ID A0A420VF52_9BACI Unreviewed; 156 AA.
AC A0A420VF52;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 16.
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=Cdeb_01028 {ECO:0000313|EMBL:RKO62292.1};
OS Caldibacillus debilis GB1.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Caldibacillus.
OX NCBI_TaxID=1339248 {ECO:0000313|EMBL:RKO62292.1, ECO:0000313|Proteomes:UP000286235};
RN [1] {ECO:0000313|EMBL:RKO62292.1, ECO:0000313|Proteomes:UP000286235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB1 {ECO:0000313|EMBL:RKO62292.1,
RC ECO:0000313|Proteomes:UP000286235};
RA Wushke S.T., Zhang X., Fristensky B., Wilkins J.A., Levin D.B.,
RA Sparling R.;
RT "Genome and proteome characterization of Caldibacillus debilis GB1 derived
RT from a cellulolytic aero-tolerant co-culture.";
RL Submitted (DEC-2013) 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:RKO62292.1}.
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DR EMBL; AZRV01000023; RKO62292.1; -; Genomic_DNA.
DR RefSeq; WP_020156046.1; NZ_AZRV01000023.1.
DR AlphaFoldDB; A0A420VF52; -.
DR Proteomes; UP000286235; 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:UP000286235}.
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
FT BINDING 125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00091"
SQ SEQUENCE 156 AA; 17887 MW; 6CF3AA3F32FC314E CRC64;
MKKDRLNVES FHLDHTKVKA PYVRLADVKT GKNGDKIYKY DVRFCQPNKE HMEMPALHSL
EHLMAERIRD HHPDVFDVSP MGCQTGFYVS IINDGDYEGF LRVLEKTLTD VLNAEEVPAC
NEIQCGNAAS HSLEGAKKLA KKMLDHRDEW TQVFAE
//
