SCOPe 2.07: Domain d5i5ea1: 5i5e A:2-334

Lineage for d5i5ea1 (5i5e A:2-334)

1. Root: SCOPe 2.07

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.36.1.0: automated matches [227300] (1 protein)
   not a true family

6. Protein automated matches [227126] (21 species)
   not a true protein

7. Species Scheffersomyces stipitis [TaxId:322104] [328848] (23 PDB entries)

8. Domain d5i5ea1: 5i5e A:2-334 [329958]
   Other proteins in same PDB: d5i5ea3
   automated match to d1ay0a1
   complexed with 5sp, ca, tpp; mutant

Details for d5i5ea1

PDB Entry: 5i5e, 1.62 Å

PDB Description: crystal structure of transketolase mutants-h66/261c complex with xylulose-5-phoaphate from pichia stipitis

PDB Compounds: (A:) transketolase

SCOPe Domain Sequences for d5i5ea1:

Sequence; same for both SEQRES and ATOM records:

>d5i5ea1 c.36.1.0 (A:2-334) automated matches {Scheffersomyces stipitis [TaxId: 322104]}
ssvdqkaistirllavdavaaansghpgaplglapaahavfkkmrfnpkdtkwinrdrfv
lsngcacallysmlvlygydltvedlkkfrqlgsktpghpentdvpgaevttgplgqgic
ngvgialaqaqfaatynkpdfpisdsytyvflgdgclmegvsseasslaghlqlgnliaf
wddnkisidgstevaftedviaryksygwhivevsdadtditaiaaaideakkvtnkptl
vrltttigfgslaqgthgvcgaplkaddikqlktkwgfnpeesfavpaevtasynehvae
nqkiqqqwnelfaaykqkypelgaelqrrldgk

Timeline for d5i5ea1:

• d5i5ea1 first appeared in SCOPe 2.06