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LUXJ_ALIF1
ID   LUXJ_ALIF1              Reviewed;         193 AA.
AC   P35328; Q5DZ02;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Acyl-homoserine-lactone synthase;
DE            EC=2.3.1.184;
DE   AltName: Full=Autoinducer synthesis protein LuxI;
GN   Name=luxI; OrderedLocusNames=VF_A0924;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gray K.M., Greenberg E.P.;
RT   "Sequencing and analysis of luxR and luxI, the luminescence regulatory
RT   genes from the squid light organ symbiont Vibrio fischeri ES114.";
RL   Mol. Mar. Biol. Biotechnol. 1:414-419(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW87994.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M96844; AAA27543.1; -; Genomic_DNA.
DR   EMBL; CP000021; AAW87994.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_047863343.1; NC_006841.2.
DR   RefSeq; YP_206882.1; NC_006841.2.
DR   AlphaFoldDB; P35328; -.
DR   SMR; P35328; -.
DR   STRING; 312309.VF_A0924; -.
DR   EnsemblBacteria; AAW87994; AAW87994; VF_A0924.
DR   KEGG; vfi:VF_A0924; -.
DR   PATRIC; fig|312309.11.peg.3526; -.
DR   eggNOG; COG3916; Bacteria.
DR   HOGENOM; CLU_085711_2_1_6; -.
DR   OrthoDB; 1725271at2; -.
DR   Proteomes; UP000000537; Chromosome II.
DR   GO; GO:0061579; F:N-acyl homoserine lactone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
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; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..193
FT                   /note="Acyl-homoserine-lactone synthase"
FT                   /id="PRO_0000210889"
SQ   SEQUENCE   193 AA;  22014 MW;  A300D104637AF801 CRC64;
     MAVMIKKSDF LGIPSEEYRG ILSLRYQVFK RRLEWDLVSE DNLESDEYDN SNAEYIYACD
     DAEEVNGCWR LLPTTGDYML KTVFPELLGD QVAPRDPNIV ELSRFAVGKN SSKINNSASE
     ITMKLFQAIY KHAVSQGITE YVTVTSIAIE RFLKRIKVPC HRIGDKEIHL LGNTRSVVLS
     MPINDQFRKA VSN
 
 
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