SCOPe 2.08: Protein: Bacterial sepiapterin reductase

Lineage for Protein: Bacterial sepiapterin reductase

Root: SCOPe 2.08
Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

Fold c.2: NAD(P)-binding Rossmann-fold domains [51734] (1 superfamily)
core: 3 layers, a/b/a; parallel beta-sheet of 6 strands, order 321456
The nucleotide-binding modes of this and the next two folds/superfamilies are similar

Superfamily c.2.1: NAD(P)-binding Rossmann-fold domains [51735] (13 families)

Family c.2.1.2: Tyrosine-dependent oxidoreductases [51751] (73 proteins)
also known as short-chain dehydrogenases and SDR family
parallel beta-sheet is extended by 7th strand, order 3214567; left-handed crossover connection between strands 6 and 7
has additional subdomain(s) that are not in the common domain

Protein Bacterial sepiapterin reductase [141892] (1 species)

Species:

Chlorobium tepidum [TaxId:1097] [141893] (1 PDB entry)
Uniprot Q8KES3 2-241
CT0609
- Domains for 2bd0:
  1. Domain d2bd0a1: 2bd0 A:2-241 [128321]
    complexed with bio, nap
  2. Domain d2bd0b_: 2bd0 B: [128322]
    automated match to d2bd0a1
    complexed with bio, nap
  3. Domain d2bd0c_: 2bd0 C: [128323]
    automated match to d2bd0a1
    complexed with bio, nap
  4. Domain d2bd0d_: 2bd0 D: [128324]
    automated match to d2bd0a1
    complexed with bio, nap

More info for Protein Bacterial sepiapterin reductase from c.2.1.2: Tyrosine-dependent oxidoreductases

Timeline for Protein Bacterial sepiapterin reductase from c.2.1.2: Tyrosine-dependent oxidoreductases:

Protein Bacterial sepiapterin reductase from c.2.1.2: Tyrosine-dependent oxidoreductases first appeared in SCOP 1.73
Protein Bacterial sepiapterin reductase from c.2.1.2: Tyrosine-dependent oxidoreductases appears in SCOPe 2.07