ID LUXS_SHOC1 Reviewed; 156 AA. AC Q5WDW1; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=S-ribosylhomocysteine lyase {ECO:0000255|HAMAP-Rule:MF_00091}; DE EC=4.4.1.21 {ECO:0000255|HAMAP-Rule:MF_00091}; DE AltName: Full=AI-2 synthesis protein {ECO:0000255|HAMAP-Rule:MF_00091}; DE AltName: Full=Autoinducer-2 production protein LuxS {ECO:0000255|HAMAP-Rule:MF_00091}; GN Name=luxS {ECO:0000255|HAMAP-Rule:MF_00091}; GN OrderedLocusNames=ABC2915; OS Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella. OX NCBI_TaxID=66692; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16; RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., RA Kawai S., Ito S., Horikoshi K.; RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM- RT K16."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the synthesis of autoinducer 2 (AI-2) which is CC secreted by bacteria and is used to communicate both the cell density CC and the metabolic potential of the environment. The regulation of gene CC expression in response to changes in cell density is called quorum CC sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to CC homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). CC {ECO:0000255|HAMAP-Rule:MF_00091}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5- CC dihydroxypentane-2,3-dione + L-homocysteine; Xref=Rhea:RHEA:17753, CC ChEBI:CHEBI:29484, ChEBI:CHEBI:58195, ChEBI:CHEBI:58199; EC=4.4.1.21; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00091}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00091}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000255|HAMAP-Rule:MF_00091}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00091}. CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000255|HAMAP- CC Rule:MF_00091}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP006627; BAD65449.1; -; Genomic_DNA. DR RefSeq; WP_011247757.1; NC_006582.1. DR AlphaFoldDB; Q5WDW1; -. DR SMR; Q5WDW1; -. DR STRING; 66692.ABC2915; -. DR KEGG; bcl:ABC2915; -. DR eggNOG; COG1854; Bacteria. DR HOGENOM; CLU_107531_2_0_9; -. DR OrthoDB; 9788129at2; -. DR BRENDA; 4.4.1.21; 7525. DR Proteomes; UP000001168; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0043768; F:S-ribosylhomocysteine lyase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.1360.80; S-ribosylhomocysteinase (LuxS); 1. DR HAMAP; MF_00091; LuxS; 1. DR InterPro; IPR037005; LuxS_sf. DR InterPro; IPR011249; Metalloenz_LuxS/M16. DR InterPro; IPR003815; S-ribosylhomocysteinase. DR PANTHER; PTHR35799; S-RIBOSYLHOMOCYSTEINE LYASE; 1. DR PANTHER; PTHR35799:SF1; S-RIBOSYLHOMOCYSTEINE LYASE; 1. DR Pfam; PF02664; LuxS; 1. DR PIRSF; PIRSF006160; AI2; 1. DR PRINTS; PR01487; LUXSPROTEIN. DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 1. PE 3: Inferred from homology; KW Autoinducer synthesis; Iron; Lyase; Metal-binding; Quorum sensing; KW Reference proteome. FT CHAIN 1..156 FT /note="S-ribosylhomocysteine lyase" FT /id="PRO_0000172210" FT BINDING 54 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091" FT BINDING 58 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091" FT BINDING 126 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091" SQ SEQUENCE 156 AA; 17629 MW; 9C38B441A23D8606 CRC64; MPSVESFELD HTIVKAPYVR HCGKHKIGSD GEVNKFDIRF CQPNKEALKP GVIHTLEHLL AINIRRFSEE YDHFDVIDIS PMGCQTGYYL IMSGTPSVEE IIDVLEKTMT YSLSIETVPA ATEKECGQAA LHDLEGTKEV MRKWLSEDKG SLKQVF //