Lineage for Fold c.1: TIM beta/alpha-barrel

  1. Root: SCOPe 2.06
  2. 2078559Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2078560Fold 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

Superfamilies:

  1. 2078561c.1.1: Triosephosphate isomerase (TIM) [51351] (2 families) (S)
  2. 2079053c.1.2: Ribulose-phoshate binding barrel [51366] (7 families) (S)
  3. 2079968c.1.3: Thiamin phosphate synthase [51391] (2 families) (S)
    automatically mapped to Pfam PF02581
  4. 2080000c.1.4: FMN-linked oxidoreductases [51395] (2 families) (S)
  5. 2080656c.1.5: Inosine monophosphate dehydrogenase (IMPDH) [51412] (2 families) (S)
    The phosphate moiety of substrate binds in the 'common' phosphate-binding site
  6. 2080829c.1.6: PLP-binding barrel [51419] (2 families) (S)
    circular permutation of the canonical fold: begins with an alpha helix and ends with a beta-strand
  7. 2080913c.1.7: NAD(P)-linked oxidoreductase [51430] (2 families) (S)
  8. 2081496c.1.8: (Trans)glycosidases [51445] (15 families) (S)
  9. 2084338c.1.9: Metallo-dependent hydrolases [51556] (19 families) (S)
    the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
    has transition metal ions bound inside the barrel
  10. 2085156c.1.10: Aldolase [51569] (9 families) (S)
    Common fold covers whole protein structure
  11. 2086988c.1.11: Enolase C-terminal domain-like [51604] (3 families) (S)
    binds metal ion (magnesium or manganese) in conserved site inside barrel
    N-terminal alpha+beta domain is common to this superfamily
  12. 2088020c.1.12: Phosphoenolpyruvate/pyruvate domain [51621] (8 families) (S)
  13. 2088435c.1.13: Malate synthase G [51645] (1 family) (S)
  14. 2088460c.1.14: RuBisCo, C-terminal domain [51649] (2 families) (S)
    automatically mapped to Pfam PF00016
  15. 2088839c.1.15: Xylose isomerase-like [51658] (8 families) (S)
    different families share similar but non-identical metal-binding sites
  16. 2089162c.1.16: Bacterial luciferase-like [51679] (5 families) (S)
    consists of clearly related families of somewhat different folds
  17. 2089241c.1.17: Nicotinate/Quinolinate PRTase C-terminal domain-like [51690] (3 families) (S)
    incomplete beta/alpha barrel with parallel beta-sheet of 7 strands
  18. 2089342c.1.18: PLC-like phosphodiesterases [51695] (4 families) (S)
  19. 2089476c.1.19: Cobalamin (vitamin B12)-dependent enzymes [51703] (4 families) (S)
  20. 2089551c.1.20: tRNA-guanine transglycosylase [51713] (1 family) (S)
  21. 2089689c.1.21: Dihydropteroate synthetase-like [51717] (3 families) (S)
  22. 2089841c.1.22: UROD/MetE-like [51726] (3 families) (S)
  23. 2089931c.1.23: FAD-linked oxidoreductase [51730] (2 families) (S)
    distinct cofactor-binding mode from both FMN- and NAD(P)-linked TIM-barrel oxidoreductases; families are related by a circular permutation
  24. 2089999c.1.24: Pyridoxine 5'-phosphate synthase [63892] (2 families) (S)
  25. 2090064c.1.25: Monomethylamine methyltransferase MtmB [75098] (1 family) (S)
    automatically mapped to Pfam PF05369
  26. 2090074c.1.26: Homocysteine S-methyltransferase [82282] (1 family) (S)
  27. 2090111c.1.27: (2r)-phospho-3-sulfolactate synthase ComA [102110] (1 family) (S)
    automatically mapped to Pfam PF02679
  28. 2090118c.1.28: Radical SAM enzymes [102114] (3 families) (S)
    common Fe-S cluster and SAM binding sites are embedded into complete or incomplete beta/alpha-barrel
  29. 2090139c.1.29: GlpP-like [110391] (1 family) (S)
    automatically mapped to Pfam PF04309
  30. 2090147c.1.30: CutC-like [110395] (2 families) (S)
    automatically mapped to Pfam PF03932
  31. 2090174c.1.31: ThiG-like [110399] (2 families) (S)
    shares the common phosphate-binding site with other superfamilies
  32. 2090198c.1.32: TM1631-like [117396] (1 family) (S)
    automatically mapped to Pfam PF01904
  33. 2090210c.1.33: EAL domain-like [141868] (1 family) (S)
    variant of the beta/alpha-barrel fold with strand 1 being antiparallel to the rest
    automatically mapped to Pfam PF00563

More info for Fold c.1: TIM beta/alpha-barrel

Timeline for Fold c.1: TIM beta/alpha-barrel: