SCOPe 2.08: Protein: N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain

Lineage for Protein: N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain

Root: SCOPe 2.08
Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

Fold c.1: TIM beta/alpha-barrel [51350] (34 superfamilies)
contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
the first seven superfamilies have similar phosphate-binding sites

Superfamily c.1.9: Metallo-dependent hydrolases [51556] (19 families)
the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
has transition metal ions bound inside the barrel
Family c.1.9.10: N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain [82261] (1 protein)
automatically mapped to Pfam PF01979
Protein N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain [82262] (3 species)

Species:

Bacillus subtilis [TaxId:1423] [102086] (1 PDB entry)
- Domains for 2vhl:
  1. Domain d2vhla2: 2vhl A:58-358 [168610]
    Other proteins in same PDB: d2vhla1, d2vhlb1
    complexed with fe, glp, pge
  2. Domain d2vhlb2: 2vhl B:58-358 [168612]
    Other proteins in same PDB: d2vhla1, d2vhlb1
    complexed with fe, glp, pge
Escherichia coli [TaxId:562] [141808] (4 PDB entries)
Uniprot P0AF18 54-350
1. Domains for 1ymy:
  1. Domain d1ymya2: 1ymy A:54-350 [123709]
    Other proteins in same PDB: d1ymya1, d1ymyb1
  2. Domain d1ymyb2: 1ymy B:54-350 [123711]
    Other proteins in same PDB: d1ymya1, d1ymyb1
    automated match to d1ymya2
2. Domains for 1yrr:
  1. Domain d1yrra2: 1yrr A:54-350 [123936]
    Other proteins in same PDB: d1yrra1, d1yrrb1
    automated match to d1ymya2
    complexed with gol, po4
  2. Domain d1yrrb2: 1yrr B:54-350 [123938]
    Other proteins in same PDB: d1yrra1, d1yrrb1
    automated match to d1ymya2
    complexed with gol, po4
3. Domains for 2p50:
  1. Domain d2p50a2: 2p50 A:54-350 [149224]
    Other proteins in same PDB: d2p50a1, d2p50b1, d2p50c1, d2p50d1
    automated match to d1ymya2
    complexed with zn
  2. Domain d2p50b2: 2p50 B:54-350 [149226]
    Other proteins in same PDB: d2p50a1, d2p50b1, d2p50c1, d2p50d1
    automated match to d1ymya2
    complexed with zn
  3. Domain d2p50c2: 2p50 C:54-350 [149228]
    Other proteins in same PDB: d2p50a1, d2p50b1, d2p50c1, d2p50d1
    automated match to d1ymya2
    complexed with zn
  4. Domain d2p50d2: 2p50 D:54-350 [149230]
    Other proteins in same PDB: d2p50a1, d2p50b1, d2p50c1, d2p50d1
    automated match to d1ymya2
    complexed with zn
4. Domains for 2p53:
  1. Domain d2p53a2: 2p53 A:54-350 [149232]
    Other proteins in same PDB: d2p53a1, d2p53b1
    automatically matched to d1ymya2
    complexed with nng, zn; mutant
  2. Domain d2p53b2: 2p53 B:54-350 [149234]
    Other proteins in same PDB: d2p53a1, d2p53b1
    automatically matched to d1ymya2
    complexed with nng, zn; mutant
Thermotoga maritima [TaxId:2336] [82263] (1 PDB entry)
TM0814
- Domains for 1o12:
  1. Domain d1o12a2: 1o12 A:44-331 [80759]
    Other proteins in same PDB: d1o12a1, d1o12b1
    structural genomics
    CASP5
    complexed with fe
  2. Domain d1o12b2: 1o12 B:44-331 [80761]
    Other proteins in same PDB: d1o12a1, d1o12b1
    structural genomics
    CASP5
    complexed with fe

More info for Protein N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain from c.1.9.10: N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain

Timeline for Protein N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain from c.1.9.10: N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain:

Protein N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain from c.1.9.10: N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain first appeared in SCOP 1.63, called Protein N-acetylglucosamine-6-phosphate deacetylase, catalytic domain from c.1.9.10: N-acetylglucosamine-6-phosphate deacetylase, catalytic domain
Protein N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain from c.1.9.10: N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain appears in SCOPe 2.07