SCOPe 2.07: Domain d1o68d1: 1o68 D:2-261

Lineage for d1o68d1 (1o68 D:2-261)

1. Root: SCOPe 2.07

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

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.12: Phosphoenolpyruvate/pyruvate domain [51621] (8 families)

5. Family c.1.12.8: Ketopantoate hydroxymethyltransferase PanB [89503] (2 proteins)
   automatically mapped to Pfam PF02548

6. Protein Ketopantoate hydroxymethyltransferase PanB [89504] (3 species)
   dodecameric enzyme; a C-terminal helix exchange is observed in the M. tuberculosis enzyme but not in the E. coli enzyme

7. Species Neisseria meningitidis [TaxId:487] [102100] (2 PDB entries)

8. Domain d1o68d1: 1o68 D:2-261 [92558]
   Other proteins in same PDB: d1o68a2, d1o68b2, d1o68c2, d1o68d2, d1o68e2
   structural genomics
   complexed with kiv, na

Details for d1o68d1

PDB Entry: 1o68, 2.1 Å

PDB Description: crystal structure of 3-methyl-2-oxobutanoate hydroxymethyltransferase

PDB Compounds: (D:) 3-methyl-2-oxobutanoate hydroxymethyltransferase

SCOPe Domain Sequences for d1o68d1:

Sequence; same for both SEQRES and ATOM records:

>d1o68d1 c.1.12.8 (D:2-261) Ketopantoate hydroxymethyltransferase PanB {Neisseria meningitidis [TaxId: 487]}
itvntlqkmkaagekiamltayessfaalmddagvemllvgdslgmavqgrkstlpvslr
dmcyhtecvargaknamivsdlpfgayqqskeqafaaaaelmaagahmvkleggvwmaet
teflqmrgipvcahigltpqsvfafggykvqgrggkaqallndakahddagaavvlmecv
laelakkvtetvscptigigagadcdgqvlvmhdmlgifpgktakfvknfmqghdsvqaa
vrayvaevkaktfpaaehif

Timeline for d1o68d1:

• d1o68d1 first appeared in SCOP 1.67, called d1o68d_
  
• d1o68d1 appears in SCOPe 2.06
  
• d1o68d1 appears in the current release, SCOPe 2.08