ID A0A024QER8_9BACI Unreviewed; 153 AA.
AC A0A024QER8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 18-JUN-2025, entry version 44.
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:CDQ40752.1};
GN ORFNames=BN990_03080 {ECO:0000313|EMBL:CDQ40752.1};
OS Virgibacillus massiliensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Virgibacillus.
OX NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ40752.1, ECO:0000313|Proteomes:UP000028875};
RN [1] {ECO:0000313|EMBL:CDQ40752.1, ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ40752.1,
RC ECO:0000313|Proteomes:UP000028875};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875};
RA Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequence of Virgibacillus massiliensis Vm-5.";
RL Submitted (MAY-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDQ40752.1}.
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; CCDP010000002; CDQ40752.1; -; Genomic_DNA.
DR RefSeq; WP_021292171.1; NZ_CCDP010000002.1.
DR AlphaFoldDB; A0A024QER8; -.
DR STRING; 1462526.BN990_03080; -.
DR eggNOG; COG1854; Bacteria.
DR OrthoDB; 9788129at2; -.
DR Proteomes; UP000028875; 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; NF002604; PRK02260.1-4; 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:UP000028875}.
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
SQ SEQUENCE 153 AA; 17661 MW; 75B9CA6345A68936 CRC64;
MAKKMNVESF NLDHTKVKAP YVRLVGVTEG ANGDKVYKYD IRFKQPNKEH MDMDGLHSIE
HLMAENIRNH MDNVLDIGPM GCQTGFYLSI MNRDQYEEVL EAFEHTLNDV LEAREVPACN
EVQCGWAANH SLEGAKKIAQ EMLDHRNEWH QVF
//