SCOP 1.63: Domain d1tkca1: 1tkc A:3-337

Lineage for d1tkca1 (1tkc A:3-337)

1. Root: SCOP 1.63

2. Class c: Alpha and beta proteins (a/b) [51349] (117 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] (4 families)
   both pyridine (Pyr)- and pyrophosphate (PP)-binding modules have this fold
   conserved core consists of two Pyr and two PP-modules and binds two coenzyme molecules

5. Family c.36.1.2: TK-like THDP-binding domains [52528] (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 and Pyr modules [52529] (2 species)

7. Species Baker's yeast (Saccharomyces cerevisiae) [TaxId:4932] [52530] (7 PDB entries)

8. Domain d1tkca1: 1tkc A:3-337 [31811]
   Other proteins in same PDB: d1tkca3, d1tkcb3

Details for d1tkca1

PDB Entry: 1tkc, 2.7 Å

PDB Description: specificity of coenzyme binding in thiamin diphosphate dependent enzymes: crystal structures of yeast transketolase in complex with analogs of thiamin diphosphate

SCOP Domain Sequences for d1tkca1:

Sequence; same for both SEQRES and ATOM records:

>d1tkca1 c.36.1.2 (A:3-337) Transketolase (TK), PP and Pyr modules {Baker's yeast (Saccharomyces cerevisiae)}
qftdidklavstirilavdtvskansghpgaplgmapaahvlwsqmrmnptnpdwinrdr
fvlsnghavallysmlhltgydlsiedlkqfrqlgsrtpghpefelpgvevttgplgqgi
snavgmamaqanlaatynkpgftlsdnytyvflgdgclqegisseasslaghlklgnlia
iyddnkitidgatsisfdedvakryeaygwevlyvengnedlagiakaiaqaklskdkpt
likmtttigygslhagshsvhgaplkaddvkqlkskfgfnpdksfvvpqevydhyqktil
kpgveannkwnklfseyqkkfpelgaelarrlsgq

Timeline for d1tkca1:

• d1tkca1 first appeared (with stable ids) in SCOP 1.55
  
• d1tkca1 appears in SCOP 1.61
  
• d1tkca1 appears in SCOP 1.65
  
• d1tkca1 appears in the current release, SCOPe 2.08