ID LUXS_KLEP3 Reviewed; 171 AA. AC B5XVC4; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 72. 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=KPK_1109; OS Klebsiella pneumoniae (strain 342). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=507522; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=342; RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141; RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H., RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y., RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W., RA Methe B.A.; RT "Complete genome sequence of the N2-fixing broad host range endophyte RT Klebsiella pneumoniae 342 and virulence predictions verified in mice."; RL PLoS Genet. 4:E1000141-E1000141(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; 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; CP000964; ACI11857.1; -; Genomic_DNA. DR AlphaFoldDB; B5XVC4; -. DR SMR; B5XVC4; -. DR KEGG; kpe:KPK_1109; -. DR HOGENOM; CLU_107531_2_0_6; -. DR Proteomes; UP000001734; 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. FT CHAIN 1..171 FT /note="S-ribosylhomocysteine lyase" FT /id="PRO_1000093312" 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; 19454 MW; C6933F282F035953 CRC64; MPLLDSFTVD HTRMEAPAVR VAKKMNTPHG DEITVFDLRF CVPNQEVMPE RGIHTLEHLF AGFMRDHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV ADAWKAAMAD VLKVKDQNQI PELNVYQCGT YTMHSLEEAQ DIARHIIERD VRINSNDELA LPKEKLQELH I //