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.36.1.5: Pyruvate oxidase and decarboxylase Pyr module [88724] (7 proteins) the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology |
Protein Carboxyethylarginine synthase [102330] (1 species) |
Species Streptomyces clavuligerus [TaxId:1901] [102331] (3 PDB entries) |
Domain d1upad2: 1upa D:12-197 [99724] Other proteins in same PDB: d1upaa1, d1upaa3, d1upab1, d1upab3, d1upac1, d1upac3, d1upad1, d1upad3 complexed with mg, so4, tpp |
PDB Entry: 1upa (more details), 2.35 Å
SCOP Domain Sequences for d1upad2:
Sequence, based on SEQRES records: (download)
>d1upad2 c.36.1.5 (D:12-197) Carboxyethylarginine synthase {Streptomyces clavuligerus} ptaahallsrlrdhgvgkvfgvvgreaasilfdevegidfvltrheftagvaadvlarit grpqacwatlgpgmtnlstgiatsvldrspvialaaqseshdifpndthqcldsvaivap mskyavelqrpheitdlvdsavnaamtepvgpsfislpvdllgssegidttvpnppantp akpvgv
>d1upad2 c.36.1.5 (D:12-197) Carboxyethylarginine synthase {Streptomyces clavuligerus} ptaahallsrlrdhgvgkvfgvvgreaasilfdevegidfvltrheftagvaadvlarit grpqacwatlgpgmtnlstgiatsvldrspvialaaqseshdifpndthqcldsvaivap mskyavelqrpheitdlvdsavnaamtepvgpsfislpvdllgssegidtnppantpakp vgv
Timeline for d1upad2: