ID R9NA01_9FIRM Unreviewed; 159 AA. AC R9NA01; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 16-JAN-2019, entry version 32. DE RecName: Full=S-ribosylhomocysteine lyase {ECO:0000256|HAMAP-Rule:MF_00091, ECO:0000256|SAAS:SAAS00962992}; DE EC=4.4.1.21 {ECO:0000256|HAMAP-Rule:MF_00091, ECO:0000256|SAAS:SAAS00962995}; DE AltName: Full=AI-2 synthesis protein {ECO:0000256|HAMAP-Rule:MF_00091}; DE AltName: Full=Autoinducer-2 production protein LuxS {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; Clostridiales; Lachnospiraceae; OC 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., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., 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 CC is secreted by bacteria and is used to communicate both the cell CC density and the metabolic potential of the environment. The CC regulation of gene expression in response to changes in cell CC density is called quorum sensing. Catalyzes the transformation of CC S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5- CC dihydroxy-2,3-pentadione (DPD). {ECO:0000256|HAMAP-Rule:MF_00091, CC ECO:0000256|SAAS:SAAS00963003}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5- CC dihydroxypentane-2,3-dione + L-homocysteine; CC Xref=Rhea:RHEA:17753, ChEBI:CHEBI:29484, ChEBI:CHEBI:58195, CC ChEBI:CHEBI:58199; EC=4.4.1.21; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00091, ECO:0000256|SAAS:SAAS01115303}; 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- CC Rule:MF_00091}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00091, CC ECO:0000256|SAAS:SAAS00962998}. CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000256|HAMAP- CC Rule:MF_00091, ECO:0000256|SAAS:SAAS00962996}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; EOS80154; EOS80154; C817_02027. DR PATRIC; fig|1235798.3.peg.2142; -. 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 ProDom; PD013172; S-ribosylhomocysteinase; 1. DR SUPFAM; SSF63411; SSF63411; 1. PE 3: Inferred from homology; KW Autoinducer synthesis {ECO:0000256|HAMAP-Rule:MF_00091, KW ECO:0000256|SAAS:SAAS00963005}; KW Complete proteome {ECO:0000313|Proteomes:UP000014211}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00091, ECO:0000256|SAAS:SAAS00962991}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00091, ECO:0000256|SAAS:SAAS00962997, KW ECO:0000313|EMBL:EOS80154.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00091, KW ECO:0000256|SAAS:SAAS00963001}; KW Quorum sensing {ECO:0000256|HAMAP-Rule:MF_00091, KW ECO:0000256|SAAS:SAAS00963004}; KW Reference proteome {ECO:0000313|Proteomes:UP000014211}. FT METAL 53 53 Iron. {ECO:0000256|HAMAP-Rule:MF_00091}. FT METAL 57 57 Iron. {ECO:0000256|HAMAP-Rule:MF_00091}. FT METAL 124 124 Iron. {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 //