ID   LUXD1_PHOLE             Reviewed;         315 AA.
AC   P21309;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   25-MAY-2022, entry version 80.
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 leiognathi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=553611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25521 / DSM 21260 / CIP 66.5 / NCIMB 2193 / L1;
RX   PubMed=1915359; DOI=10.1111/j.1432-1033.1991.tb16269.x;
RA   Lee C.Y., Szittner R.B., Meighen E.A.;
RT   "The lux genes of the luminous bacterial symbiont, Photobacterium
RT   leiognathi, of the ponyfish. Nucleotide sequence, difference in gene
RT   organization, and high expression in mutant Escherichia coli.";
RL   Eur. J. Biochem. 201:161-167(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-307.
RC   STRAIN=554;
RX   PubMed=2311938; DOI=10.1016/0378-1119(90)90117-a;
RA   Illarionov B.A., Blinov V.M., Donchenko A.P., Protopopova M.V.,
RA   Karginov V.A., Mertvetsov N.P., Gitelson J.I.;
RT   "Isolation of bioluminescent functions from Photobacterium leiognathi:
RT   analysis of luxA, luxB, luxG and neighboring genes.";
RL   Gene 86:89-94(1990).
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}.
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; M63594; AAA25617.1; -; Genomic_DNA.
DR   EMBL; X08036; CAA30830.1; -; Genomic_DNA.
DR   PIR; PQ0049; PQ0049.
DR   PIR; S17952; S17952.
DR   RefSeq; WP_045065774.1; NZ_PYOI01000014.1.
DR   AlphaFoldDB; P21309; -.
DR   SMR; P21309; -.
DR   ESTHER; phole-lxd1; Thioesterase_acyl-transferase.
DR   PATRIC; fig|553611.3.peg.3622; -.
DR   OrthoDB; 631878at2; -.
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..315
FT                   /note="Acyl transferase"
FT                   /id="PRO_0000220187"
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"
FT   CONFLICT        261
FT                   /note="K -> R (in Ref. 2; CAA30830)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        264..265
FT                   /note="VS -> IG (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        268..272
FT                   /note="RQLVE -> SEVID (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276..278
FT                   /note="EII -> DIS (in Ref. 2; CAA30830)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="V -> I (in Ref. 2; CAA30830)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303..307
FT                   /note="IINRL -> MFASA (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   315 AA;  35742 MW;  7D4DD3902AE92452 CRC64;
     MENTQHSLPI DHVIDIGDNR YIRVWETKPK NKETKRNNTI VIASGFARRM DHFAGLAEYL
     ANNGFRVIRY DSLNHVGLSS GEIKQFSMSV GKHSLLTVID WLKERNINNI GLIASSLSAR
     IAYEVAAEID LSFLITAVGV VNLRSTLEKA LKYDYLQMEV NTIPEDLIFE GHNLGSKVFV
     TDCFENNWDS LDSTINKICE LDIPFIAFTS DGDDWVCQHE VKHLVSNVKS DKKKIYSLVG
     SSHDLGENLV VLRNFYQSMT KAAVSLDRQL VELVDEIIEP NFEDLTVITV NERRLKNKIE
     NEIINRLADR VLASV