SCOP 1.71: Family c.1.12.7: Phosphoenolpyruvate mutase/Isocitrate lyase-like

Lineage for Family c.1.12.7: Phosphoenolpyruvate mutase/Isocitrate lyase-like

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (32 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] (6 families)

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

Proteins:

1. 2-methylisocitrate lyase [89499] (2 species)

   1. Species Escherichia coli [TaxId:562] [89500] (2 PDB entries)

   2. Species Salmonella typhimurium [TaxId:90371] [102099] (2 PDB entries)

2. Isocitrate lyase [51642] (3 species)
   elaborated with additional subdomains

   1. Species Aspergillus nidulans [TaxId:162425] [51643] (1 PDB entry)

   2. Species Escherichia coli [TaxId:562] [63923] (1 PDB entry)

   3. Species Mycobacterium tuberculosis [TaxId:1773] [51644] (3 PDB entries)

3. Phosphoenolpyruvate mutase [51636] (1 species)

   • Species Blue mussel (Mytilus edulis) [TaxId:6550] [51637] (6 PDB entries)

More info for Family c.1.12.7: Phosphoenolpyruvate mutase/Isocitrate lyase-like

Timeline for Family c.1.12.7: Phosphoenolpyruvate mutase/Isocitrate lyase-like:

• Family c.1.12.7: Phosphoenolpyruvate mutase/Isocitrate lyase-like first appeared in SCOP 1.65
  
• Family c.1.12.7: Phosphoenolpyruvate mutase/Isocitrate lyase-like appears in SCOP 1.69
  
• Family c.1.12.7: Phosphoenolpyruvate mutase/Isocitrate lyase-like appears in SCOP 1.73
  
• Family c.1.12.7: Phosphoenolpyruvate mutase/Isocitrate lyase-like appears in the current release, SCOPe 2.08