ID   LUXD2_PHOLU             Reviewed;         307 AA.
AC   P23148;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 67.
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   Photorhabdus luminescens (Xenorhabdus luminescens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=29488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hw;
RX   PubMed=1995589; DOI=10.1128/jb.173.4.1399-1405.1991;
RA   Xi L., Cho K.W., Tu S.C.;
RT   "Cloning and nucleotide sequences of lux genes and characterization of
RT   luciferase of Xenorhabdus luminescens from a human wound.";
RL   J. Bacteriol. 173:1399-1405(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hw;
RX   PubMed=1644764; DOI=10.1128/jb.174.16.5371-5381.1992;
RA   Meighen E.A., Szittner R.B.;
RT   "Multiple repetitive elements and organization of the lux operons of
RT   luminescent terrestrial bacteria.";
RL   J. Bacteriol. 174:5371-5381(1992).
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.
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; M90092; AAD05356.1; -; Genomic_DNA.
DR   EMBL; M62917; AAA63564.1; -; Genomic_DNA.
DR   PIR; B38448; B38448.
DR   AlphaFoldDB; P23148; -.
DR   SMR; P23148; -.
DR   ESTHER; pholu-lxd2; 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; 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_0000220191"
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;  34583 MW;  A26244FDAEEFC8F6 CRC64;
     MENKSRYKTI DHVICVEENR KIHVWETLPK ENSPKRKNTL IIASGFARRM DHFAGLAEYL
     SQNGFHVIRY DSLHHVGLSS GTIDEFTMSI GKQSLLAVVD WLNTRKINNL GMLASSLSAR
     IAYASLSEIN VSFLITAVGV VNLRYTLERA LGFDYLSLPI DELPDNLDFE GHKLGAEVFA
     RDCFDSGWED LTSTINSMMH LDIPFIAFTA NNDDWVKQDE VITLLSSIRS HQCKIYSLLG
     SSHDLGENLV VLRNFYQSVT KAAIAMDNGC LDIDVDIIEP SFEHLTIAAV NERRMKIEIE
     NQVISLS