ID   LUCI_AQULA              Reviewed;         548 AA.
AC   Q01158;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Luciferin 4-monooxygenase;
DE            Short=Luciferase;
DE            EC=1.13.12.7 {ECO:0000250|UniProtKB:Q26304};
OS   Aquatica lateralis (Heike firefly) (Luciola lateralis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia; Elateroidea;
OC   Lampyridae; Luciolinae; Aquatica.
OX   NCBI_TaxID=7052;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1610896; DOI=10.1016/0167-4781(92)90071-7;
RA   Tatsumi H., Kajiyama N., Nakano E.;
RT   "Molecular cloning and expression in Escherichia coli of a cDNA clone
RT   encoding luciferase of a firefly, Luciola lateralis.";
RL   Biochim. Biophys. Acta 1131:161-165(1992).
CC   -!- FUNCTION: Produces green light. {ECO:0000250|UniProtKB:Q26304}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + firefly D-luciferin + O2 = AMP + CO2 + diphosphate +
CC         firefly oxyluciferin + hnu; Xref=Rhea:RHEA:10732, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16792, ChEBI:CHEBI:30212,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58038,
CC         ChEBI:CHEBI:456215; EC=1.13.12.7;
CC         Evidence={ECO:0000250|UniProtKB:Q26304};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; X66919; CAA47358.1; -; mRNA.
DR   PIR; S23437; S23437.
DR   AlphaFoldDB; Q01158; -.
DR   SMR; Q01158; -.
DR   BindingDB; Q01158; -.
DR   ChEMBL; CHEMBL3701; -.
DR   BRENDA; 1.13.12.7; 3081.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0047077; F:Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Luminescence; Magnesium; Metal-binding; Monooxygenase;
KW   Nucleotide-binding; Oxidoreductase; Peroxisome; Photoprotein.
FT   CHAIN           1..548
FT                   /note="Luciferin 4-monooxygenase"
FT                   /id="PRO_0000193144"
FT   MOTIF           546..548
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   548 AA;  60125 MW;  AC62F9320BB6D4A6 CRC64;
     MENMENDENI VYGPEPFYPI EEGSAGAQLR KYMDRYAKLG AIAFTNALTG VDYTYAEYLE
     KSCCLGEALK NYGLVVDGRI ALCSENCEEF FIPVLAGLFI GVGVAPTNEI YTLRELVHSL
     GISKPTIVFS SKKGLDKVIT VQKTVTAIKT IVILDSKVDY RGYQSMDNFI KKNTPQGFKG
     SSFKTVEVNR KEQVALIMNS SGSTGLPKGV QLTHENAVTR FSHARDPIYG NQVSPGTAIL
     TVVPFHHGFG MFTTLGYLTC GFRIVMLTKF DEETFLKTLQ DYKCSSVILV PTLFAILNRS
     ELLDKYDLSN LVEIASGGAP LSKEIGEAVA RRFNLPGVRQ GYGLTETTSA IIITPEGDDK
     PGASGKVVPL FKAKVIDLDT KKTLGPNRRG EVCVKGPMLM KGYVDNPEAT REIIDEEGWL
     HTGDIGYYDE EKHFFIVDRL KSLIKYKGYQ VPPAELESVL LQHPNIFDAG VAGVPDPIAG
     ELPGAVVVLE KGKSMTEKEV MDYVASQVSN AKRLRGGVRF VDEVPKGLTG KIDGKAIREI
     LKKPVAKM