ID LUXS_PASMU Reviewed; 168 AA. AC P57901; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=S-ribosylhomocysteine lyase; DE EC=4.4.1.21; DE AltName: Full=AI-2 synthesis protein; DE AltName: Full=Autoinducer-2 production protein LuxS; GN Name=luxS; OrderedLocusNames=PM1054; OS Pasteurella multocida (strain Pm70). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=272843; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pm70; RX PubMed=11248100; DOI=10.1073/pnas.051634598; RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.; RT "Complete genomic sequence of Pasteurella multocida Pm70."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001). 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) (By CC similarity). {ECO:0000250}. 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 -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000305}. 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; AE004439; AAK03138.1; -; Genomic_DNA. DR RefSeq; WP_005717368.1; NC_002663.1. DR AlphaFoldDB; P57901; -. DR SMR; P57901; -. DR STRING; 272843.PM1054; -. DR EnsemblBacteria; AAK03138; AAK03138; PM1054. DR GeneID; 77206370; -. DR KEGG; pmu:PM1054; -. DR HOGENOM; CLU_107531_2_0_6; -. DR OrthoDB; 9788129at2; -. DR Proteomes; UP000000809; 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..168 FT /note="S-ribosylhomocysteine lyase" FT /id="PRO_0000172242" FT BINDING 54 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 58 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 128 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" SQ SEQUENCE 168 AA; 18806 MW; 0B32EBBF99E7DC7C CRC64; MPLLDSFKVD HTRMKAPAVR IAKTMTTPKG DNITVFDLRF CIPNKEILSP KGIHTLEHLF AGFMRDHLNG TEVEIIDISP MGCRTGFYMS LIGTPNEQQV ADAWLASMRD VLLVKDQAQI PELNAFQCGT YTEHSLAEAQ QIAHNVLERG VSVNKNEDLL LDEQLLSL //