ID   LUXS_HELPJ              Reviewed;         152 AA.
AC   Q9ZMW8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 134.
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=jhp_0097;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS).
RX   PubMed=11435117; DOI=10.1016/s0969-2126(01)00613-x;
RA   Lewis H.A., Furlong E.B., Laubert B., Eroshkina G.A., Batiyenko Y.,
RA   Adams J.M., Bergseid M.G., Marsh C.D., Peat T.S., Sanderson W.E.,
RA   Sauder J.M., Buchanan S.G.;
RT   "A structural genomics approach to the study of quorum sensing: crystal
RT   structures of three LuxS orthologs.";
RL   Structure 9:527-537(2001).
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   -!- 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;
CC       Note=Binds 1 Fe cation per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD05688.1; -; Genomic_DNA.
DR   PIR; C71973; C71973.
DR   RefSeq; WP_000783567.1; NZ_CP011330.1.
DR   PDB; 1J6X; X-ray; 2.38 A; A/B=1-152.
DR   PDBsum; 1J6X; -.
DR   AlphaFoldDB; Q9ZMW8; -.
DR   SMR; Q9ZMW8; -.
DR   KEGG; hpj:jhp_0097; -.
DR   PATRIC; fig|85963.30.peg.931; -.
DR   eggNOG; COG1854; Bacteria.
DR   BRENDA; 4.4.1.21; 2604.
DR   EvolutionaryTrace; Q9ZMW8; -.
DR   Proteomes; UP000000804; 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   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   1: Evidence at protein level;
KW   3D-structure; Autoinducer synthesis; Iron; Lyase; Metal-binding;
KW   Quorum sensing.
FT   CHAIN           1..152
FT                   /note="S-ribosylhomocysteine lyase"
FT                   /id="PRO_0000172230"
FT   BINDING         55
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         59
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         122
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   HELIX           6..9
FT                   /evidence="ECO:0007829|PDB:1J6X"
FT   STRAND          17..27
FT                   /evidence="ECO:0007829|PDB:1J6X"
FT   STRAND          33..40
FT                   /evidence="ECO:0007829|PDB:1J6X"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:1J6X"
FT   HELIX           51..68
FT                   /evidence="ECO:0007829|PDB:1J6X"
FT   STRAND          72..77
FT                   /evidence="ECO:0007829|PDB:1J6X"
FT   STRAND          81..90
FT                   /evidence="ECO:0007829|PDB:1J6X"
FT   HELIX           94..108
FT                   /evidence="ECO:0007829|PDB:1J6X"
FT   TURN            119..121
FT                   /evidence="ECO:0007829|PDB:1J6X"
FT   TURN            123..126
FT                   /evidence="ECO:0007829|PDB:1J6X"
FT   HELIX           130..142
FT                   /evidence="ECO:0007829|PDB:1J6X"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:1J6X"
SQ   SEQUENCE   152 AA;  17424 MW;  B2E154CF36958315 CRC64;
     MKMNVESFNL DHTKVKAPYV RIADRKKGVN GDLIVKYDVR FKQPNRDHMD MPSLHSLEHL
     VAEIIRNHAN YVVDWSPMGC QTGFYLTVLN HDNYTEILEV LEKTMQDVLK AKEVPASNEK
     QCGWAANHTL EGAQNLARAF LDKRAEWSEV GV
//