GenomeNet

Database: UniProt
Entry: A0A3Q9I8Y3_9BACL
LinkDB: A0A3Q9I8Y3_9BACL
Original site: A0A3Q9I8Y3_9BACL 
ID   A0A3Q9I8Y3_9BACL        Unreviewed;       153 AA.
AC   A0A3Q9I8Y3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   18-JUN-2025, entry version 21.
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=EI981_04950 {ECO:0000313|EMBL:AZS13865.1};
OS   Paenibacillus lutimineralis.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=2707005 {ECO:0000313|EMBL:AZS13865.1, ECO:0000313|Proteomes:UP000270678};
RN   [1] {ECO:0000313|Proteomes:UP000270678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBLB1234 {ECO:0000313|Proteomes:UP000270678};
RA   Nam Y.-D., Kang J., Chung W.-H., Park Y.S.;
RT   "Complete genome sequence of Paenibacillus sp. MBLB1234.";
RL   Submitted (DEC-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   ---------------------------------------------------------------------------
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; CP034346; AZS13865.1; -; Genomic_DNA.
DR   RefSeq; WP_126995959.1; NZ_CP034346.1.
DR   AlphaFoldDB; A0A3Q9I8Y3; -.
DR   KEGG; plut:EI981_04950; -.
DR   OrthoDB; 9788129at2; -.
DR   Proteomes; UP000270678; Chromosome.
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   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:UP000270678}.
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;  17216 MW;  F6B9B34712BC69E9 CRC64;
     MAKVESFQLD HTIVKAPYVR AAGLEHDEKG STVQKYDLRF LQPNKDAIPT AALHTLEHLL
     ATYMRDEVQG IIDISPMGCR TGYYLILWNE HAPEEIASAL ERTLKRVLET TEVPAVSALE
     CGNYKDHSLF SAQEYAKIVL DAGISRDPFE RVL
//
DBGET integrated database retrieval system