SCOPe 2.07: Domain d2ihub3: 2ihu B:375-562

Lineage for d2ihub3 (2ihu B:375-562)

1. Root: SCOPe 2.07

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 d2ihub3: 2ihu B:375-562 [198067]
   Other proteins in same PDB: d2ihua1, d2ihua2, d2ihub1, d2ihub2, d2ihuc1, d2ihuc2, d2ihud1, d2ihud2
   automated match to d1upaa3
   complexed with gol, k, mg, tar, tp8, tp9

Details for d2ihub3

PDB Entry: 2ihu, 2.05 Å

PDB Description: Carboxyethylarginine synthase from Streptomyces clavuligerus: putative reaction intermediate complex

PDB Compounds: (B:) carboxyethylarginine synthase

SCOPe Domain Sequences for d2ihub3:

Sequence; same for both SEQRES and ATOM records:

>d2ihub3 c.36.1.9 (B:375-562) Carboxyethylarginine synthase {Streptomyces clavuligerus [TaxId: 1901]}
petyedgmrvhqvidsmntvmeeaaepgegtivsdigffrhygvlfaradqpfgfltsag
cssfgygipaaigaqmarpdqptfliagdggfhsnssdletiarlnlpivtvvvnndtng
lielyqnighhrshdpavkfggvdfvalaeangvdatratnreellaalrkgaelgrpfl
ievpvnyd

Timeline for d2ihub3:

• d2ihub3 first appeared in SCOPe 2.03
  
• d2ihub3 appears in SCOPe 2.06
  
• d2ihub3 appears in the current release, SCOPe 2.08