SCOP 1.63: Domain d1o12a2: 1o12 A:44-331

Lineage for d1o12a2 (1o12 A:44-331)

1. Root: SCOP 1.63

2. Class c: Alpha and beta proteins (a/b) [51349] (117 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (26 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.1.9: Metallo-dependent hydrolases [51556] (12 families)
   the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
   has transition metal ions bound inside the barrel

5. Family c.1.9.10: N-acetylglucosamine-6-phosphate deacetylase, catalytic domain [82261] (1 protein)

6. Protein N-acetylglucosamine-6-phosphate deacetylase, catalytic domain [82262] (1 species)

7. Species Thermotoga maritima [TaxId:243274] [82263] (1 PDB entry)
   TM0814

8. Domain d1o12a2: 1o12 A:44-331 [80759]
   Other proteins in same PDB: d1o12a1, d1o12b1

Details for d1o12a2

PDB Entry: 1o12, 2.5 Å

PDB Description: crystal structure of n-acetylglucosamine-6-phosphate deacetylase (tm0814) from thermotoga maritima at 2.5 a resolution

SCOP Domain Sequences for d1o12a2:

Sequence; same for both SEQRES and ATOM records:

>d1o12a2 c.1.9.10 (A:44-331) N-acetylglucosamine-6-phosphate deacetylase, catalytic domain {Thermotoga maritima}
gfvdphihgvvgadtmncdfsemeeflysqgvttflattvstslekmkeilrkardyile
npstsllgvhlegpyiskekkgahsekhirppserelseidspakmltfapeiesselll
rlvkrdivlsaghsiatfeefmkfykegvkrithfpnglkplhhreigitgaglllddvk
lelicdgvhlsremvklvykvkkangivlvtdsisaaglkdgtttlgdlvvkvkdgvprl
edgtlagstlffsqavknfrkftgcsitelakvssynscvelglddrg

Timeline for d1o12a2:

• d1o12a2 is new in SCOP 1.63
  
• d1o12a2 appears in SCOP 1.65
  
• d1o12a2 appears in the current release, SCOPe 2.08