Lineage for Protein: AMP deaminase (AMPD), catalytic domain

  1. Root: SCOP 1.73
  2. 681097Class c: Alpha and beta proteins (a/b) [51349] (141 folds)
  3. 681098Fold 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. 683612Superfamily c.1.9: Metallo-dependent hydrolases [51556] (15 families) (S)
    the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
    has transition metal ions bound inside the barrel
  5. 683613Family c.1.9.1: Adenosine/AMP deaminase [51557] (2 proteins)
  6. 683656Protein AMP deaminase (AMPD), catalytic domain [141800] (1 species)
    elaborated fold with additional structures

Species:

More info for Protein AMP deaminase (AMPD), catalytic domain from c.1.9.1: Adenosine/AMP deaminase

Timeline for Protein AMP deaminase (AMPD), catalytic domain from c.1.9.1: Adenosine/AMP deaminase:

  • Protein AMP deaminase (AMPD), catalytic domain from c.1.9.1: Adenosine/AMP deaminase is new in SCOP 1.73
  • Protein AMP deaminase (AMPD), catalytic domain from c.1.9.1: Adenosine/AMP deaminase appears in SCOP 1.75
  • Protein AMP deaminase (AMPD), catalytic domain from c.1.9.1: Adenosine/AMP deaminase appears in the current release, SCOPe 2.08