Lineage for d1upab3 (1upa B:375-572)

  1. Root: SCOP 1.67
  2. 383641Class c: Alpha and beta proteins (a/b) [51349] (130 folds)
  3. 393047Fold 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. 393048Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (8 families) (S)
    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. 393191Family 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
  6. 393217Protein Carboxyethylarginine synthase [102335] (1 species)
  7. 393218Species Streptomyces clavuligerus [TaxId:1901] [102336] (3 PDB entries)
  8. 393220Domain d1upab3: 1upa B:375-572 [99719]
    Other proteins in same PDB: d1upaa1, d1upaa2, d1upab1, d1upab2, d1upac1, d1upac2, d1upad1, d1upad2

Details for d1upab3

PDB Entry: 1upa (more details), 2.35 Å

PDB Description: carboxyethylarginine synthase from streptomyces clavuligerus (semet structure)

SCOP Domain Sequences for d1upab3:

Sequence; same for both SEQRES and ATOM records: (download)

>d1upab3 c.36.1.9 (B:375-572) Carboxyethylarginine synthase {Streptomyces clavuligerus}
petyedgmrvhqvidsmntvmeeaaepgegtivsdigffrhygvlfaradqpfgfltsag
cssfgygipaaigaqmarpdqptfliagdggfhsnssdletiarlnlpivtvvvnndtng
lielyqnighhrshdpavkfggvdfvalaeangvdatratnreellaalrkgaelgrpfl
ievpvnydfqpggfgals

SCOP Domain Coordinates for d1upab3:

Click to download the PDB-style file with coordinates for d1upab3.
(The format of our PDB-style files is described here.)

Timeline for d1upab3: