ID   LUXS_VIBC1              Reviewed;         172 AA.
AC   Q9Z5X1; A7MYV6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 123.
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=VIBHAR_03484;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=9990077; DOI=10.1073/pnas.96.4.1639;
RA   Surette M.G., Miller M.B., Bassler B.L.;
RT   "Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio
RT   harveyi: a new family of genes responsible for autoinducer production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1639-1644(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) 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:0000269|PubMed:9990077}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABU72429.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF120098; AAD17292.1; -; Genomic_DNA.
DR   EMBL; CP000789; ABU72429.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_012128886.1; NC_022269.1.
DR   AlphaFoldDB; Q9Z5X1; -.
DR   SMR; Q9Z5X1; -.
DR   BindingDB; Q9Z5X1; -.
DR   ChEMBL; CHEMBL4682; -.
DR   KEGG; vha:VIBHAR_03484; -.
DR   PATRIC; fig|338187.25.peg.2716; -.
DR   BRENDA; 4.4.1.21; 6632.
DR   Proteomes; UP000008152; Chromosome I.
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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..172
FT                   /note="S-ribosylhomocysteine lyase"
FT                   /id="PRO_0000172275"
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   172 AA;  19143 MW;  2B36D46F68118E89 CRC64;
     MPLLDSFTVD HTRMNAPAVR VAKTMQTPKG DTITVFDLRF TAPNKDILSE KGIHTLEHLY
     AGFMRNHLNG DSVEIIDISP MGCRTGFYMS LIGTPSEQQV ADAWIAAMED VLKVENQNKI
     PELNEYQCGT AAMHSLDEAK QIAKNILEVG VAVNKNDELA LPESMLRELR ID
//