SCOP 1.69: Domain d1o66a_: 1o66 A:

Lineage for d1o66a_ (1o66 A:)

1. Root: SCOP 1.69

2. Class c: Alpha and beta proteins (a/b) [51349] (136 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (31 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] (6 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 d1o66a_: 1o66 A: [92547]

Details for d1o66a_

PDB Entry: 1o66, 1.75 Å

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

SCOP Domain Sequences for d1o66a_:

Sequence, based on SEQRES records:

>d1o66a_ c.1.12.8 (A:) Ketopantoate hydroxymethyltransferase PanB {Neisseria meningitidis}
litvntlqkmkaagekiamltayessfaalmddagvemllvgdslgmavqgrkstlpvsl
rdmcyhtecvargaknamivsdlpfgayqqskeqafaaaaelmaagahmvkleggvwmae
tteflqmrgipvcahigltpqsvfafggykvqgrggkaqallndakahddagaavvlmec
vlaelakkvtetvscptigigagadcdgqvlvmhdmlgifpgktakfvknfmqghdsvqa
avrayvaevkaktfpaaehi

Sequence, based on observed residues (ATOM records):

>d1o66a_ c.1.12.8 (A:) Ketopantoate hydroxymethyltransferase PanB {Neisseria meningitidis}
litvntlqkmkaagekiamltayessfaalmddagvemllvgdslgmavqgrkstlpvsl
rdmcyhtecvargaknamivsdlpfgayqqskeqafaaaaelmaagahmvkleggvwmae
tteflqmrgipvcahigltpqsvfakaqallndakahddagaavvlmecvlaelakkvte
tvscptigigagadcdgqvlvmhdmlgifpgktakfvknfmqghdsvqaavrayvaevka
ktfpaaehi

Timeline for d1o66a_:

• d1o66a_ first appeared in SCOP 1.67
  
• d1o66a_ appears in SCOP 1.71
  
• d1o66a_ appears in the current release, SCOPe 2.08, called d1o66a1