ID R9NA01_9FIRM Unreviewed; 159 AA. AC R9NA01; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 03-AUG-2022, entry version 44. DE RecName: Full=S-ribosylhomocysteine lyase {ECO:0000256|ARBA:ARBA00015130, ECO:0000256|HAMAP-Rule:MF_00091}; DE EC=4.4.1.21 {ECO:0000256|ARBA:ARBA00012240, ECO:0000256|HAMAP-Rule:MF_00091}; DE AltName: Full=AI-2 synthesis protein {ECO:0000256|ARBA:ARBA00030600, ECO:0000256|HAMAP-Rule:MF_00091}; DE AltName: Full=Autoinducer-2 production protein LuxS {ECO:0000256|ARBA:ARBA00031777, ECO:0000256|HAMAP-Rule:MF_00091}; GN Name=luxS {ECO:0000256|HAMAP-Rule:MF_00091}; GN ORFNames=C817_02027 {ECO:0000313|EMBL:EOS80154.1}; OS Dorea sp. 5-2. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae; Dorea; OC unclassified Dorea. OX NCBI_TaxID=1235798 {ECO:0000313|EMBL:EOS80154.1, ECO:0000313|Proteomes:UP000014211}; RN [1] {ECO:0000313|EMBL:EOS80154.1, ECO:0000313|Proteomes:UP000014211} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5-2 {ECO:0000313|EMBL:EOS80154.1, RC ECO:0000313|Proteomes:UP000014211}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Dorea bacterium 5-2."; RL Submitted (APR-2013) 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:0000256|ARBA:ARBA00024654, ECO:0000256|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:0000256|ARBA:ARBA00000297, ECO:0000256|HAMAP- CC Rule:MF_00091}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00091}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000256|HAMAP-Rule:MF_00091}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_00091}. CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000256|ARBA:ARBA00007311, CC ECO:0000256|HAMAP-Rule:MF_00091}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EOS80154.1}. 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; ASTD01000037; EOS80154.1; -; Genomic_DNA. DR RefSeq; WP_016218764.1; NZ_KE159759.1. DR STRING; 1235798.C817_02027; -. DR EnsemblBacteria; EOS80154; EOS80154; C817_02027. DR PATRIC; fig|1235798.3.peg.2142; -. DR eggNOG; COG1854; Bacteria. DR HOGENOM; CLU_107531_1_0_9; -. DR OrthoDB; 1779617at2; -. DR Proteomes; UP000014211; Unassembled WGS sequence. 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; -; 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; PTHR35799; 1. DR Pfam; PF02664; LuxS; 1. DR PIRSF; PIRSF006160; AI2; 1. DR PRINTS; PR01487; LUXSPROTEIN. DR SUPFAM; SSF63411; SSF63411; 1. PE 3: Inferred from homology; KW Autoinducer synthesis {ECO:0000256|ARBA:ARBA00022929, ECO:0000256|HAMAP- KW Rule:MF_00091}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00091}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00091}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00091}; KW Quorum sensing {ECO:0000256|ARBA:ARBA00022654, ECO:0000256|HAMAP- KW Rule:MF_00091}; Reference proteome {ECO:0000313|Proteomes:UP000014211}. FT BINDING 53 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091" FT BINDING 57 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091" FT BINDING 124 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091" SQ SEQUENCE 159 AA; 18055 MW; 22C14DDD67A7076E CRC64; MEKITSFTID HLRLVPGLYV SRIDQVEGHP ITTFDIRMTS PNDEPVMNTA EMHAIEHLAA TFLRNHATYA DKTLYFGPMG CRTGFYLLLA GEYASRDIVP LMTEMFTFIA SFDGDVPGAC AKDCGNYLDM NLPMARYLAR KYLREVLTDI TDQQLLYPE //