ID   LUXE_PHOLU              Reviewed;         116 AA.
AC   P19842;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 3.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Long-chain-fatty-acid--luciferin-component ligase;
DE            EC=6.2.1.19;
DE   AltName: Full=Acyl-protein synthetase;
DE   Flags: Fragment;
GN   Name=luxE;
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] OF 1-37.
RC   STRAIN=Hm;
RX   PubMed=2383248; DOI=10.1016/0006-291x(90)92106-a;
RA   Johnston T.C., Rucker E.B., Cochrum L., Hruska K.S., Vandegrift V.;
RT   "The nucleotide sequence of the luxA and luxB genes of Xenorhabdus
RT   luminescens HM and a comparison of the amino acid sequences of luciferases
RT   from four species of bioluminescent bacteria.";
RL   Biochem. Biophys. Res. Commun. 170:407-415(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
RC   STRAIN=ATCC 29999 / DSM 3368 / BCRC 14801 / CIP 106429 / NCIMB 12670 / Hb;
RX   PubMed=2204626; DOI=10.1016/s0021-9258(17)46262-4;
RA   Szittner R., Meighen E.;
RT   "Nucleotide sequence, expression, and properties of luciferase coded by lux
RT   genes from a terrestrial bacterium.";
RL   J. Biol. Chem. 265:16581-16587(1990).
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}.
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DR   EMBL; M62917; AAA63567.1; -; Genomic_DNA.
DR   EMBL; M57416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M55977; AAA27628.1; -; Genomic_DNA.
DR   AlphaFoldDB; P19842; -.
DR   STRING; 29488.KS18_21630; -.
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   InterPro; IPR007534; LuxE.
DR   Pfam; PF04443; LuxE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Luminescence; Nucleotide-binding.
FT   CHAIN           1..>116
FT                   /note="Long-chain-fatty-acid--luciferin-component ligase"
FT                   /id="PRO_0000208064"
FT   NON_TER         116
SQ   SEQUENCE   116 AA;  13575 MW;  4E7C717FD749CAC5 CRC64;
     MTSYVDKQEI TASSEIDDLI FSSDPLVCAY DEQEKIRKKL VLDAFRHHYK HCQEYRHYCQ
     AHKVDDNITE IDDIPVFPTS VFKFTRLLTS NENEIESWFT SSGTNGLKSQ VPRDRL