ID   LUXS_SHIB3              Reviewed;         171 AA.
AC   B2U054;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=SbBS512_E3189;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) 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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; CP001063; ACD07481.1; -; Genomic_DNA.
DR   RefSeq; WP_001130216.1; NC_010658.1.
DR   AlphaFoldDB; B2U054; -.
DR   SMR; B2U054; -.
DR   STRING; 344609.SbBS512_E3189; -.
DR   EnsemblBacteria; ACD07481; ACD07481; SbBS512_E3189.
DR   KEGG; sbc:SbBS512_E3189; -.
DR   HOGENOM; CLU_107531_2_0_6; -.
DR   OMA; GPMGCLT; -.
DR   Proteomes; UP000001030; 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.
FT   CHAIN           1..171
FT                   /note="S-ribosylhomocysteine lyase"
FT                   /id="PRO_1000093329"
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;  19390 MW;  191F57F19C6DAAC2 CRC64;
     MPLLDSFTVD HTRMEAPAVR VAKTMNTPHG DAITVFDLRF CVPNKEVMPE RGSHTLEHLF
     AGFMRNHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV ADAWKAAMED VLKVQDQNQI
     PELNVYQCGT YQMHSLQEAQ DIARSILERD VRINSNEELA LPKEKLQELH I