ID   R9NA01_9FIRM            Unreviewed;       159 AA.
AC   R9NA01;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   29-APR-2015, entry version 15.
DE   RecName: Full=S-ribosylhomocysteine lyase {ECO:0000256|HAMAP-Rule:MF_00091, ECO:0000256|SAAS:SAAS00059609};
DE            EC=4.4.1.21 {ECO:0000256|HAMAP-Rule:MF_00091, ECO:0000256|SAAS:SAAS00059628};
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};
RN   [1] {ECO:0000313|EMBL:EOS80154.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=5-2 {ECO:0000313|EMBL:EOS80154.1};
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:SAAS00059595}.
CC   -!- CATALYTIC ACTIVITY: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-
CC       homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione.
CC       {ECO:0000256|HAMAP-Rule:MF_00091, ECO:0000256|SAAS:SAAS00059622}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00091,
CC         ECO:0000256|SAAS:SAAS00170279};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00091, ECO:0000256|SAAS:SAAS00170279};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 1 Fe cation per subunit.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00091,
CC       ECO:0000256|SAAS:SAAS00059580}.
CC   -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00091}.
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}.
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DR   EMBL; ASTD01000037; EOS80154.1; -; Genomic_DNA.
DR   RefSeq; WP_016218764.1; NZ_KE159759.1.
DR   EnsemblBacteria; EOS80154; EOS80154; C817_02027.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0043768; F:S-ribosylhomocysteine lyase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.1360.80; -; 1.
DR   HAMAP; MF_00091; LuxS; 1.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR003815; S-ribosylhomocysteinase.
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:SAAS00059589};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00091, ECO:0000256|SAAS:SAAS00059587};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00091,
KW   ECO:0000256|SAAS:SAAS00059585};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00091,
KW   ECO:0000256|SAAS:SAAS00059563};
KW   Quorum sensing {ECO:0000256|HAMAP-Rule:MF_00091,
KW   ECO:0000256|SAAS:SAAS00059594}.
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
//