Class c: Alpha and beta proteins (a/b) [51349] (130 folds) |
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 |
Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (8 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 |
Family c.36.1.9: Pyruvate oxidase and decarboxylase PP module [88749] (7 proteins) the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology |
Protein Carboxyethylarginine synthase [102335] (1 species) |
Species Streptomyces clavuligerus [TaxId:1901] [102336] (3 PDB entries) |
Domain d1upca3: 1upc A:375-572 [99740] Other proteins in same PDB: d1upca1, d1upca2, d1upcb1, d1upcb2, d1upcc1, d1upcc2, d1upcd1, d1upcd2, d1upce1, d1upce2, d1upcf1, d1upcf2 |
PDB Entry: 1upc (more details), 2.45 Å
SCOP Domain Sequences for d1upca3:
Sequence; same for both SEQRES and ATOM records: (download)
>d1upca3 c.36.1.9 (A:375-572) Carboxyethylarginine synthase {Streptomyces clavuligerus} petyedgmrvhqvidsmntvmeeaaepgegtivsdigffrhygvlfaradqpfgfltsag cssfgygipaaigaqmarpdqptfliagdggfhsnssdletiarlnlpivtvvvnndtng lielyqnighhrshdpavkfggvdfvalaeangvdatratnreellaalrkgaelgrpfl ievpvnydfqpggfgals
Timeline for d1upca3: