ID LUXS_GEOTN Reviewed; 158 AA. AC A4IS03; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 2. DT 02-SEP-2026, entry version 86. 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=GTNG_2762; OS Geobacillus thermodenitrificans (strain NG80-2). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae; OC Geobacillus. OX NCBI_TaxID=420246; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NG80-2; RX PubMed=17372208; DOI=10.1073/pnas.0609650104; RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., RA Han W., Peng X., Liu R., Wang L.; RT "Genome and proteome of long-chain alkane degrading Geobacillus RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."; RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007). 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 -!- SEQUENCE CAUTION: CC Sequence=ABO68107.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CP000557; ABO68107.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_008880964.1; NC_009328.1. DR AlphaFoldDB; A4IS03; -. DR SMR; A4IS03; -. DR GeneID; 87623095; -. DR KEGG; gtn:GTNG_2762; -. DR eggNOG; COG1854; Bacteria. DR HOGENOM; CLU_107531_1_0_9; -. 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 NCBIfam; NF002603; PRK02260.1-3; 1. DR NCBIfam; NF002604; PRK02260.1-4; 1. 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 CHAIN 1..158 FT /note="S-ribosylhomocysteine lyase" FT /id="PRO_0000297998" FT BINDING 55 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091" FT BINDING 59 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091" FT BINDING 127 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091" SQ SEQUENCE 158 AA; 17744 MW; 4507CC34DDC964B9 CRC64; MPSPVESFEL DHCAVKAPYV RHCGVHKIGS DGVVNKFDIR FCQPNKEAMD PAAIHTLEHL LAYTLRKHVT KYDHFDIIDI SPMGCQTGFY LVVSGSPTVD EIIDLLEETM KDALNATEVP AATERQCGQA KLHDLEAAKE LMRFWLSQEK SELKKVFG //