ID   LUXE_VIBHA              Reviewed;         378 AA.
AC   P14286; Q56697;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Long-chain-fatty-acid--luciferin-component ligase;
DE            EC=6.2.1.19;
DE   AltName: Full=Acyl-protein synthetase;
GN   Name=luxE;
OS   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2775296; DOI=10.1016/0006-291x(89)92103-7;
RA   Johnston T.C., Hruska K.S., Adams L.F.;
RT   "The nucleotide sequence of the luxE gene of Vibrio harveyi and a
RT   comparison of the amino acid sequences of the acyl-protein synthetases from
RT   V. harveyi and V. fischeri.";
RL   Biochem. Biophys. Res. Commun. 163:93-101(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 370-378.
RX   PubMed=2303459; DOI=10.1016/s0021-9258(19)39798-4;
RA   Swartzman E., Miyamoto C., Graham A., Meighen E.;
RT   "Delineation of the transcriptional boundaries of the lux operon of Vibrio
RT   harveyi demonstrates the presence of two new lux genes.";
RL   J. Biol. Chem. 265:3513-3517(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
RX   PubMed=3514602; DOI=10.1016/s0021-9258(19)89176-7;
RA   Johnston T.C., Thompson R.B., Baldwin T.O.;
RT   "Nucleotide sequence of the luxB gene of Vibrio harveyi and the complete
RT   amino acid sequence of the beta subunit of bacterial luciferase.";
RL   J. Biol. Chem. 261:4805-4811(1986).
CC   -!- FUNCTION: Acyl-protein synthetase activates tetradecanoic acid. It is a
CC       component of the fatty acid reductase complex responsible for
CC       converting tetradecanoic acid to the aldehyde which serves as substrate
CC       in the luciferase-catalyzed reaction.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + L-cysteinyl-[protein] = AMP +
CC         diphosphate + S-(long-chain fatty acyl)-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:20101, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12762,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57560, ChEBI:CHEBI:133479, ChEBI:CHEBI:456215;
CC         EC=6.2.1.19;
CC   -!- PATHWAY: Lipid metabolism; fatty acid reduction for biolumincescence.
CC   -!- SIMILARITY: Belongs to the LuxE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA88687.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M28815; AAA27531.1; -; Genomic_DNA.
DR   EMBL; M27139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M10961; AAA88687.1; ALT_INIT; Genomic_DNA.
DR   PIR; A32916; A32916.
DR   AlphaFoldDB; P14286; -.
DR   SMR; P14286; -.
DR   UniPathway; UPA00569; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047474; F:long-chain fatty acid luciferin component ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR007534; LuxE.
DR   InterPro; IPR016671; LuxE_bac.
DR   Pfam; PF04443; LuxE; 1.
DR   PIRSF; PIRSF016580; Acyl-protein_synthetase_LuxE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Luminescence; Nucleotide-binding.
FT   CHAIN           1..378
FT                   /note="Long-chain-fatty-acid--luciferin-component ligase"
FT                   /id="PRO_0000208066"
SQ   SEQUENCE   378 AA;  42960 MW;  985E6AE65425DB92 CRC64;
     MDVLSAVKQE NIAASTEIDD LIFMGTPQQW SLQEQKQLTS RLVKGAYQYH YHNNDDYRQF
     CERLGVGEVV EDLNDIPVFP TSIFKLKTLL TLDDDEVENR FTSSGTSGIK SIVARDRLSI
     ERLLGSVNFG MNYVGDWFDH QMELVNLGPD RFNANNIWFK YVMSLVELLY PTAFTVTEDE
     IDFEATLANM NRIKQSGKTI CLIGPPYFIY LLCCFMREQG QTFNGGRDLY IITGGGWKKH
     QDQSLDRDEF NQLLCETFTL ESPEQIRDTF NQEELNTCFF EDTEHKNGVP PWVFARALDP
     KTLKPLPHGQ SGLMSYMDAS AVSYPCFLVT DDIGIVREEE GDRPGTTVEI VRRVKTRGMK
     GCALSMSQAF TAKNDGGN