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Database: UniProt/TrEMBL
Entry: C6STF9_STRMN
LinkDB: C6STF9_STRMN
Original site: C6STF9_STRMN 
ID   C6STF9_STRMN            Unreviewed;       158 AA.
AC   C6STF9;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   01-MAY-2013, entry version 28.
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=SmuNN2025_0080;
OS   Streptococcus mutans serotype c (strain NN2025).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=511691;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NN2025;
RX   PubMed=19656368; DOI=10.1186/1471-2164-10-358;
RA   Maruyama F., Kobata M., Kurokawa K., Nishida K., Sakurai A.,
RA   Nakano K., Nomura R., Kawabata S., Ooshima T., Nakai K., Hattori M.,
RA   Hamada S., Nakagawa I.;
RT   "Comparative genomic analyses of Streptococcus mutans provide insights
RT   into chromosomal shuffling and species-specific content.";
RL   BMC Genomics 10:358-358(2009).
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) (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-
CC       homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione.
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the LuxS family.
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DR   EMBL; AP010655; BAH87106.1; -; Genomic_DNA.
DR   RefSeq; YP_003483998.1; NC_013928.1.
DR   EnsemblBacteria; BAH87106; BAH87106; SmuNN2025_0080.
DR   GeneID; 8835715; -.
DR   KEGG; smc:SmuNN2025_0080; -.
DR   PATRIC; 35311981; VBIStrMut11111_0078.
DR   HOGENOM; HOG000040372; -.
DR   KO; K07173; -.
DR   OMA; FTINHNI; -.
DR   ProtClustDB; PRK02260; -.
DR   BioCyc; SMUT511691:GH9C-131-MONOMER; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0043768; F:S-ribosylhomocysteine lyase activity; IEA:HAMAP.
DR   GO; GO:0008152; P:metabolic process; IEA:GOC.
DR   GO; GO:0009372; P:quorum sensing; IEA: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; Metalloenz_metal-bd; 1.
PE   3: Inferred from homology;
KW   Autoinducer synthesis; Complete proteome; Iron; Lyase; Metal-binding;
KW   Quorum sensing.
FT   METAL        54     54       Iron (By similarity).
FT   METAL        58     58       Iron (By similarity).
FT   METAL       125    125       Iron (By similarity).
SQ   SEQUENCE   158 AA;  17962 MW;  67309C470D3BF66A CRC64;
     MARVESFELD HTKVRAPYVR KIDTQVGEKG DSISNFDIRL VQPNQSAIPS GGIHTIEHSL
     ASLIRNRIDG VIDFSPFGCR TGFHLIIWGN HTSKEIALVI KESLKEMVSD EFRWENVPGI
     SERQCGNYRD HSLFTAKEWG KQILRQGISS DPFLRKIV
//
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