ID   LUXS_CLOPE              Reviewed;         151 AA.
AC   Q9XDU6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=CPE0178;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=10692162; DOI=10.1046/j.1365-2958.2000.01760.x;
RA   Banu S., Ohtani K., Yaguchi H., Swe T., Cole S.T., Hayashi H., Shimizu T.;
RT   "Identification of novel VirR/VirS-regulated genes in Clostridium
RT   perfringens.";
RL   Mol. Microbiol. 35:854-864(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN   [3]
RP   FUNCTION.
RX   PubMed=11967077; DOI=10.1046/j.1365-2958.2002.02863.x;
RA   Ohtani K., Hayashi H., Shimizu T.;
RT   "The luxS gene is involved in cell-cell signalling for toxin production in
RT   Clostridium perfringens.";
RL   Mol. Microbiol. 44:171-179(2002).
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:0000269|PubMed:11967077}.
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; AB028629; BAA81641.1; -; Genomic_DNA.
DR   EMBL; BA000016; BAB79884.1; -; Genomic_DNA.
DR   PIR; T43793; T43793.
DR   RefSeq; WP_003452649.1; NC_003366.1.
DR   AlphaFoldDB; Q9XDU6; -.
DR   SMR; Q9XDU6; -.
DR   STRING; 195102.gene:10489422; -.
DR   EnsemblBacteria; BAB79884; BAB79884; BAB79884.
DR   KEGG; cpe:CPE0178; -.
DR   HOGENOM; CLU_107531_2_0_9; -.
DR   OMA; GPMGCLT; -.
DR   Proteomes; UP000000818; 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..151
FT                   /note="S-ribosylhomocysteine lyase"
FT                   /id="PRO_0000172217"
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         121
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   151 AA;  16932 MW;  F9564886EBF75561 CRC64;
     MVKVESFELD HTKVKAPYVR KAGIKIGPKG DIVSKFDLRF VQPNKELLSD KGMHTLEHFL
     AGFMREKLDD VIDISPMGCK TGFYLTSFGD IDVKDIIEAL EYSLSKVLEQ EEIPAANELQ
     CGSAKLHSLE LAKSHAKQVL ENGISDKFYV E