Lineage for Protein: Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI

  1. Root: SCOP 1.63
  2. 235644Class c: Alpha and beta proteins (a/b) [51349] (117 folds)
  3. 242757Fold c.36: Thiamin diphosphate-binding fold (THDP-binding) [52517] (1 superfamily)
    3 layers: a/b/a; parallel beta-sheet of 6 strands, order 213465
  4. 242758Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (4 families) (S)
    both pyridine (Pyr)- and pyrophosphate (PP)-binding modules have this fold
    conserved core consists of two Pyr and two PP-modules and binds two coenzyme molecules
  5. 242896Family c.36.1.4: Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI [52536] (1 protein)
    domains VI, I and II are arranged in the same way as the TK PP, Pyr and C domains
  6. 242897Protein Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI [52537] (1 species)
    domain I is the Pyr module; domain VI is the PP module

Species:

More info for Protein Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI from c.36.1.4: Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI

Timeline for Protein Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI from c.36.1.4: Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI:

  • Protein Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI from c.36.1.4: Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI first appeared (with stable ids) in SCOP 1.55
  • Protein Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI from c.36.1.4: Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI appears in SCOP 1.61
  • Protein Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI from c.36.1.4: Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI does not appear in SCOP 1.65