LUXS_SALTI
ID LUXS_SALTI Reviewed; 171 AA.
AC Q8Z4D7;
DT 06-JUN-2002, 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 {ECO:0000255|HAMAP-Rule:MF_00091};
DE EC=4.4.1.21 {ECO:0000255|HAMAP-Rule:MF_00091};
DE AltName: Full=AI-2 synthesis protein {ECO:0000255|HAMAP-Rule:MF_00091};
DE AltName: Full=Autoinducer-2 production protein LuxS {ECO:0000255|HAMAP-Rule:MF_00091};
GN Name=luxS {ECO:0000255|HAMAP-Rule:MF_00091};
GN OrderedLocusNames=STY2943, t2714;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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:0000255|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:0000255|HAMAP-Rule:MF_00091};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00091};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000255|HAMAP-Rule:MF_00091};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00091}.
CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000255|HAMAP-
CC Rule:MF_00091}.
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DR EMBL; AL513382; CAD05928.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70280.1; -; Genomic_DNA.
DR RefSeq; NP_457215.1; NC_003198.1.
DR PDB; 5E68; X-ray; 1.58 A; A/B=1-171.
DR PDB; 5V2W; X-ray; 2.30 A; A/B=1-171.
DR PDBsum; 5E68; -.
DR PDBsum; 5V2W; -.
DR AlphaFoldDB; Q8Z4D7; -.
DR SMR; Q8Z4D7; -.
DR STRING; 220341.16503899; -.
DR EnsemblBacteria; AAO70280; AAO70280; t2714.
DR KEGG; stt:t2714; -.
DR KEGG; sty:STY2943; -.
DR PATRIC; fig|220341.7.peg.2996; -.
DR eggNOG; COG1854; Bacteria.
DR HOGENOM; CLU_107531_2_0_6; -.
DR OMA; GPMGCLT; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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; -; 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 1: Evidence at protein level;
KW 3D-structure; Autoinducer synthesis; Iron; Lyase; Metal-binding;
KW Quorum sensing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..171
FT /note="S-ribosylhomocysteine lyase"
FT /id="PRO_0000172248"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00091"
FT CONFLICT 21
FT /note="G -> V (in Ref. 2; AAO70280)"
FT /evidence="ECO:0000305"
FT STRAND 16..26
FT /evidence="ECO:0007829|PDB:5E68"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:5E68"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:5E68"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:5E68"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5E68"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:5E68"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:5E68"
FT HELIX 97..112
FT /evidence="ECO:0007829|PDB:5E68"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5E68"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:5E68"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:5E68"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:5E68"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:5E68"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:5E68"
SQ SEQUENCE 171 AA; 19266 MW; 653B89330FE461A2 CRC64;
MPLLDSFAVD HTRMQAPAVR GAKTMNTPHG DAITVFDLRF CIPNKEVMPE KGIHTLEHLF
AGFMRDHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV ADAWKAAMAD VLKVQDQNQI
PELNVYQCGT YQMHSLSEAQ DIARHILERD VRVNSNKELA LPKEKLQELH I
