SCOP 1.65: Domain d1qgda2: 1qgd A:2-332

Lineage for d1qgda2 (1qgd A:2-332)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 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] (8 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.36.1.10: TK-like PP module [88760] (2 proteins)
   different order of the modules, PP module is N-terminal, Pyr module is next to it followed by a Rossmann-like domain

6. Protein Transketolase (TK), PP module [88761] (3 species)

7. Species Escherichia coli [TaxId:562] [89656] (1 PDB entry)

8. Domain d1qgda2: 1qgd A:2-332 [88368]
   Other proteins in same PDB: d1qgda1, d1qgda3, d1qgdb1, d1qgdb3

Details for d1qgda2

PDB Entry: 1qgd, 1.9 Å

PDB Description: transketolase from escherichia coli

SCOP Domain Sequences for d1qgda2:

Sequence; same for both SEQRES and ATOM records:

>d1qgda2 c.36.1.10 (A:2-332) Transketolase (TK), PP module {Escherichia coli}
ssrkelanairalsmdavqkaksghpgapmgmadiaevlwrdflkhnpqnpswadrdrfv
lsnghgsmliysllhltgydlpmeelknfrqlhsktpghpevgktagvetttgplgqgia
navgmaiaektlaaqfnrpghdivdhytyafmgdgcmmegishevcslagtlklgkliaf
yddngisidghvegwftddtamrfeaygwhvirdidghdaasikraveearavtdkpsll
mcktiigfgspnkagthdshgaplgdaeialtreqlgwkyapfeipseiyaqwdakeagq
akesawnekfaayakaypqeaaeftrrmkge

Timeline for d1qgda2:

• d1qgda2 is new in SCOP 1.65
  
• d1qgda2 appears in SCOP 1.67
  
• d1qgda2 appears in the current release, SCOPe 2.08