SCOPe 2.05: Domain d2ihvd3: 2ihv D:375-573

Lineage for d2ihvd3 (2ihv D:375-573)

1. Root: SCOPe 2.05

2. Class c: Alpha and beta proteins (a/b) [51349] (148 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.36.1.9: Pyruvate oxidase and decarboxylase PP module [88749] (8 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 Carboxyethylarginine synthase [102335] (1 species)

7. Species Streptomyces clavuligerus [TaxId:1901] [102336] (6 PDB entries)

8. Domain d2ihvd3: 2ihv D:375-573 [147708]
   Other proteins in same PDB: d2ihva1, d2ihva2, d2ihvb1, d2ihvb2, d2ihvc1, d2ihvc2, d2ihvd1, d2ihvd2
   automated match to d1upaa3
   complexed with gva, k, mg, tpp

Details for d2ihvd3

PDB Entry: 2ihv, 2.3 Å

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

PDB Compounds: (D:) carboxyethylarginine synthase

SCOPe Domain Sequences for d2ihvd3:

Sequence; same for both SEQRES and ATOM records:

>d2ihvd3 c.36.1.9 (D:375-573) Carboxyethylarginine synthase {Streptomyces clavuligerus [TaxId: 1901]}
petyedgmrvhqvidsmntvmeeaaepgegtivsdigffrhygvlfaradqpfgfltsag
cssfgygipaaigaqmarpdqptfliagdggfhsnssdletiarlnlpivtvvvnndtng
lielyqnighhrshdpavkfggvdfvalaeangvdatratnreellaalrkgaelgrpfl
ievpvnydfqpggfgalsi

Timeline for d2ihvd3:

• d2ihvd3 first appeared in SCOP 1.75
  
• d2ihvd3 appears in SCOPe 2.04
  
• d2ihvd3 appears in SCOPe 2.06
  
• d2ihvd3 appears in the current release, SCOPe 2.08