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Database: UniProt
Entry: A0A365L843_9BACL
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ID   A0A365L843_9BACL        Unreviewed;       154 AA.
AC   A0A365L843;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   18-JUN-2025, entry version 19.
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   ORFNames=DP120_00730 {ECO:0000313|EMBL:RAZ81570.1};
OS   Planococcus halotolerans.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Caryophanaceae;
OC   Planococcus.
OX   NCBI_TaxID=2233542 {ECO:0000313|EMBL:RAZ81570.1, ECO:0000313|Proteomes:UP000251002};
RN   [1] {ECO:0000313|EMBL:RAZ81570.1, ECO:0000313|Proteomes:UP000251002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCU63 {ECO:0000313|EMBL:RAZ81570.1,
RC   ECO:0000313|Proteomes:UP000251002};
RA   Gan L.;
RT   "The draft genome sequences of strains SCU63 and S1.";
RL   Submitted (JUN-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}.
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:RAZ81570.1}.
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DR   EMBL; QLZR01000001; RAZ81570.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365L843; -.
DR   Proteomes; UP000251002; 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:UP000251002}.
FT   BINDING         53
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
FT   BINDING         57
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
FT   BINDING         120
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
SQ   SEQUENCE   154 AA;  17496 MW;  799BE5CB2DF63020 CRC64;
     MNVESFNLDH TKVAAPYVRL AGEKTGANGD TIRKYDIRFK QPNKEHMEMP GLHSLEHMMA
     EHSRNHSDQI IDIGPMGCQT GYYLSLINHD DYDDVLRIIE NTLKDVIEAD EVPACNEVQC
     GWAASHSLEG AKELAREMLA KKDEWHQVFA EETV
//
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