ID   LUCI_LUCMI              Reviewed;         548 AA.
AC   Q26304;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Luciferin 4-monooxygenase;
DE            Short=Luciferase;
DE            EC=1.13.12.7 {ECO:0000269|PubMed:2801227};
OS   Luciola mingrelica (Southern Russian firefly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia; Elateroidea;
OC   Lampyridae; Luciolinae; Luciola.
OX   NCBI_TaxID=27446;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8504162; DOI=10.1016/0167-4781(93)90172-a;
RA   Devine J.H., Kutuzova G.D., Green V.A., Ugarova N.N., Baldwin T.O.;
RT   "Luciferase from the east European firefly Luciola mingrelica: cloning and
RT   nucleotide sequence of the cDNA, overexpression in Escherichia coli and
RT   purification of the enzyme.";
RL   Biochim. Biophys. Acta 1173:121-132(1993).
RN   [2]
RP   SUBUNIT.
RA   Ugarova N.N., Brovko L. Jr., Belyayeva E.I., Philippova N. Jr.,
RA   Berezin I.V.;
RT   "Dimers as catalytically active particles of firefly luciferase.";
RL   Dokl. Akad. Nauk SSSR 260:358-360(1981).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=2801227; DOI=10.1002/bio.1170040155;
RA   Ugarova N.N.;
RT   "Luciferase of Luciola mingrelica fireflies. Kinetics and regulation
RT   mechanism.";
RL   J. Biolumin. Chemilumin. 4:406-418(1989).
CC   -!- FUNCTION: Produces green light with a wavelength of 570 nm.
CC       {ECO:0000269|PubMed:2801227}.
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:0000269|PubMed:2801227};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Inhibited by ATP analogs and sodium deoxycholate.
CC       Activated by choline-containing phospholipids.
CC       {ECO:0000269|PubMed:2801227}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=11.5 uM for luciferin {ECO:0000269|PubMed:2801227};
CC         KM=130 uM for ATP {ECO:0000269|PubMed:2801227};
CC       pH dependence:
CC         Optimum pH is 7.7. {ECO:0000269|PubMed:2801227};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000255}.
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DR   EMBL; S61961; AAB26932.1; -; mRNA.
DR   PIR; S33788; S33788.
DR   AlphaFoldDB; Q26304; -.
DR   SMR; Q26304; -.
DR   KEGG; ag:AAB26932; -.
DR   BioCyc; MetaCyc:MON-16916; -.
DR   BRENDA; 1.13.12.7; 3082.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0047077; F:Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity; IDA:UniProtKB.
DR   GO; GO:0008218; P:bioluminescence; IDA:UniProtKB.
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   1: Evidence at protein 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_0000193145"
FT   MOTIF           546..548
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   548 AA;  60495 MW;  62C8953BDFFBC423 CRC64;
     MEMEKEENVV YGPLPFYPIE EGSAGIQLHK YMHQYAKLGA IAFSNALTGV DISYQEYFDI
     TCRLAEAMKN FGMKPEEHIA LCSENCEEFF IPVLAGLYIG VAVAPTNEIY TLRELNHSLG
     IAQPTIVFSS RKGLPKVLEV QKTVTCIKKI VILDSKVNFG GHDCMETFIK KHVELGFQPS
     SFVPIDVKNR KQHVALLMNS SGSTGLPKGV RITHEGAVTR FSHAKDPIYG NQVSPGTAIL
     TVVPFHHGFG MFTTLGYFAC GYRVVMLTKF DEELFLRTLQ DYKCTSVILV PTLFAILNKS
     ELIDKFDLSN LTEIASGGAP LAKEVGEAVA RRFNLPGVRQ GYGLTETTSA FIITPEGDDK
     PGASGKVVPL FKVKVIDLDT KKTLGVNRRG EICVKGPSLM LGYSNNPEAT RETIDEEGWL
     HTGDIGYYDE DEHFFIVDRL KSLIKYKGYQ VPPAELESVL LQHPNIFDAG VAGVPDPDAG
     ELPGAVVVME KGKTMTEKEI VDYVNSQVVN HKRLRGGVRF VDEVPKGLTG KIDAKVIREI
     LKKPQAKM