ID A0A182NT79_9DIPT Unreviewed; 973 AA.
AC A0A182NT79;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Luciferin 4-monooxygenase {ECO:0000256|ARBA:ARBA00019043};
DE EC=1.13.12.7 {ECO:0000256|ARBA:ARBA00012532};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR010869-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR010869-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR010869-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A182NT79; -.
DR STRING; 7168.A0A182NT79; -.
DR EnsemblMetazoa; ADIR010869-RA; ADIR010869-PA; ADIR010869.
DR VEuPathDB; VectorBase:ADIR010869; -.
DR OrthoDB; 1404660at2759; -.
DR Proteomes; UP000075884; 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}.
FT DOMAIN 1..279
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 331..408
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT DOMAIN 470..823
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 874..952
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 973 AA; 106788 MW; C84793153A52E31C CRC64;
MLQTTKPKLV FCDDNNYEVV RSALERVVAN GDQMPPLYVL ESDRKDVKHA EDLLKETGQE
ERFLAPYLGD SRKTLAAILC SSGSSGVHKG VRITHAACAH KTRTFCFSSV PAVDFNFSSL
YWTTGFTLLL STFFTGHIRL FTRNAFNEND LFTAIEEHRA SVIFTPPSSA SAMLAHPRTK
TADFSSVVYW ITGGSSVPER LRDRMDALLA PTGGRFVNAI GPTETGMIAI DLVKRKPNAI
GPLMPNIMVR IVDEDGNRMG VGEPGELLVK AVEAFGGYYE NEEATANALD ADGFFRTGDV
AYIDEEGYLY VVDRQKDIFK YRNYQISPTD LEAIISRIEG VRDVCVVGIP DEESATDVPA
AAIVRLPNAS GLEASQVRTV VDGQVSDFKR LRGGVYFVEE LPKTHSGKIL RRKSVGKCRV
SECRTRENSS SMSLCTYDEQ SRTWHGPAVV SVYNPQANVG HILNRILLGT PERIIQIDMD
TDYRMSCAEF RLRMVRFARG LTKAGLKTGD IVALASGNSE NVAPLVCALM TIGAPFNPLA
PGLNENDMAH MMRVTQPKMV FCDECNVDVV RKAIVKATGG ELPLYVVESS RGDVLHAEDL
LQETGGEEHF VPARLGDSHE LLSMILCSSG TTGPPKGVCV THAQIIAMLG AYPMGQPGTI
FNFSPLYWAT GMHTLLCSFT GASARLITRR PFSEETFFEA VEKHRINVTF MPPSYASQLV
RHARVQQVDF GSLHMLALGG SYVSDGLRDQ LDRLLPNGRT YNSLGSSELG WISTDFGRRK
PGSVGTPAVN ISAQIVAEDG TRLGVGERGQ VLLKGPEPFV GYYRNEAATA DTIDEHGFIR
TGDVGYFDEE GYLYLIDRQK DIFKYRGFHV SPSELEAILA GIEGVLEVCV VGVPADADRT
TELPTAAIVR APGSTLTAPD VNRIFDGQVS DFSRLRGGVY FVEQLPKTPS GKILRRTVLD
EMVRLRETEV TKV
//