ID   LUXC_PHOLL              Reviewed;         480 AA.
AC   Q7N577;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Long-chain acyl-protein thioester reductase {ECO:0000305};
DE            EC=1.2.1.50 {ECO:0000250|UniProtKB:P19841};
DE   AltName: Full=Acyl-CoA reductase;
GN   Name=luxC; OrderedLocusNames=plu2079;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
CC   -!- FUNCTION: LuxC is the fatty acid reductase enzyme responsible for
CC       synthesis of the aldehyde substrate for the luminescent reaction
CC       catalyzed by luciferase. {ECO:0000250|UniProtKB:P19841}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty aldehyde + CoA + NADP(+) = a long-chain
CC         fatty acyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:15437,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17176, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83139; EC=1.2.1.50;
CC         Evidence={ECO:0000250|UniProtKB:P19841};
CC   -!- PATHWAY: Lipid metabolism; fatty acid reduction for biolumincescence.
CC   -!- SIMILARITY: Belongs to the LuxC family. {ECO:0000305}.
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DR   EMBL; BX571866; CAE14372.1; -; Genomic_DNA.
DR   RefSeq; WP_011146334.1; NC_005126.1.
DR   AlphaFoldDB; Q7N577; -.
DR   SMR; Q7N577; -.
DR   STRING; 243265.plu2079; -.
DR   EnsemblBacteria; CAE14372; CAE14372; plu2079.
DR   GeneID; 24166560; -.
DR   KEGG; plu:plu2079; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_567216_0_0_6; -.
DR   OMA; PEAGWHH; -.
DR   OrthoDB; 1776958at2; -.
DR   BioCyc; PLUM243265:PLU_RS10385-MON; -.
DR   UniPathway; UPA00569; -.
DR   Proteomes; UP000002514; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050062; F:long-chain-fatty-acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR   CDD; cd07080; ALDH_Acyl-CoA-Red_LuxC; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR008670; CoA_reduct_LuxC.
DR   Pfam; PF05893; LuxC; 1.
DR   PIRSF; PIRSF009414; LuxC; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
PE   3: Inferred from homology;
KW   Luminescence; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..480
FT                   /note="Long-chain acyl-protein thioester reductase"
FT                   /id="PRO_0000220198"
SQ   SEQUENCE   480 AA;  54815 MW;  48DC9106D75662BB CRC64;
     MTKKISFIIN GQVEIFPESD DLVQSINFGD NSVYLPILNN SHVKNIIDYN ENNKLRLHNI
     VNFLYTVGQR WKNEEYSRRR TYIRDLKKYM GYSEAMAKLE ANWISMILCS KGGLYDVVEN
     ELGSRHIMDE WLPQDESYIK AFPKGKSIHL LAGNVPLSGI MSILRAILTK NQCIIKTSST
     DPFTANALAL SFIDVDPNHP ITRSLSVVYW PHQGDTSLAK EIMQHMDVIV AWGGEDAINW
     AVEHAPPYAD VIKFGSKKSF CIIDNPVDLT SAATGAAHDI CFYDQRACFS AQNIYYMGNQ
     YEEFKLALIE KLNLYAHILP NAKKDFDEKA AYSLVQKESL FAGLKVEVDV HQRWMIIESN
     AGVEFNQPLG RCVYLHHVDN IEQVLPYVQK NKTQTISIFP WESAFKYRDA LALRGAERIV
     EAGMNNIFRV GGSHDGMRPL QRLVTYISHE RPSHYTAKDV AVEIEQTRFL EEDKFLVFVP