ID A0A1D2LQ15_BROTH Unreviewed; 153 AA.
AC A0A1D2LQ15;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 18-JUN-2025, entry version 38.
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 ECO:0000313|EMBL:SPP27514.1};
GN ORFNames=BTBSAS_160017 {ECO:0000313|EMBL:SPP27514.1}, CNY62_03735
GN {ECO:0000313|EMBL:ATF25579.1};
OS Brochothrix thermosphacta (Microbacterium thermosphactum).
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
OC Brochothrix.
OX NCBI_TaxID=2756 {ECO:0000313|EMBL:ATF25579.1, ECO:0000313|Proteomes:UP000243591};
RN [1] {ECO:0000313|EMBL:ATF25579.1, ECO:0000313|Proteomes:UP000243591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BI {ECO:0000313|EMBL:ATF25579.1,
RC ECO:0000313|Proteomes:UP000243591};
RA Paoli G.C., Wijey C., Chen C.-Y., Nguyen L., Yan X., Irwin P.L.;
RT "Complete Genome Sequences of Two Strains of the Meat Spoilage Bacterium
RT Brochothrix thermosphacta Isolated from Ground Chicken.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPP27514.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BSAS1 3 {ECO:0000313|EMBL:SPP27514.1};
RA Go L.Y., Mitchell J.A.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000270190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Illikoud N.;
RL Submitted (APR-2018) 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}.
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DR EMBL; CP023483; ATF25579.1; -; Genomic_DNA.
DR EMBL; OUNC01000008; SPP27514.1; -; Genomic_DNA.
DR RefSeq; WP_029091376.1; NZ_RSDU01000003.1.
DR AlphaFoldDB; A0A1D2LQ15; -.
DR STRING; 2756.BFR44_00175; -.
DR KEGG; bths:CNY62_03735; -.
DR OrthoDB; 9788129at2; -.
DR Proteomes; UP000243591; Chromosome.
DR Proteomes; UP000270190; 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; S-ribosylhomocysteinase (LuxS); 1.
DR HAMAP; MF_00091; LuxS; 1.
DR InterPro; IPR037005; LuxS_sf.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR003815; S-ribosylhomocysteinase.
DR NCBIfam; NF002606; PRK02260.2-4; 1.
DR PANTHER; PTHR35799; S-RIBOSYLHOMOCYSTEINE LYASE; 1.
DR PANTHER; PTHR35799:SF1; S-RIBOSYLHOMOCYSTEINE LYASE; 1.
DR Pfam; PF02664; LuxS; 1.
DR PIRSF; PIRSF006160; AI2; 1.
DR PRINTS; PR01487; LUXSPROTEIN.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 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:UP000243591}.
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
SQ SEQUENCE 153 AA; 17219 MW; 10684EC898BDD1AF CRC64;
MARVESFELD HTIVKAPYVR AAGVETSPQG STVQKYDLRF LQPNEDSLPT AAVHTLEHLL
ATYLRDEVEG IIDISPMGCR TGFYLILWDL HEPEEIAVAL EKTLKRIIET VDVPAVSALE
CGNYKDHSLF SAKIYAENVL NQGISRDPFK RIF
//
