LUXS_VIBC1
ID LUXS_VIBC1 Reviewed; 172 AA.
AC Q9Z5X1; A7MYV6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=S-ribosylhomocysteine lyase;
DE EC=4.4.1.21;
DE AltName: Full=AI-2 synthesis protein;
DE AltName: Full=Autoinducer-2 production protein LuxS;
GN Name=luxS; OrderedLocusNames=VIBHAR_03484;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9990077; DOI=10.1073/pnas.96.4.1639;
RA Surette M.G., Miller M.B., Bassler B.L.;
RT "Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio
RT harveyi: a new family of genes responsible for autoinducer production.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1639-1644(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) 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:0000269|PubMed:9990077}.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABU72429.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF120098; AAD17292.1; -; Genomic_DNA.
DR EMBL; CP000789; ABU72429.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_012128886.1; NC_022269.1.
DR AlphaFoldDB; Q9Z5X1; -.
DR SMR; Q9Z5X1; -.
DR BindingDB; Q9Z5X1; -.
DR ChEMBL; CHEMBL4682; -.
DR EnsemblBacteria; ABU72429; ABU72429; VIBHAR_03484.
DR KEGG; vha:VIBHAR_03484; -.
DR PATRIC; fig|338187.25.peg.2716; -.
DR OMA; GPMGCLT; -.
DR OrthoDB; 1779617at2; -.
DR BRENDA; 4.4.1.21; 6632.
DR Proteomes; UP000008152; Chromosome I.
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; -; 1.
DR HAMAP; MF_00091; LuxS; 1.
DR InterPro; IPR037005; LuxS_sf.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR003815; S-ribosylhomocysteinase.
DR PANTHER; PTHR35799; PTHR35799; 1.
DR Pfam; PF02664; LuxS; 1.
DR PIRSF; PIRSF006160; AI2; 1.
DR PRINTS; PR01487; LUXSPROTEIN.
DR SUPFAM; SSF63411; SSF63411; 1.
PE 3: Inferred from homology;
KW Autoinducer synthesis; Iron; Lyase; Metal-binding; Quorum sensing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..172
FT /note="S-ribosylhomocysteine lyase"
FT /id="PRO_0000172275"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 172 AA; 19143 MW; 2B36D46F68118E89 CRC64;
MPLLDSFTVD HTRMNAPAVR VAKTMQTPKG DTITVFDLRF TAPNKDILSE KGIHTLEHLY
AGFMRNHLNG DSVEIIDISP MGCRTGFYMS LIGTPSEQQV ADAWIAAMED VLKVENQNKI
PELNEYQCGT AAMHSLDEAK QIAKNILEVG VAVNKNDELA LPESMLRELR ID
