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   03-AUG-2022, entry version 111.
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; Proteobacteria; 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}.
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DR   EMBL; AE004439; AAK03138.1; -; Genomic_DNA.
DR   RefSeq; WP_005717368.1; NC_002663.1.
DR   AlphaFoldDB; P57901; -.
DR   SMR; P57901; -.
DR   STRING; 747.DR93_914; -.
DR   EnsemblBacteria; AAK03138; AAK03138; PM1054.
DR   KEGG; pmu:PM1054; -.
DR   HOGENOM; CLU_107531_2_0_6; -.
DR   OMA; GPMGCLT; -.
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; -; 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; PTHR35799; 1.
DR   Pfam; PF02664; LuxS; 1.
DR   PIRSF; PIRSF006160; AI2; 1.
DR   PRINTS; PR01487; LUXSPROTEIN.
DR   SUPFAM; SSF63411; SSF63411; 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