LUXS_SALEP
ID LUXS_SALEP Reviewed; 171 AA.
AC B5QV71;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=SEN2662;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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; AM933172; CAR34242.1; -; Genomic_DNA.
DR RefSeq; WP_001130194.1; NC_011294.1.
DR AlphaFoldDB; B5QV71; -.
DR SMR; B5QV71; -.
DR KEGG; set:SEN2662; -.
DR HOGENOM; CLU_107531_2_0_6; -.
DR OMA; GPMGCLT; -.
DR Proteomes; UP000000613; 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_1000093322"
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; 19308 MW; 359A88331FF56CDF CRC64;
MPLLDSFAVD HTRMQAPAVR VAKTMNTPHG DAITVFDLRF CIPNKEVMPE KGIHTLEHLF
AGFMRDHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV ADAWKAAMAD VLKVQDQNQI
PELNVYQCGT YQMHSLSEAQ DIARHILERD VRVNSNKELA LPKEKLQELH I