ID   LUXM_VIBHA              Reviewed;         399 AA.
AC   P54298; P54297;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Acyl-homoserine-lactone synthase LuxM;
DE            Short=AHL synthase LuxM;
DE            EC=2.3.1.184;
GN   Name=luxM; Synonyms=luxL;
OS   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND FUNCTION IN HOMOSERINE LACTONE
RP   SYNTHESIS.
RC   STRAIN=BB7;
RX   PubMed=8231809; DOI=10.1111/j.1365-2958.1993.tb01737.x;
RA   Bassler B.L., Wright M.E., Showalter R.E., Silverman M.R.;
RT   "Intercellular signalling in Vibrio harveyi: sequence and function of genes
RT   regulating expression of luminescence.";
RL   Mol. Microbiol. 9:773-786(1993).
RN   [2]
RP   IDENTIFICATION OF FRAMESHIFT.
RX   PubMed=11371516; DOI=10.1128/jb.183.12.3537-3547.2001;
RA   Milton D.L., Chalker V.J., Kirke D., Hardman A., Camara M., Williams P.;
RT   "The LuxM homologue VanM from Vibrio anguillarum directs the synthesis of
RT   N-(3-hydroxyhexanoyl)homoserine lactone and N-hexanoylhomoserine lactone.";
RL   J. Bacteriol. 183:3537-3547(2001).
CC   -!- FUNCTION: Required for the synthesis of an autoinducer molecule beta-
CC       hydroxybutyryl homoserine lactone, which binds to LuxN and thus acts in
CC       bioluminescence regulation. {ECO:0000269|PubMed:8231809}.
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 LuxM / VanM family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC36806.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAC36807.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L13940; AAC36806.1; ALT_FRAME; Genomic_RNA.
DR   EMBL; L13940; AAC36807.1; ALT_FRAME; Genomic_RNA.
DR   PIR; S37348; S37348.
DR   PIR; S37349; S37349.
DR   AlphaFoldDB; P54298; -.
DR   GO; GO:0061579; F:N-acyl homoserine lactone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR   InterPro; IPR035304; AHL_synthase.
DR   Pfam; PF17327; AHL_synthase; 1.
PE   1: Evidence at protein level;
KW   Autoinducer synthesis; Quorum sensing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..399
FT                   /note="Acyl-homoserine-lactone synthase LuxM"
FT                   /id="PRO_0000084525"
SQ   SEQUENCE   399 AA;  46371 MW;  DD5479ACE2FC2807 CRC64;
     MKLMLSLGSL SANSLPIEKK QQVLIDLVIR TYQSHERTEL FKAITEYRKN QLIALFPEHA
     NKSYSIIFEL MDYRDLIERY PSTLSEEATL LEKVVGQCFM HWLDFWCECE IAAIKAKFPL
     KENELPAPQL LFEDSAYYGA LVERVEDTQL MVQIPSHPQA MPLSDAITLS NLELFIQGEK
     WYEMLSLLSL SQVGKHFIVL KHPVQDSCPT LVASALIQNW SVRDTWLSYA PQFSNEQWNY
     CFPSYGYSEF TRLQLFTPSS LSKCYSLPEF DNEFKLQLSD TQAVCEVLRL TVSGNAQQKL
     YFLYLAQKEL MSVLHQAGYK IGFTIIEQPF MLNFYRAIDA KAYFHSGYCD LNDDGKQTYR
     GFWNFEMMVK AFSNIDFRGY KRAVRASRKR GSLERDEHV