ID   LUXC1_PHOLE             Reviewed;         478 AA.
AC   Q03324;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Long-chain acyl-protein thioester reductase 1 {ECO:0000305};
DE            EC=1.2.1.50 {ECO:0000250|UniProtKB:P19841};
DE   AltName: Full=Acyl-CoA reductase 1;
GN   Name=luxC;
OS   Photobacterium leiognathi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=553611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=741;
RX   PubMed=8447834; DOI=10.1006/bbrc.1993.1219;
RA   Lin J.-W., Chao Y.-F., Weng S.-F.;
RT   "Nucleotide sequence of the luxC gene encoding fatty acid reductase of the
RT   lux operon from Photobacterium leiognathi.";
RL   Biochem. Biophys. Res. Commun. 191:314-318(1993).
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; X65156; CAA46274.1; -; Genomic_DNA.
DR   PIR; JC1475; JC1475.
DR   AlphaFoldDB; Q03324; -.
DR   SMR; Q03324; -.
DR   STRING; 553611.GCA_001557755_01583; -.
DR   KEGG; ag:CAA46274; -.
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..478
FT                   /note="Long-chain acyl-protein thioester reductase 1"
FT                   /id="PRO_0000220196"
SQ   SEQUENCE   478 AA;  53858 MW;  D730A3BE2462086B CRC64;
     MIKKIPLIIG GEVQDTSEHD VRELTLNNNT VNVPIITDKD AESITSLKIE NKLNINQIVN
     FLYTVGQKWK SENYSRRLTY IRDLVKFMGY SPEMAKLEAN WISMILCSKS ALYDIVENDL
     SSRHIVDEWL PQGDCYVKAL PKGKSIHLLA GNVPLSGVTS ILRAILTKNE CIIKTSSADP
     FTATALASSF IDTDANHPIT RSMSVMYWSH NEDITIPQKI MNCADVVVAW GGNDAIKWAT
     KHSPAHVDIL KFGPKKSISI VDNPTDIKAA AIGVAHDICF YDQQACFSTQ DIYYMGDKLD
     VFFDELTKQL NIYKVILPKG DQSFDEKGAF SLTERECLFA KYKVQKGEEQ AWLLTQSPAG
     TFGNQPLSRS AYIHHVNDIS EITPYIQNDI TQTVSITPWE ASFKYRDTLA SHGAERIIES
     GMNNIFRVGG AHDGMRPLQR LVKYISHERP STYTTKDVAV KIEQTRYLEE DKFLVFVP