ID LUXS_BACAN Reviewed; 157 AA. AC Q81KF3; Q6HRV7; Q6KL63; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 127. 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=BA_5047, GBAA_5047, BAS4687; OS Bacillus anthracis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames / isolate Porton; RX PubMed=12721629; DOI=10.1038/nature01586; RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L., RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., RA Hanna P.C., Kolstoe A.-B., Fraser C.M.; RT "The genome sequence of Bacillus anthracis Ames and comparison to closely RT related bacteria."; RL Nature 423:81-86(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor; RX PubMed=18952800; DOI=10.1128/jb.01347-08; RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.; RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."; RL J. Bacteriol. 191:445-446(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sterne; RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., RA Richardson P., Rubin E., Tice H.; RT "Complete genome sequence of Bacillus anthracis Sterne."; RL Submitted (JAN-2004) 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016879; AAP28724.1; -; Genomic_DNA. DR EMBL; AE017334; AAT34170.1; -; Genomic_DNA. DR EMBL; AE017225; AAT56981.1; -; Genomic_DNA. DR RefSeq; NP_847238.1; NC_003997.3. DR RefSeq; WP_001141369.1; NZ_WXXJ01000026.1. DR RefSeq; YP_030931.1; NC_005945.1. DR AlphaFoldDB; Q81KF3; -. DR SMR; Q81KF3; -. DR STRING; 261594.GBAA_5047; -. DR DNASU; 1084317; -. DR GeneID; 75087962; -. DR KEGG; ban:BA_5047; -. DR KEGG; bar:GBAA_5047; -. DR KEGG; bat:BAS4687; -. DR PATRIC; fig|198094.11.peg.5008; -. DR eggNOG; COG1854; Bacteria. DR HOGENOM; CLU_107531_2_0_9; -. DR OMA; DVSPMGC; -. DR OrthoDB; 9788129at2; -. DR BRENDA; 4.4.1.21; 634. DR Proteomes; UP000000427; Chromosome. DR Proteomes; UP000000594; 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 3: Inferred from homology; KW Autoinducer synthesis; Iron; Lyase; Metal-binding; Quorum sensing; KW Reference proteome. FT CHAIN 1..157 FT /note="S-ribosylhomocysteine lyase" FT /id="PRO_0000172204" 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 126 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091" SQ SEQUENCE 157 AA; 17856 MW; 5D2BB8F36D754793 CRC64; MPSVESFELD HTIVKAPYVR HCGVHNVGSD GIVNKFDIRF CQPNKQAMKP DVIHTLEHLL AFNLRKYIDR YPHFDIIDIS PMGCQTGYYL VVSGTPTVRE IIDLLELTLK DAVQITEIPA ANETQCGQAK LHDLEGAKRL MNFWLSQDKD ELEKVFG //