ID   LUXD_PHOPO              Reviewed;         306 AA.
AC   P41302;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 59.
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   Photobacterium phosphoreum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2071574; DOI=10.1016/s0021-9258(18)98772-7;
RA   Ferri S.R., Meighen E.A.;
RT   "A lux-specific myristoyl transferase in luminescent bacteria related to
RT   eukaryotic serine esterases.";
RL   J. Biol. Chem. 266:12852-12857(1991).
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; M64224; AAA25626.1; -; Genomic_DNA.
DR   PIR; A39853; A39853.
DR   AlphaFoldDB; P41302; -.
DR   SMR; P41302; -.
DR   STRING; 659.AYY26_10990; -.
DR   ESTHER; phopo-luxd; Thioesterase_acyl-transferase.
DR   PRIDE; P41302; -.
DR   BioCyc; MetaCyc:MON-19533; -.
DR   UniPathway; UPA00569; -.
DR   GO; GO:0016746; F:acyltransferase activity; IDA:CACAO.
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..306
FT                   /note="Acyl transferase"
FT                   /id="PRO_0000220192"
FT   ACT_SITE        117
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00774"
FT   ACT_SITE        214
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00774"
FT   ACT_SITE        244
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00774"
SQ   SEQUENCE   306 AA;  34418 MW;  CA2A53B0CC166A8E CRC64;
     MKSENNSVPI DHVIKVDNER HIRVWETFPK NQCDKRNNTI VIASGFARRM DHFAGLAEYL
     STNGFHVIRY DSLNHVGLSS GEIDQFSMSV GKKSLLTVID WLKSEHGIDQ VGLIASSLSA
     RIAYDIVADV NLSFLITAVG VVNLRNTLEQ ALKYDYLQME IDEIPEDLDF DGYNLGSKVF
     VTDCFENNWD TLDSTINKTK NLNVPFIAFV ANDDSWVQQH EVEELMSNIN SDKTKIYSLI
     GSSHDLGENL IVLRNFYQSI TKAAIALDSN LVGLVSEIIE PQFEALTIAT VNERRLKNKI
     QSKSLA