SCOPe 2.05: Superfamily d.185.1: LuxS/MPP-like metallohydrolase

Lineage for Superfamily d.185.1: LuxS/MPP-like metallohydrolase

1. Root: SCOPe 2.05

2. Class d: Alpha and beta proteins (a+b) [53931] (381 folds)

3. Fold d.185: LuxS/MPP-like metallohydrolase [63410] (1 superfamily)
   core: beta-alpha-beta(2)-alpha(2); 2 layers: alpha/beta

4. Superfamily d.185.1: LuxS/MPP-like metallohydrolase [63411] (3 families)
   Share the same "active site motif" HxxEH located in the first core helix, but differ in one of the zinc-binding residues

Families:

1. d.185.1.1: MPP-like [63412] (7 proteins)
   Common fold elaborated with many additional structures; duplication: each family member consists of two similar domains of beta(2)-alpha(2)-beta(2)-alpha(5)-beta structure, but only the N-terminal domain of MPP beta chain binds the catalytic metal

2. d.185.1.2: Autoinducer-2 production protein LuxS [64294] (1 protein)
   contains additional N-terminal strand; possible relationships to the putative editing domain of ThrRS (d.67.1)
   automatically mapped to Pfam PF02664

3. d.185.1.0: automated matches [232765] (1 protein)
   not a true family

More info for Superfamily d.185.1: LuxS/MPP-like metallohydrolase

Timeline for Superfamily d.185.1: LuxS/MPP-like metallohydrolase:

• Superfamily d.185.1: LuxS/MPP-like metallohydrolase first appeared in SCOP 1.57
  
• Superfamily d.185.1: LuxS/MPP-like metallohydrolase appears in SCOPe 2.04
  
• Superfamily d.185.1: LuxS/MPP-like metallohydrolase appears in SCOPe 2.06
  
• Superfamily d.185.1: LuxS/MPP-like metallohydrolase appears in the current release, SCOPe 2.08