ID LUXS_SODGM Reviewed; 171 AA. AC Q2NVK8; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 96. 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}; OrderedLocusNames=SG0542; OS Sodalis glossinidius (strain morsitans). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Bruguierivoracaceae; Sodalis. OX NCBI_TaxID=343509; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=morsitans; RX PubMed=16365377; DOI=10.1101/gr.4106106; RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., RA Aksoy S.; RT "Massive genome erosion and functional adaptations provide insights into RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host."; RL Genome Res. 16:149-156(2006). 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; AP008232; BAE73817.1; -; Genomic_DNA. DR RefSeq; WP_011410515.1; NC_007712.1. DR AlphaFoldDB; Q2NVK8; -. DR SMR; Q2NVK8; -. DR STRING; 343509.SG0542; -. DR KEGG; sgl:SG0542; -. DR eggNOG; COG1854; Bacteria. DR HOGENOM; CLU_107531_2_0_6; -. DR OrthoDB; 9788129at2; -. DR BioCyc; SGLO343509:SGP1_RS04795-MONOMER; -. DR Proteomes; UP000001932; 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. FT CHAIN 1..171 FT /note="S-ribosylhomocysteine lyase" FT /id="PRO_0000298034" 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 128 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091" SQ SEQUENCE 171 AA; 19310 MW; EE3BA60D793AEACB CRC64; MPLLDSFTVD HTRMAAPAVR VAKTMKTPHG DTITVFDLRF CRPNLEVMPE RGIHTLEHLF AGFMRNHLNG EGVEIVDISP MGCRTGFYMS LIGAPEEQRV ADAWKAAMAD VLKVKDQKQI PELNEYQCGT YQMHSLTEAQ DIAQHILDNA IRVNQNDELT LPKEKLAELH I //