LUXC_ALIFS
ID LUXC_ALIFS Reviewed; 479 AA.
AC P12748; Q9S3Z3;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 3.
DT 25-MAY-2022, entry version 83.
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 Aliivibrio fischeri (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MJ-1;
RA Knight T., Papadakis N.;
RT "Vibrio fischeri Lux operon SalI digest.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RX PubMed=3697093; DOI=10.1093/nar/15.24.10455;
RA Engebrecht J., Silverman M.;
RT "Nucleotide sequence of the regulatory locus controlling expression of
RT bacterial genes for bioluminescence.";
RL Nucleic Acids Res. 15:10455-10467(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RC STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
RA Devine J.H., Countryman C., Baldwin T.O.;
RT "Nucleotide sequence of the luxR and luxI genes and structure of the
RT primary regulatory region of the lux regulon of Vibrio fischeri ATCC
RT 7744.";
RL Biochemistry 27:837-842(1988).
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; AF170104; AAD48475.1; -; Genomic_DNA.
DR EMBL; M19039; AAA27553.1; -; Genomic_DNA.
DR EMBL; Y00509; CAA68563.1; -; Genomic_DNA.
DR PIR; S06862; S06862.
DR AlphaFoldDB; P12748; -.
DR SMR; P12748; -.
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; IMP:CACAO.
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..479
FT /note="Long-chain acyl-protein thioester reductase"
FT /id="PRO_0000220201"
SQ SEQUENCE 479 AA; 54578 MW; 10FD9567E5026340 CRC64;
MNKCIPMIIN GMIQDFDNYA YKEVKLNNDN RVKLSVITES SVSKTLNIKD RINLNLNQIV
NFLYTVGQRW KSEEYNRRRT YIRELKTYLG YSDEMARLEA NWIAMLLCSK SALYDIVNYD
LGSIHVLDEW LPRGDCYVKA QPKGVSVHLL AGNVPLSGVT SILRAILTKN ECIIKTSSSD
PFTANALVSS FIDVNADHPI TKSMSVMYWP HDEDMTLSQR IMNHADVVIA WGGDEAIKWA
VKYSPPHVDI LKFGPKKSLS IIEAPKDIEA AAMGVAHDIC FYDQQACFST QDVYYIGDNL
PLFLNELEKQ LDRYAKILPK GSNSFDEKAA FTLTEKESLF AGYEVRKGDK QAWLIVVSPT
NSFGNQPLSR SVYVHQVSDI KEIIPFVNKN RTQTVSIYPW EASLKYRDKL ARSGVERIVE
SGMNNIFRVG GAHDSLSPLQ YLVRFVSHER PFNYTTKDVA VEIEQTRYLE EDKFLVFVP
