Structural Classification of Proteins
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Family: Formate dehydrogenase/DMSO reductase, C-terminal domain

molybdopterine enzyme

Lineage:

  1. Root: scop
  2. Class: All beta proteins [48724]
  3. Fold: Double psi beta-barrel [50684]
    barrel, closed; n=6, S=10; complex topology with crossover (psi) loops
  4. Superfamily: ADC-like [50692]
    link to SUPERFAMILY database - Superfamily
  5. Family: Formate dehydrogenase/DMSO reductase, C-terminal domain [50696]
    molybdopterine enzyme

Protein Domains:

  1. Dimethylsulfoxide reductase (DMSO reductase) [50697]
    1. Rhodobacter sphaeroides [TaxId: 1063] [50698] (1) picpic
    2. Rhodobacter capsulatus [TaxId: 1061] [50699] (10) picpic
  2. Formate dehydrogenase H [50700]
    1. Escherichia coli [TaxId: 562] [50701] (4) picpic
  3. Formate dehydrogenase N, alpha subunit [74987]
    1. Escherichia coli [TaxId: 562] [74988] (2) picpic
  4. Tungsten containing formate dehydrogenase, large subunit [82138]
    1. Desulfovibrio gigas [TaxId: 879] [82139] (1) picpic
  5. Trimethylamine N-oxide reductase [50702]
    1. Shewanella massilia [TaxId: 76854] [50703] (1) picpic
  6. Arsenite oxidase large subunit [50704]
    1. Alcaligenes faecalis [TaxId: 511] [50705] (2) picpic
  7. Periplasmic nitrate reductase alpha chain, NapA [50706]
    1. Desulfovibrio desulfuricans [TaxId: 876] [50707] (8) picpic
      dissimilatory nitrate reductase (NAP)
    2. Rhodobacter sphaeroides [TaxId: 1063] [101827] (1) picpic
  8. Respiratory nitrate reductase 1 alpha chain [101828]
    1. Escherichia coli [TaxId: 562] [101829] (7) picpic
      SQ P09152
  9. Transhydroxylase alpha subunit, AthL [110250]
    1. Pelobacter acidigallici [TaxId: 35816] [110251] (6) picpic
      SQ P80563
  10. NADH-quinone oxidoreductase chain 3, Nqo3, C-terminal domain [141393]
    topoisomer of the common fold, lacking the second psi loop
    1. Thermus thermophilus [TaxId: 274] [141394] (4) picpic
      SQ Q56223 686-767
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MRC site Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright © 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk