Lineage for Species: Alcaligenes faecalis
- Root: SCOP 1.63
Class c: Alpha and beta proteins (a/b) [51349] (117 folds) 
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
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
Family c.1.9.11: D-aminoacylase, catalitic domain [82264] (1 protein) Protein N-acyl-D-aminoacid amidohydrolase, catalytic domain [82265] (1 species)
contains small a/b subdomain inserted after strand 7; unusual for the superfamily metal coordination by CysSpecies Alcaligenes faecalis [TaxId:511] [82266] (1 PDB entry)
PDB entry in Species: Alcaligenes faecalis:
- Domain(s) for 1m7j:
Domain d1m7ja3: 1m7j A:62-419 [78734]
Other proteins in same PDB: d1m7ja1, d1m7ja2
complexed with act, zn
More info for Species Alcaligenes faecalis [TaxId:511] from c.1.9.11 N-acyl-D-aminoacid amidohydrolase, catalytic domain
Timeline for Species Alcaligenes faecalis [TaxId:511] from c.1.9.11 N-acyl-D-aminoacid amidohydrolase, catalytic domain:
- Species Alcaligenes faecalis [TaxId:511] from c.1.9.11 N-acyl-D-aminoacid amidohydrolase, catalytic domain is new in SCOP 1.63
- Species Alcaligenes faecalis [TaxId:511] from c.1.9.11 N-acyl-D-aminoacid amidohydrolase, catalytic domain appears in SCOP 1.65
- Species Alcaligenes faecalis [TaxId:511] from c.1.9.11 N-acyl-D-aminoacid amidohydrolase, catalytic domain appears in the current release, SCOPe 2.08