Lineage for Protein: NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase

  1. Root: SCOP 1.71
  2. 570216Class c: Alpha and beta proteins (a/b) [51349] (134 folds)
  3. 576286Fold c.3: FAD/NAD(P)-binding domain [51904] (1 superfamily)
    core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander
  4. 576287Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (5 families) (S)
  5. 576622Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (15 proteins)
    duplication: both domains have similar folds and functions
    most members of the family contain common C-terminal alpha+beta domain
  6. 576784Protein NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase [82313] (1 species)

Species:

More info for Protein NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase from c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains

Timeline for Protein NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase from c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains:

  • Protein NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase from c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains first appeared in SCOP 1.63
  • Protein NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase from c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains appears in SCOP 1.69
  • Protein NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase from c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains appears in SCOP 1.73
  • Protein NADH-dependent 2-ketopropyl coenzyme M oxidoreductase/carboxylase from c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains last appears in SCOPe 2.07