SCOP 1.73: Domain d2fqta1: 2fqt A:4-157

Lineage for d2fqta1 (2fqt A:4-157)

1. Root: SCOP 1.73

2. Class d: Alpha and beta proteins (a+b) [53931] (334 folds)

3. Fold d.185: LuxS/MPP-like metallohydrolase [63410] (1 superfamily)
   core: beta-alpha-beta(2)-alpha(2); 2 layers: alpha/beta

4. Superfamily d.185.1: LuxS/MPP-like metallohydrolase [63411] (2 families)
   Share the same "active site motif" HxxEH located in the first core helix, but differ in one of the zinc-binding residues

5. Family d.185.1.2: Autoinducer-2 production protein LuxS [64294] (1 protein)
   contains additional N-terminal strand; possible relationships to the putative editing domain of ThrRS (d.67.1)

6. Protein Autoinducer-2 production protein LuxS [64295] (4 species)
   S-ribosylhomocysteinase

7. Species Bacillus subtilis [TaxId:1423] [64296] (6 PDB entries)

8. Domain d2fqta1: 2fqt A:4-157 [133958]
   automatically matched to d1ie0a_
   complexed with co, h1d, so4

Details for d2fqta1

PDB Entry: 2fqt, 1.79 Å

PDB Description: Crystal structure of B.subtilis LuxS in complex with (2S)-2-Amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoyl-propylmercapto]butyric acid

PDB Compounds: (A:) S-ribosylhomocysteine lyase

SCOP Domain Sequences for d2fqta1:

Sequence; same for both SEQRES and ATOM records:

>d2fqta1 d.185.1.2 (A:4-157) Autoinducer-2 production protein LuxS {Bacillus subtilis [TaxId: 1423]}
vesfeldhnavvapyvrhcgvhkvgtdgvvnkfdirfcqpnkqamkpdtihtlehllaft
irshaekydhfdiidispmgcqtgyylvvsgeptsaeivdlledtmkeaveiteipaane
kqcgqaklhdlegakrlmrfwlsqdkeellkvfg

Timeline for d2fqta1:

• d2fqta1 is new in SCOP 1.73
  
• d2fqta1 appears in SCOP 1.75
  
• d2fqta1 appears in the current release, SCOPe 2.08, called d2fqta_