ID   LUCI_PHOPE              Reviewed;         545 AA.
AC   Q27757; O02653;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Luciferin 4-monooxygenase;
DE            Short=Luciferase;
DE            EC=1.13.12.7 {ECO:0000250|UniProtKB:Q26304};
OS   Photuris pensylvanica (Pennsylania firefly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia; Elateroidea;
OC   Lampyridae; Photurinae; Photuris.
OX   NCBI_TaxID=1710587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lantern;
RX   PubMed=9165098; DOI=10.1016/s0167-4838(96)00211-7;
RA   Ye L., Buck L.M., Schaeffer H.J., Leach F.R.;
RT   "Cloning and sequencing of a cDNA for firefly luciferase from Photuris
RT   pennsylvanica.";
RL   Biochim. Biophys. Acta 1339:39-52(1997).
CC   -!- FUNCTION: Produces green light with a wavelength of 562 nm.
CC       {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; Evidence={ECO:0000250};
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; U31240; AAB60897.1; -; mRNA.
DR   AlphaFoldDB; Q27757; -.
DR   SMR; Q27757; -.
DR   BindingDB; Q27757; -.
DR   ChEMBL; CHEMBL5150; -.
DR   BRENDA; 1.13.12.7; 10849.
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..545
FT                   /note="Luciferin 4-monooxygenase"
FT                   /id="PRO_0000193146"
FT   MOTIF           543..545
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   545 AA;  60649 MW;  F0FE4E828047C26E CRC64;
     MEDKNILYGP EPFHPLADGT AGEQMFYALS RYADISGCIA LTNAHTKENV LYEEFLKLSC
     RLAESFKKYG LKQNDTIAVC SENGLQFFLP LIASLYLGII AAPVSDKYIE RELIHSLGIV
     KPRIIFCSKN TFQKVLNVKS KLKYVETIII LDLNEDLGGY QCLNNFISQN SDINLDVKKF
     KPNSFNRDDQ VALVMFSSGT TGVSKGVMLT HKNIVARFSH CKDPTFGNAI NPTTAILTVI
     PFHHGFGMTT TLGYFTCGFR VALMHTFEEK LFLQSLQDYK VESTLLVPTL MAFFPKSALV
     EKYDLSHLKE IASGGAPLSK EIGEMVKKRF KLNFVRQGYG LTETTSAVLI TPDTDVRPGS
     TGKIVPFHAV KVVDPTTGKI LGPNETGELY FKGDMIMKSY YNNEEATKAI INKDGWLRSG
     DIAYYDNDGH FYIVDRLKSL IKYKGYQVAP AEIEGILLQH PYIVDAGVTG IPDEAAGELP
     AAGVVVQTGK YLNEQIVQNF VSSQVSTAKW LRGGVKFLDE IPKGSTGKID RKVLRQMFEK
     HKSKL