ID   LUXC_PHOLU              Reviewed;         480 AA.
AC   P23113; Q56820;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   25-MAY-2022, entry version 78.
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;
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: 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; M62917; AAA63563.1; -; Genomic_DNA.
DR   EMBL; M90092; AAD05355.1; -; Genomic_DNA.
DR   PIR; A42951; A42951.
DR   AlphaFoldDB; P23113; -.
DR   SMR; P23113; -.
DR   UniPathway; UPA00569; -.
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.
FT   CHAIN           1..480
FT                   /note="Long-chain acyl-protein thioester reductase"
FT                   /id="PRO_0000220199"
FT   CONFLICT        2..3
FT                   /note="NK -> PP (in Ref. 1; AAA63563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="T -> P (in Ref. 1; AAA63563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86..95
FT                   /note="LKRYMGYSEE -> PKKIYGIFRR (in Ref. 1; AAA63563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="W -> R (in Ref. 1; AAA63563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="D -> V (in Ref. 1; AAA63563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="Y -> D (in Ref. 1; AAA63563)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   480 AA;  54847 MW;  57C40EF27BB3810D CRC64;
     MNKKISFIIN GRVEIFPESD DLVQSINFGD NSVHLPVLND SQVKNIIDYN ENNELQLHNI
     INFLYTVGQR WKNEEYSRRR TYIRDLKRYM GYSEEMAKLE ANWISMILCS KGGLYDLVKN
     ELGSRHIMDE WLPQDESYIR AFPKGKSVHL LTGNVPLSGV LSILRAILTK NQCIIKTSST
     DPFTANALAL SFIDVDPHHP VTRSLSVVYW QHQGDISLAK EIMQHADVVV AWGGEDAINW
     AVKHAPPDID VMKFGPKKSF CIIDNPVDLV SAATGAAHDV CFYDQQACFS TQNIYYMGSH
     YEEFKLALIE KLNLYAHILP NTKKDFDEKA AYSLVQKECL FAGLKVEVDV HQRWMVIESN
     AGVELNQPLG RCVYLHHVDN IEQILPYVRK NKTQTISVFP WEAALKYRDL LALKGAERIV
     EAGMNNIFRV GGAHDGMRPL QRLVTYISHE RPSHYTAKDV AVEIEQTRFL EEDKFLVFVP