ID LUXS_HAEIN Reviewed; 167 AA. AC P44007; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 143. 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=HI_0491; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=9719565; DOI=10.1002/elps.1150191046; RA Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P., RA Langen H.; RT "Reference map of the low molecular mass proteins of Haemophilus RT influenzae."; RL Electrophoresis 19:1819-1827(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=11435117; DOI=10.1016/s0969-2126(01)00613-x; RA Lewis H.A., Furlong E.B., Laubert B., Eroshkina G.A., Batiyenko Y., RA Adams J.M., Bergseid M.G., Marsh C.D., Peat T.S., Sanderson W.E., RA Sauder J.M., Buchanan S.G.; RT "A structural genomics approach to the study of quorum sensing: crystal RT structures of three LuxS orthologs."; RL Structure 9:527-537(2001). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RA Chen C.C.H., Parsons J.F., Lim K., Lehmann C., Tempczyk A., Eisenstein E., RA Herzberg O.; RT "Crystal structure of autoinducer-2 production protein (luxS) from RT Haemophilus influenzae -- a case of twinned crystal."; RL Submitted (JUL-2001) to the PDB data bank. 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 Note=Binds 1 Fe cation per subunit.; CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the LuxS family. {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; L42023; AAC22149.1; -; Genomic_DNA. DR PIR; G64008; G64008. DR RefSeq; NP_438651.1; NC_000907.1. DR PDB; 1J6W; X-ray; 2.10 A; A/B=2-167. DR PDB; 1JOE; X-ray; 2.40 A; A/B/C/D=1-167. DR PDBsum; 1J6W; -. DR PDBsum; 1JOE; -. DR AlphaFoldDB; P44007; -. DR SMR; P44007; -. DR STRING; 71421.HI_0491; -. DR EnsemblBacteria; AAC22149; AAC22149; HI_0491. DR KEGG; hin:HI_0491; -. DR PATRIC; fig|71421.8.peg.510; -. DR eggNOG; COG1854; Bacteria. DR HOGENOM; CLU_107531_2_0_6; -. DR OrthoDB; 9788129at2; -. DR PhylomeDB; P44007; -. DR BioCyc; HINF71421:G1GJ1-506-MONOMER; -. DR BRENDA; 4.4.1.21; 2529. DR EvolutionaryTrace; P44007; -. DR Proteomes; UP000000579; 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 INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..167 FT /note="S-ribosylhomocysteine lyase" FT /id="PRO_0000172227" 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 128 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT HELIX 5..8 FT /evidence="ECO:0007829|PDB:1J6W" FT HELIX 11..13 FT /evidence="ECO:0007829|PDB:1J6W" FT STRAND 16..26 FT /evidence="ECO:0007829|PDB:1J6W" FT STRAND 32..39 FT /evidence="ECO:0007829|PDB:1J6W" FT TURN 43..45 FT /evidence="ECO:0007829|PDB:1J6W" FT HELIX 50..68 FT /evidence="ECO:0007829|PDB:1J6W" FT STRAND 73..80 FT /evidence="ECO:0007829|PDB:1J6W" FT STRAND 84..93 FT /evidence="ECO:0007829|PDB:1J6W" FT HELIX 97..112 FT /evidence="ECO:0007829|PDB:1J6W" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:1J6W" FT TURN 125..127 FT /evidence="ECO:0007829|PDB:1J6W" FT TURN 129..132 FT /evidence="ECO:0007829|PDB:1J6W" FT HELIX 136..149 FT /evidence="ECO:0007829|PDB:1J6W" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:1J6W" FT HELIX 156..159 FT /evidence="ECO:0007829|PDB:1J6W" SQ SEQUENCE 167 AA; 18527 MW; A8116FE96BA5F817 CRC64; MPLLDSFKVD HTKMNAPAVR IAKTMLTPKG DNITVFDLRF CIPNKEILSP KGIHTLEHLF AGFMRDHLNG DSIEIIDISP MGCRTGFYMS LIGTPNEQKV SEAWLASMQD VLGVQDQASI PELNIYQCGS YTEHSLEDAH EIAKNVIARG IGVNKNEDLS LDNSLLK //