ID   LUXD_ALIFS              Reviewed;         307 AA.
AC   Q9S3Z2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 51.
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};
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=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: 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF170104; AAD48476.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S3Z2; -.
DR   SMR; Q9S3Z2; -.
DR   ESTHER; vibfi-LUXD; Thioesterase_acyl-transferase.
DR   UniPathway; UPA00569; -.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0008218; P:bioluminescence; IMP:CACAO.
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_0000220194"
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;  34456 MW;  3E22C4738A4B61B4 CRC64;
     MKDESAFFTI DHIIKLDNGQ SIRVWETLPK KNVPEKKHTI LIASGFARRM DHFAGLAEYL
     STNGFHVIRY DSLHHVGLSS GCINEFTMSI GKNSLLTVVD WLTDHGVERI GLIAASLSAR
     IAYEVVNKIK LSFLITAVGV VNLRDTLEKA LEYDYLQLPI SELPEDLDFE GHNLGSEVFV
     TDCFKHNWDT LDSTLNSVKG LAIPFIAFTA NDDSWVKQSE VIELIDSIES SNCKLYSLIG
     SSHDLGENLV VLRNFYQSVT KAALALDDGL LDLEIDIIEP RFEDVTSITV KERRLKNEIE
     NELLELA