ID LUXS_LACJO Reviewed; 158 AA.
AC Q74HV0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 01-MAY-2013, entry version 59.
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=LJ_0631;
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533;
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium
RT Lactobacillus johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS09590.1; -; Genomic_DNA.
DR RefSeq; NP_965624.1; NC_005362.1.
DR ProteinModelPortal; Q74HV0; -.
DR STRING; 257314.LJ0631; -.
DR EnsemblBacteria; AAS09590; AAS09590; LJ_0631.
DR GeneID; 2743085; -.
DR KEGG; ljo:LJ0631; -.
DR PATRIC; 22240057; VBILacJoh1832_1644.
DR eggNOG; COG1854; -.
DR KO; K07173; -.
DR OMA; KAPYVRV; -.
DR ProtClustDB; PRK02260; -.
DR BioCyc; LJOH257314:GJN3-1695-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 CHAIN 1 158 S-ribosylhomocysteine lyase.
FT /FTId=PRO_0000172231.
FT METAL 54 54 Iron (By similarity).
FT METAL 58 58 Iron (By similarity).
FT METAL 124 124 Iron (By similarity).
SQ SEQUENCE 158 AA; 17795 MW; D5B0B6C088F9DAF3 CRC64;
MGKVESFELD HTKVKAPYVR LITVEEGQKG DKISNFDLRL VQPNENAIPT GGLHTIEHLL
AGLLRDRIDG YIDCSPFGCR TGFHLLVWGT PSTTDVAKAL KESLEEIRDN ITWEDVPGTT
IESCGNYRDH SLFSAKQWSR DILEKGISDD PFERHVVE
//
