ID   LUXI_ALIFS              Reviewed;         193 AA.
AC   P12747;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Acyl-homoserine-lactone synthase;
DE            EC=2.3.1.184;
DE   AltName: Full=Autoinducer synthesis protein LuxI;
GN   Name=luxI;
OS   Aliivibrio fischeri (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
RA   Devine J.H., Countryman C., Baldwin T.O.;
RT   "Nucleotide sequence of the luxR and luxI genes and structure of the
RT   primary regulatory region of the lux regulon of Vibrio fischeri ATCC
RT   7744.";
RL   Biochemistry 27:837-842(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MJ-1;
RX   PubMed=3697093; DOI=10.1093/nar/15.24.10455;
RA   Engebrecht J., Silverman M.;
RT   "Nucleotide sequence of the regulatory locus controlling expression of
RT   bacterial genes for bioluminescence.";
RL   Nucleic Acids Res. 15:10455-10467(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MJ-1;
RA   Knight T., Papadakis N.;
RT   "Vibrio fischeri Lux operon SalI digest.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the synthesis of OHHL (N-(3-oxohexanoyl)-L-
CC       homoserine lactone) also known as VAI or N-(beta-ketocaproyl)homoserine
CC       lactone or 3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-hexanamide, an
CC       autoinducer molecule which binds to LuxR and thus acts in
CC       bioluminescence regulation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + S-adenosyl-L-methionine = an N-acyl-L-
CC         homoserine lactone + H(+) + holo-[ACP] + S-methyl-5'-thioadenosine;
CC         Xref=Rhea:RHEA:10096, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:55474,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC         EC=2.3.1.184;
CC   -!- SIMILARITY: Belongs to the autoinducer synthase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00533}.
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DR   EMBL; M19039; AAA27552.1; -; Genomic_DNA.
DR   EMBL; Y00509; CAA68562.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF170104; AAD48474.1; -; Genomic_DNA.
DR   PIR; B28705; B28705.
DR   RefSeq; WP_005423459.1; NZ_BMPC01000001.1.
DR   AlphaFoldDB; P12747; -.
DR   SMR; P12747; -.
DR   BioCyc; MetaCyc:MON-14564; -.
DR   GO; GO:0061579; F:N-acyl homoserine lactone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008218; P:bioluminescence; IMP:CACAO.
DR   GO; GO:0052043; P:modification by symbiont of host cellular component; IMP:CACAO.
DR   GO; GO:1905087; P:positive regulation of bioluminescence; IMP:CACAO.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR018311; Autoind_synth_CS.
DR   InterPro; IPR001690; Autoind_synthase.
DR   PANTHER; PTHR39322; PTHR39322; 1.
DR   Pfam; PF00765; Autoind_synth; 1.
DR   PRINTS; PR01549; AUTOINDCRSYN.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS00949; AUTOINDUCER_SYNTH_1; 1.
DR   PROSITE; PS51187; AUTOINDUCER_SYNTH_2; 1.
PE   3: Inferred from homology;
KW   Autoinducer synthesis; Luminescence; Quorum sensing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..193
FT                   /note="Acyl-homoserine-lactone synthase"
FT                   /id="PRO_0000210888"
SQ   SEQUENCE   193 AA;  21934 MW;  C97DA69B688E1287 CRC64;
     MTIMIKKSDF LAIPSEEYKG ILSLRYQVFK QRLEWDLVVE NNLESDEYDN SNAEYIYACD
     DTENVSGCWR LLPTTGDYML KSVFPELLGQ QSAPKDPNIV ELSRFAVGKN SSKINNSASE
     ITMKLFEAIY KHAVSQGITE YVTVTSTAIE RFLKRIKVPC HRIGDKEIHV LGDTKSVVLS
     MPINEQFKKA VLN