ID   LUXE_ALIFS              Reviewed;         378 AA.
AC   P24272; Q9S3Z0;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 2.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Long-chain-fatty-acid--luciferin-component ligase {ECO:0000305};
DE            EC=6.2.1.19 {ECO:0000250};
DE   AltName: Full=Acyl-protein synthetase {ECO:0000305};
GN   Name=luxE {ECO:0000312|EMBL:AAD48479.1};
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 {ECO:0000312|EMBL:AAD48479.1};
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 376-378.
RC   STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
RX   PubMed=2254256; DOI=10.1128/jb.172.12.6797-6802.1990;
RA   Swartzman E., Kapoor S., Graham A.F., Meighen E.A.;
RT   "A new Vibrio fischeri lux gene precedes a bidirectional termination site
RT   for the lux operon.";
RL   J. Bacteriol. 172:6797-6802(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. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; fatty acid reduction for biolumincescence.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LuxE family. {ECO:0000305}.
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DR   EMBL; AF170104; AAD48479.1; -; Genomic_DNA.
DR   EMBL; M62812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_005423445.1; NZ_WOBZ01000007.1.
DR   AlphaFoldDB; P24272; -.
DR   SMR; P24272; -.
DR   GeneID; 64240409; -.
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; IMP:CACAO.
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_0000208065"
SQ   SEQUENCE   378 AA;  44281 MW;  46FF3205F963EF0A CRC64;
     MTVHTEYKRN QIIASSEIDD LIFMTKPQEW SFEEQKEIRD KLVREAFYFH YNRNEEYRNY
     CINQHVSDNL HTIDEIPVFP TSVFKYKKLH TVTAEDIENW YTSSGTRGVK SHIARDRLSI
     ERLLGSVNFG MKYVGDWFEH QMELINLGPD RFNTNNIWFK YVMSLVELLY PTEFTVDNDK
     IDFEKTVKHL FRIKNSKKDI CLIGPPFFVY LLCQYMKENN IEFKGGDRVH IITGGGWKSN
     QNDSLDRADF NQLLMDTFQL DKINQIRDTF NQVELNTCFF EDEFQRKHVP PWVYARALDP
     ETLKPVADGE IGLLSYMDAS STAYPAFIVT DDIGIVKEIR EPDPYPGVTV EIVRRLNTRA
     QKGCALSMAN VIQKNIKD