ID   LUXE_PHOLE              Reviewed;         373 AA.
AC   P29334;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   02-SEP-2026, entry version 71.
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   Photobacterium leiognathi.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=553611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25521 / DSM 21260 / CCUG 16229 / CIP 66.5 / NCIMB 2193 /
RC   L1;
RX   PubMed=1915359; DOI=10.1111/j.1432-1033.1991.tb16269.x;
RA   Lee C.Y., Szittner R.B., Meighen E.A.;
RT   "The lux genes of the luminous bacterial symbiont, Photobacterium
RT   leiognathi, of the ponyfish. Nucleotide sequence, difference in gene
RT   organization, and high expression in mutant Escherichia coli.";
RL   Eur. J. Biochem. 201:161-167(1991).
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 + L-cysteinyl-[protein] + ATP = an S-
CC         (long-chain fatty acyl)-L-cysteinyl-[protein] + AMP + diphosphate;
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; M63594; AAA25620.1; -; Genomic_DNA.
DR   PIR; S17955; S17955.
DR   AlphaFoldDB; P29334; -.
DR   SMR; P29334; -.
DR   STRING; 553611.GCA_001557755_01578; -.
DR   UniPathway; UPA00569; -.
DR   GO; GO:0047474; F:long-chain fatty acid--protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008218; P:bioluminescence; IEA:InterPro.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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..373
FT                   /note="Long-chain-fatty-acid--luciferin-component ligase"
FT                   /id="PRO_0000208063"
SQ   SEQUENCE   373 AA;  43099 MW;  1B31848B00BF9921 CRC64;
     MSTLLNIDAT EIKVSTEIDD IIFTSSPLTL LFEDQEKIQK ELILESFHYH YNHNKDYKYY
     CNIQGVDENI QSIDDIPVFP TSMFKYSRLH TADESNIENW FTSSGTKGVK SHIARDRQSI
     ERLLGSVNYG MKYLGEFHEH QLELVNMGPD RFSASNVWFK YVMSLVQLLY PTTFTVENDE
     IDFEQTILAL KAIQRKGKGI CLIGPPYFIY LLCHYMKEHN IEFNAGAHMF IITGGGWKTK
     QKEALNRQDF NQLLMETFSL FHESQIRDIF NQVELNTCFF EDSLQRKHVP PWVYARALDP
     VTLTPVEDGQ EGLMSYMDAS STSYPTFIVT DDIGIVRHLK EPDPFQGTTV EIVRRLNTRE
     QKGCSLSMAT SLK
//