ID   LUXD_ALIFM              Reviewed;         307 AA.
AC   B5EV70;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Acyl transferase {ECO:0000255|HAMAP-Rule:MF_00774};
DE            Short=ACT {ECO:0000255|HAMAP-Rule:MF_00774};
DE            EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_00774};
DE   AltName: Full=C14ACP-TE {ECO:0000255|HAMAP-Rule:MF_00774};
DE   AltName: Full=Myristoyl-ACP-specific thioesterase {ECO:0000255|HAMAP-Rule:MF_00774};
GN   Name=luxD {ECO:0000255|HAMAP-Rule:MF_00774};
GN   OrderedLocusNames=VFMJ11_A1040;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acyl transferase is part of the fatty acid reductase system
CC       required for aldehyde biosynthesis; it produces fatty acids for the
CC       luminescent reaction. {ECO:0000255|HAMAP-Rule:MF_00774}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid reduction for biolumincescence.
CC       {ECO:0000255|HAMAP-Rule:MF_00774}.
CC   -!- SIMILARITY: Belongs to the LuxD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00774}.
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DR   EMBL; CP001133; ACH64605.1; -; Genomic_DNA.
DR   RefSeq; WP_012535652.1; NC_011186.1.
DR   AlphaFoldDB; B5EV70; -.
DR   SMR; B5EV70; -.
DR   ESTHER; vibfi-LUXD; Thioesterase_acyl-transferase.
DR   EnsemblBacteria; ACH64605; ACH64605; VFMJ11_A1040.
DR   KEGG; vfm:VFMJ11_A1040; -.
DR   HOGENOM; CLU_882365_0_0_6; -.
DR   OMA; FARRMDH; -.
DR   UniPathway; UPA00569; -.
DR   Proteomes; UP000001857; Chromosome II.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-UniRule.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_00774; LuxD; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003157; LuxD.
DR   Pfam; PF02273; Acyl_transf_2; 1.
DR   PIRSF; PIRSF009416; LuxD; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Luminescence; Transferase.
FT   CHAIN           1..307
FT                   /note="Acyl transferase"
FT                   /id="PRO_1000200690"
FT   ACT_SITE        116
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00774"
FT   ACT_SITE        213
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00774"
FT   ACT_SITE        243
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00774"
SQ   SEQUENCE   307 AA;  34400 MW;  33911884E268375A CRC64;
     MKDESALFTI DHIIKLDNGQ SIRVWETLPK KNVPEKKNTI LIASGFARRM DHFAGLAEYL
     STNGFHVIRY DSLHHVGLSS GCINEFTMSI GKNSLLTVVD WLTDHGVERI GLIAASLSAR
     IAYEVVNKIK LSFLITAVGV VNLRDTLEKA LEYDYLQLPI SELPEDLDFE GHNLGSEVFV
     TDCFKHDWDT LDSTLNSVKG LAIPFIAFTA NDDSWVKQSE VIELIDSIES SNCKLYSLIG
     SSHDLGENLV VLRNFYQSVT KAALALDDGL LDLEIDIIEP RFEDVTSITV KERRLKNEIE
     NELLELA