ID   A0A212FN15_DANPL        Unreviewed;      1082 AA.
AC   A0A212FN15;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Luciferin 4-monooxygenase {ECO:0000256|ARBA:ARBA00019043};
DE            EC=1.13.12.7 {ECO:0000256|ARBA:ARBA00012532};
GN   ORFNames=KGM_206945 {ECO:0000313|EMBL:OWR55128.1};
OS   Danaus plexippus plexippus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX   NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR55128.1, ECO:0000313|Proteomes:UP000007151};
RN   [1] {ECO:0000313|EMBL:OWR55128.1, ECO:0000313|Proteomes:UP000007151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-2 {ECO:0000313|EMBL:OWR55128.1};
RX   PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA   Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT   "The monarch butterfly genome yields insights into long-distance
RT   migration.";
RL   Cell 147:1171-1185(2011).
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:0000256|ARBA:ARBA00001278};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWR55128.1}.
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DR   EMBL; AGBW02007648; OWR55128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212FN15; -.
DR   STRING; 278856.A0A212FN15; -.
DR   KEGG; dpl:KGM_206945; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   InParanoid; A0A212FN15; -.
DR   Proteomes; UP000007151; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
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_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR24096:SF353; GH16244P-RELATED; 1.
DR   PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Luminescence {ECO:0000256|ARBA:ARBA00023223};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Photoprotein {ECO:0000256|ARBA:ARBA00023262};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007151}.
FT   DOMAIN          41..404
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          455..531
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   DOMAIN          589..939
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          990..1066
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   1082 AA;  120984 MW;  5D7CC53EF256F595 CRC64;
     MQQSFDSCNY YFNEISNKVT AESGIWTDGE HLGKIIIRCL KEAPNFIAQI DGGTGEKETN
     KSVLERTVMC AQSFINFGLK YQDVVMVIAP NHLHISIPLY AAFCTGVIFA GIDFNLGENE
     LADTFKSGQP KMIFCQNSNL QTVRKALARI KSNAEIVTFD EGQDCISFTK FISKYSGDAT
     VENFRICDFE PVETIALLIA TSGSTGLPKV AVLTHQNVSV GFIQNWKGLS KAPNPFDIGL
     VISPIQWISS TFQIVMSPIL RYTRLQTSNK LSPEHVYDLI NKYKPKYTIC SPTYMTTLLR
     NDHQHVCDFT SFKYILIGGS AVSKELYADL KKVAPNVMIQ VGYGMSEASG LIFSPHYVPL
     GSIGRPMEHV NWKLVDPDTE EIIPEPYKAG EIRIKGRSIF KGYYNNPEMT AQAFDKDGWL
     KSGDIVYRDE NYNFFYVDRQ KLLLKYRNHQ VSPLEIENVI LKHPGVVDVA VSGIPDPEYG
     DLPIAFVVKK NDYDLTAQCV EDLVKETLTD SKQLRGGVIF LDELPVTSTS KLDRTKLKNM
     AVNMAKWVRS RNAVNMHLEE LSSRIVADSG IPTDRYHLGK LILQSLKDAP DYLSQIDGAS
     GETENFESVL RRSVRCATAL KNLGLKQGDV VVLMAPNHIH LCIPIYAALY IGAIVAGIDM
     NLKINELKDS FKINKPSVIF CQSEKAADIN LALSNLNIDP KIVTFDKGSD YLNFHQFVDK
     YGDDTPVEEF KATNLDPNEA IALLISTSGT TGLPKSAAAT HANFAISAAN MWVLFDTCPS
     PTRLSVIMSP LQWYSALFQY IYTPIVRTTR LQSSLPMTQE HAYYIINKYK PTFTMCSPNM
     WAELFKKGDR DKCDLSCFDL IMAAGSDVPS TLFDTINSVV PETCFIPAYG LSEISGIAFV
     YDSTNPRSLV SPETKLDVTE PNVPGELFIK GPAVFKGYYN DEKCTEETFT DDGWFKTGDI
     FKRDENWYFY FVERRKMLLI HKNYQVSPLE IENVIIQHPA VYQVAVTSVP HPEHGDLPVA
     CVVKHKDSTV TAQDIKDMVE ETLSEQKHLS GGVIFLDALP MTSTSKVNKS KLAALARVSE
     RL
//