SCOP 1.75: Superfamily c.1.12: Phosphoenolpyruvate/pyruvate domain

Lineage for Superfamily c.1.12: Phosphoenolpyruvate/pyruvate domain

1. Root: SCOP 1.75

2. Class c: Alpha and beta proteins (a/b) [51349] (147 folds)

3. Fold 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. Superfamily c.1.12: Phosphoenolpyruvate/pyruvate domain [51621] (7 families)

Families:

1. c.1.12.1: Pyruvate kinase [51622] (1 protein)

2. c.1.12.2: Pyruvate phosphate dikinase, C-terminal domain [51629] (1 protein)

3. c.1.12.3: Phosphoenolpyruvate carboxylase [51632] (1 protein)

4. c.1.12.5: HpcH/HpaI aldolase [51638] (3 proteins)
   forms a swapped dimer; contains a PK-type metal-binding site

5. c.1.12.7: Phosphoenolpyruvate mutase/Isocitrate lyase-like [88704] (3 proteins)
   forms a swapped dimer

6. c.1.12.8: Ketopantoate hydroxymethyltransferase PanB [89503] (1 protein)

7. c.1.12.9: Mll9387-like [159416] (1 protein)
   Pfam PF09370; TIM-barrel signal transduction protein; forms a swapped dimer similar to the Phosphoenolpyruvate mutase/Isocitrate lyase-like and HpcH/HpaI aldolase families

More info for Superfamily c.1.12: Phosphoenolpyruvate/pyruvate domain

Timeline for Superfamily c.1.12: Phosphoenolpyruvate/pyruvate domain:

• Superfamily c.1.12: Phosphoenolpyruvate/pyruvate domain first appeared (with stable ids) in SCOP 1.55
  
• Superfamily c.1.12: Phosphoenolpyruvate/pyruvate domain appears in SCOP 1.73
  
• Superfamily c.1.12: Phosphoenolpyruvate/pyruvate domain appears in SCOPe 2.01
  
• Superfamily c.1.12: Phosphoenolpyruvate/pyruvate domain appears in the current release, SCOPe 2.08