SCOPe 2.08: Domain d1yi1a2: 1yi1 A:86-280

Lineage for d1yi1a2 (1yi1 A:86-280)

1. Root: SCOPe 2.08

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.36.1.5: Pyruvate oxidase and decarboxylase Pyr module [88724] (8 proteins)
   the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology
   automatically mapped to Pfam PF02776

6. Protein Acetohydroxyacid synthase catalytic subunit [88733] (3 species)

7. Species Thale cress (Arabidopsis thaliana), chloroplast [TaxId:3702] [142204] (12 PDB entries)
   Uniprot P17597 86-280

8. Domain d1yi1a2: 1yi1 A:86-280 [123225]
   Other proteins in same PDB: d1yi1a1, d1yi1a3
   automated match to d1ybha2
   complexed with 1tb, fad, mg, nhe, p22

Details for d1yi1a2

PDB Entry: 1yi1, 2.9 Å

PDB Description: Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Tribenuron methyl

PDB Compounds: (A:) Acetolactate synthase

SCOPe Domain Sequences for d1yi1a2:

Sequence; same for both SEQRES and ATOM records:

>d1yi1a2 c.36.1.5 (A:86-280) Acetohydroxyacid synthase catalytic subunit {Thale cress (Arabidopsis thaliana), chloroplast [TaxId: 3702]}
tfisrfapdqprkgadilvealerqgvetvfaypggasmeihqaltrsssirnvlprheq
ggvfaaegyarssgkpgiciatsgpgatnlvsgladalldsvplvaitgqvprrmigtda
fqetpivevtrsitkhnylvmdvedipriieeafflatsgrpgpvlvdvpkdiqqqlaip
nweqamrlpgymsrm

Timeline for d1yi1a2:

• d1yi1a2 first appeared in SCOP 1.73
  
• d1yi1a2 appears in SCOPe 2.07