SCOP 1.63: Domain d1mczc3: 1mcz C:342-525

Lineage for d1mczc3 (1mcz C:342-525)

1. Root: SCOP 1.63

2. Class c: Alpha and beta proteins (a/b) [51349] (117 folds)

3. Fold 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. Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (4 families)
   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. Family c.36.1.1: Pyruvate oxidase and decarboxylase THDP-binding domains [52519] (4 proteins)
   the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology

6. Protein Benzoylformate decarboxylase [52526] (1 species)

7. Species Pseudomonas putida [TaxId:303] [52527] (2 PDB entries)

8. Domain d1mczc3: 1mcz C:342-525 [78960]
   Other proteins in same PDB: d1mcza1, d1mczb1, d1mczc1, d1mczd1, d1mcze1, d1mczf1, d1mczg1, d1mczh1, d1mczi1, d1mczj1, d1mczk1, d1mczl1, d1mczm1, d1mczn1, d1mczo1, d1mczp1

Details for d1mczc3

PDB Entry: 1mcz, 2.8 Å

PDB Description: benzoylformate decarboxylase from pseudomonas putida complexed with an inhibitor, r-mandelate

SCOP Domain Sequences for d1mczc3:

Sequence; same for both SEQRES and ATOM records:

>d1mczc3 c.36.1.1 (C:342-525) Benzoylformate decarboxylase {Pseudomonas putida}
epakvdqdagrlhpetvfdtlndmapenaiylneststtaqmwqrlnmrnpgsyyfcaag
glgfalpaaigvqlaeperqviavigdgsanysisalwtaaqyniptifvimnngtygal
rwfagvleaenvpgldvpgidfralakgygvqalkadnleqlkgslqealsakgpvliev
stvs

Timeline for d1mczc3:

• d1mczc3 is new in SCOP 1.63
  
• d1mczc3 appears in SCOP 1.65
  
• d1mczc3 appears in the current release, SCOPe 2.08