SCOP 1.65: Domain d1trka2: 1trk A:338-534

Lineage for d1trka2 (1trk A:338-534)

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.36.1.6: TK-like Pyr module [88735] (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), Pyr module [88736] (3 species)

7. Species Baker's yeast (Saccharomyces cerevisiae) [TaxId:4932] [88737] (7 PDB entries)

8. Domain d1trka2: 1trk A:338-534 [31804]
   Other proteins in same PDB: d1trka1, d1trka3, d1trkb1, d1trkb3

Details for d1trka2

PDB Entry: 1trk, 2 Å

PDB Description: refined structure of transketolase from saccharomyces cerevisiae at 2.0 angstroms resolution

SCOP Domain Sequences for d1trka2:

Sequence; same for both SEQRES and ATOM records:

>d1trka2 c.36.1.6 (A:338-534) Transketolase (TK), Pyr module {Baker's yeast (Saccharomyces cerevisiae)}
lpanwesklptytakdsavatrklsetvledvynqlpeliggsadltpsnltrwkealdf
qppssgsgnysgryirygirehamgaimngisafganykpyggtflnfvsyaagavrlsa
lsghpviwvathdsigvgedgpthqpietlahfrslpniqvwrpadgnevsaayknsles
khtpsiialsrqnlpql

Timeline for d1trka2:

• d1trka2 first appeared (with stable ids) in SCOP 1.55
  
• d1trka2 appears in SCOP 1.63
  
• d1trka2 appears in SCOP 1.67
  
• d1trka2 appears in the current release, SCOPe 2.08