ID   LUXS_BACSU              Reviewed;         157 AA.
AC   O34667;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 152.
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; Synonyms=ytjB; OrderedLocusNames=BSU30670;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   COFACTOR, CHARACTERIZATION, AND MUTAGENESIS OF GLU-57 AND CYS-84.
RX   PubMed=12705835; DOI=10.1021/bi034289j;
RA   Zhu J., Dizin E., Hu X., Wavreille A.-S., Park J., Pei D.;
RT   "S-ribosylhomocysteinase (LuxS) is a mononuclear iron protein.";
RL   Biochemistry 42:4717-4726(2003).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
RX   PubMed=11601850; DOI=10.1006/jmbi.2001.5027;
RA   Ruzheinikov S.N., Das S.K., Sedelnikova S.E., Hartley A., Foster S.J.,
RA   Horsburgh M.J., Cox A.G., McCleod C.W., Mekhalfia A., Blackburn G.M.,
RA   Rice D.W., Baker P.J.;
RT   "The 1.2 A structure of a novel quorum-sensing protein, Bacillus subtilis
RT   LuxS.";
RL   J. Mol. Biol. 313:111-122(2001).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=11553770; DOI=10.1073/pnas.191223098;
RA   Hilgers M.T., Ludwig M.L.;
RT   "Crystal structure of the quorum-sensing protein LuxS reveals a catalytic
RT   metal site.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:11169-11174(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).
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;
CC         Evidence={ECO:0000269|PubMed:12705835};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:12705835};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000305}.
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DR   EMBL; AF008220; AAC00235.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15045.1; -; Genomic_DNA.
DR   PIR; A69994; A69994.
DR   RefSeq; NP_390945.1; NC_000964.3.
DR   RefSeq; WP_003219361.1; NZ_JNCM01000036.1.
DR   PDB; 1IE0; X-ray; 1.60 A; A=1-157.
DR   PDB; 1J98; X-ray; 1.20 A; A=1-157.
DR   PDB; 1JQW; X-ray; 2.30 A; A=1-157.
DR   PDB; 1JVI; X-ray; 2.20 A; A=1-157.
DR   PDB; 1YCL; X-ray; 1.80 A; A=2-157.
DR   PDB; 2FQO; X-ray; 1.87 A; A=1-157.
DR   PDB; 2FQT; X-ray; 1.79 A; A=1-157.
DR   PDBsum; 1IE0; -.
DR   PDBsum; 1J98; -.
DR   PDBsum; 1JQW; -.
DR   PDBsum; 1JVI; -.
DR   PDBsum; 1YCL; -.
DR   PDBsum; 2FQO; -.
DR   PDBsum; 2FQT; -.
DR   AlphaFoldDB; O34667; -.
DR   SMR; O34667; -.
DR   STRING; 224308.BSU30670; -.
DR   BindingDB; O34667; -.
DR   ChEMBL; CHEMBL5171; -.
DR   DrugBank; DB04182; (S)-2-Amino-4-[(2s,3r)-2,3,5-Trihydroxy-4-Oxo-Pentyl]Mercapto-Butyric Acid.
DR   DrugBank; DB02321; 5-(3-Amino-4,4-Dihyroxy-Butylsulfanylmethyl)-Tetrahydro-Furan-2,3,4-Triol.
DR   DrugBank; DB04422; Homocysteine.
DR   DrugBank; DB03661; L-cysteic acid.
DR   DrugCentral; O34667; -.
DR   jPOST; O34667; -.
DR   PaxDb; 224308-BSU30670; -.
DR   EnsemblBacteria; CAB15045; CAB15045; BSU_30670.
DR   GeneID; 64304786; -.
DR   GeneID; 937106; -.
DR   KEGG; bsu:BSU30670; -.
DR   PATRIC; fig|224308.179.peg.3325; -.
DR   eggNOG; COG1854; Bacteria.
DR   InParanoid; O34667; -.
DR   OrthoDB; 9788129at2; -.
DR   PhylomeDB; O34667; -.
DR   BioCyc; BSUB:BSU30670-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-14557; -.
DR   BRENDA; 4.4.1.21; 658.
DR   SABIO-RK; O34667; -.
DR   EvolutionaryTrace; O34667; -.
DR   Proteomes; UP000001570; 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; 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   1: Evidence at protein level;
KW   3D-structure; Autoinducer synthesis; Iron; Lyase; Metal-binding;
KW   Quorum sensing; Reference proteome.
FT   CHAIN           1..157
FT                   /note="S-ribosylhomocysteine lyase"
FT                   /id="PRO_0000172211"
FT   BINDING         54
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         58
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         126
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   MUTAGEN         57
FT                   /note="E->A,Q: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:12705835"
FT   MUTAGEN         57
FT                   /note="E->D: 220-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:12705835"
FT   MUTAGEN         84
FT                   /note="C->A: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:12705835"
FT   MUTAGEN         84
FT                   /note="C->D,S: Almost complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:12705835"
FT   HELIX           5..8
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   TURN            11..13
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   STRAND          16..27
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   STRAND          31..39
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   HELIX           50..68
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   STRAND          72..81
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   STRAND          85..94
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   HELIX           98..112
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   TURN            123..125
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   TURN            127..130
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   HELIX           134..145
FT                   /evidence="ECO:0007829|PDB:1J98"
FT   HELIX           149..152
FT                   /evidence="ECO:0007829|PDB:1J98"
SQ   SEQUENCE   157 AA;  17714 MW;  DD011A2A88BD2FFB CRC64;
     MPSVESFELD HNAVVAPYVR HCGVHKVGTD GVVNKFDIRF CQPNKQAMKP DTIHTLEHLL
     AFTIRSHAEK YDHFDIIDIS PMGCQTGYYL VVSGEPTSAE IVDLLEDTMK EAVEITEIPA
     ANEKQCGQAK LHDLEGAKRL MRFWLSQDKE ELLKVFG
//