ID   LUXC_PHOPO              Reviewed;         488 AA.
AC   P19841; A8R7C6;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 3.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Long-chain acyl-protein thioester reductase {ECO:0000305};
DE            EC=1.2.1.50 {ECO:0000269|PubMed:7085612};
DE   AltName: Full=Acyl-CoA reductase;
GN   Name=luxC;
OS   Photobacterium phosphoreum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ABC {ECO:0000312|EMBL:BAF92773.1};
RA   Kasai S.;
RT   "Nucleotide sequence of the lux operon and its upstream region of
RT   Photobacterium phosphoreum, strain ABC.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-371.
RC   STRAIN=A13;
RX   PubMed=2243804; DOI=10.1093/nar/18.21.6450;
RA   Prasher D.C., O'Kane D., Lee J., Woodward B.;
RT   "The lumazine protein gene in Photobacterium phosphoreum is linked to the
RT   lux operon.";
RL   Nucleic Acids Res. 18:6450-6450(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 478-488.
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).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=7085612; DOI=10.1016/s0021-9258(18)34515-0;
RA   Riendeau D., Rodriguez A., Meighen E.;
RT   "Resolution of the fatty acid reductase from Photobacterium phosphoreum
RT   into acyl protein synthetase and acyl-CoA reductase activities. Evidence
RT   for an enzyme complex.";
RL   J. Biol. Chem. 257:6908-6915(1982).
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:0000269|PubMed:7085612}.
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:0000269|PubMed:7085612};
CC   -!- PATHWAY: Lipid metabolism; fatty acid reduction for biolumincescence.
CC   -!- SIMILARITY: Belongs to the LuxC family. {ECO:0000305}.
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DR   EMBL; AB367391; BAF92773.1; -; Genomic_DNA.
DR   EMBL; X54690; CAA38506.1; -; Genomic_DNA.
DR   EMBL; M64224; AAA25625.1; -; Genomic_DNA.
DR   PIR; B39853; B39853.
DR   PIR; S12116; S12116.
DR   AlphaFoldDB; P19841; -.
DR   SMR; P19841; -.
DR   STRING; 659.AYY26_10995; -.
DR   BioCyc; MetaCyc:MON-19532; -.
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; IDA:CACAO.
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   1: Evidence at protein level;
KW   Luminescence; NADP; Oxidoreductase.
FT   CHAIN           1..488
FT                   /note="Long-chain acyl-protein thioester reductase"
FT                   /id="PRO_0000220200"
FT   CONFLICT        58
FT                   /note="S -> N (in Ref. 2; CAA38506)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   488 AA;  55238 MW;  71A5A06BBA43C993 CRC64;
     MCNAEFKGDC MIKKIPMIIG GAERDTSEHE YRELTLNSYK VSIPIINQDD VEAIKSQSVE
     NNLNINQIVN FLYTVGQKWK SENYSRRLTY IRDLVRFLGY SPEMAKLEAN WISMILSSKS
     ALYDIVETEL GSRHIVDEWL PQGDCYVKAM PKGKSVHLLA GNVPLSGVTS IIRAILTKNE
     CIIKTSSADP FTAIALASSF IDTDEHHPIS RSMSVMYWSH NEDIAIPQQI MNCADVVVSW
     GGYDAIKWAT EHTPVNVDIL KFGPKKSIAI VDNPVDITAS AIGVAHDICF YDQQACFSTQ
     DIYYIGDNID AFFDELVEQL NLYMDILPKG DQTFDEKASF SLIEKECQFA KYKVEKGDNQ
     SWLLVKSPLG SFGNQPLARS AYIHHVSDIS EITPYIENRI TQTVTVTPWE SSFKYRDVLA
     SHGAERIVES GMNNIFRVGG AHDGMRPLQR LVKYISHERP YTYSTKDVAV KIEQTRYLEE
     DKFLVFVP