SCOP 1.75: Domain d1o68d_: 1o68 D:

Lineage for d1o68d_ (1o68 D:)

1. Root: SCOP 1.75

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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] (7 families)

5. Family c.1.12.8: Ketopantoate hydroxymethyltransferase PanB [89503] (1 protein)

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 d1o68d_: 1o68 D: [92558]
   structural genomics

Details for d1o68d_

PDB Entry: 1o68, 2.1 Å

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

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

SCOP Domain Sequences for d1o68d_:

Sequence; same for both SEQRES and ATOM records:

>d1o68d_ c.1.12.8 (D:) Ketopantoate hydroxymethyltransferase PanB {Neisseria meningitidis [TaxId: 487]}
slitvntlqkmkaagekiamltayessfaalmddagvemllvgdslgmavqgrkstlpvs
lrdmcyhtecvargaknamivsdlpfgayqqskeqafaaaaelmaagahmvkleggvwma
etteflqmrgipvcahigltpqsvfafggykvqgrggkaqallndakahddagaavvlme
cvlaelakkvtetvscptigigagadcdgqvlvmhdmlgifpgktakfvknfmqghdsvq
aavrayvaevkaktfpaaehif

Timeline for d1o68d_:

• d1o68d_ first appeared in SCOP 1.67
  
• d1o68d_ appears in SCOP 1.73
  
• d1o68d_ appears in SCOPe 2.01
  
• d1o68d_ appears in the current release, SCOPe 2.08, called d1o68d1