SCOPe 2.03: Domain d2ihvc1: 2ihv C:11-197

Lineage for d2ihvc1 (2ihv C:11-197)

1. Root: SCOPe 2.03

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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] (9 families)
   there are two different functional modules of this fold: pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules
   two Pyr and two PP modules assemble together in a conserved heterotetrameric core that binds two THDP coenzyme molecules

5. Family c.36.1.5: Pyruvate oxidase and decarboxylase Pyr module [88724] (8 proteins)
   the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology
   automatically mapped to Pfam PF02776

6. Protein Carboxyethylarginine synthase [102330] (1 species)

7. Species Streptomyces clavuligerus [TaxId:1901] [102331] (6 PDB entries)

8. Domain d2ihvc1: 2ihv C:11-197 [198074]
   Other proteins in same PDB: d2ihva1, d2ihva3, d2ihvb1, d2ihvb3, d2ihvc2, d2ihvc3, d2ihvd1, d2ihvd3
   automated match to d1upaa2
   complexed with gva, k, mg, tpp

Details for d2ihvc1

PDB Entry: 2ihv, 2.3 Å

PDB Description: carboxyethylarginine synthase from streptomyces clavuligerus: 5- guanidinovaleric acid complex

PDB Compounds: (C:) carboxyethylarginine synthase

SCOPe Domain Sequences for d2ihvc1:

Sequence; same for both SEQRES and ATOM records:

>d2ihvc1 c.36.1.5 (C:11-197) Carboxyethylarginine synthase {Streptomyces clavuligerus [TaxId: 1901]}
kptaahallsrlrdhgvgkvfgvvgreaasilfdevegidfvltrheftagvaadvlari
tgrpqacwatlgpgmtnlstgiatsvldrspvialaaqseshdifpndthqcldsvaiva
pmskyavelqrpheitdlvdsavnaamtepvgpsfislpvdllgssegidttvpnppant
pakpvgv

Timeline for d2ihvc1:

• d2ihvc1 is new in SCOPe 2.03-stable
  
• d2ihvc1 appears in SCOPe 2.04
  
• d2ihvc1 appears in the current release, SCOPe 2.08