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Database: UniProt
Entry: A0A0L0BPT7_LUCCU
LinkDB: A0A0L0BPT7_LUCCU
Original site: A0A0L0BPT7_LUCCU 
ID   A0A0L0BPT7_LUCCU        Unreviewed;      1053 AA.
AC   A0A0L0BPT7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Luciferin 4-monooxygenase {ECO:0000256|ARBA:ARBA00019043};
DE            EC=1.13.12.7 {ECO:0000256|ARBA:ARBA00012532};
GN   ORFNames=FF38_14204 {ECO:0000313|EMBL:KNC22021.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC22021.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC22021.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC22021.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC22021.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
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:KNC22021.1}.
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DR   EMBL; JRES01001565; KNC22021.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0BPT7; -.
DR   STRING; 7375.A0A0L0BPT7; -.
DR   EnsemblMetazoa; KNC22021; KNC22021; FF38_14204.
DR   OMA; CDENVYE; -.
DR   Proteomes; UP000037069; 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:UP000037069}.
FT   DOMAIN          49..385
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          443..518
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   DOMAIN          561..905
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          957..1033
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   1053 AA;  118268 MW;  804EF56D24B664A6 CRC64;
     MYDYLCQYDK DQKLWTSAKR HEFYNENVSA GELAYFVMRN TNPSEVMQIS DSDGTVMTYG
     SALTTAIRIA QHFDTIGLTE DDIVSIFAPN TTYVMPVALA AWFNGTPFQP MNTVMETNVC
     TQIFEKIQPK IIFCDGLHYE KLKKAAAAFK PAIYTICNHV ENVPRIEELL EPTKSERNFK
     PKPLTKGPTQ TMIIMLSSGT TGLPKGICLS NRYVISDMAF TYQYDTIFST SSIDWLTGLV
     TLLTNVLVGG TRVITSKPYS AEYLHEIITK YKISVLVTNP SAMLELTSLP IYSKECMKSI
     RMLIMGGSSC PENTLKIIRS SLTNGKLYFG YGSTEMGAIA FNNRDYKLKS VGQILPNLQM
     KIVDSTTGER LGPNEKGEVC LRKTNDQWLG YYKNPEANKS TIDAEGFVHT GDLGYVDDEH
     YLYLVDRCRD VMKYWGYKWS PHEIEVLVAE MPEVKEVCAF GVYDNVKLYV PAAAVVVKPG
     CSLTSKDVVE FMERRSEVHY KHLDAGAFIV NELPRNRNDM ADFITIYHQE EKLWKGLDKP
     KLCNDNISAG AKALEVLRSK NPQDIMQISD SEKTTITYGS ALKAAIKIAE YFKSLSLNAD
     DVVGILAPDT TYVMPVALAS WFNGTPFQAI NCKWETAVVR NLYEFSRPKI IFCDGLQYEK
     VKAACENFKP LIYTLCNHLE NVPQIEDLLQ RASGAKPLKY GSKQTMVIMV SSGTSGMPKG
     VCVPNSTCIT DFGFTNDTTK MFSTSSIDWS SGLLTFMANV LVGGTRIITQ QPFTAEYLLQ
     LIVKYKINFL STNPSNLIQA SLLKEYTPET MQSVKLIFTA GSYCSELNLE RMRSALTKGL
     LFYGYGGTET GGVAGRLNSN KPKSVGRLLP NVQLKIVDVN NGEHLGPNEI GEICVRHDYE
     WCGYYNNAKA TANTLDSEGF IHTGDLGYMD EDNFLFLTGR CKDIMKYLGF QYSPNDIEEI
     IAEMEDVVDV CVFGVYDEVE QDVAAAAVVK REGSTLTKQQ VIKYVESKTE VQHKRIHYGI
     FFVKELPRNH NGKLLRDKIK KICLEMERCD KNE
//
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