pyruvate.

PDB Compounds: (A:) protein (pyruvate-ferredoxin oxidoreductase)

SCOPe Domain Sequences for d2pdaa1:

Sequence; same for both SEQRES and ATOM records:

>d2pdaa1 c.36.1.8 (A:2-258) Pyruvate-ferredoxin oxidoreductase, PFOR, domain I {Desulfovibrio africanus [TaxId: 873]}
gkkmmttdgntatahvayamsevaaiypitpsstmgeeaddwaaqgrknifgqtltirem
qseagaagavhgalaagaltttftasqglllmipnmykisgellpgvfhvtaraiaahal
sifgdhqdiyaarqtgfamlasssvqeahdmalvahlaaiesnvpfmhffdgfrtsheiq
kievldyadmaslvnqkalaefraksmnpehphvrgtaqnpdiyfqgreaanpyylkvpg
ivaeymqkvasltgrsy

Timeline for d2pdaa1:

• d2pdaa1 first appeared (with stable ids) in SCOP 1.55
  
• d2pdaa1 appears in SCOPe 2.07