ID A0A0J7KI18_LASNI Unreviewed; 425 AA.
AC A0A0J7KI18;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Luciferin 4-monooxygenase {ECO:0000256|ARBA:ARBA00019043};
DE EC=1.13.12.7 {ECO:0000256|ARBA:ARBA00012532};
GN ORFNames=RF55_10451 {ECO:0000313|EMBL:KMQ89861.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ89861.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ89861.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ89861.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KMQ89861.1}.
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DR EMBL; LBMM01007304; KMQ89861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7KI18; -.
DR STRING; 67767.A0A0J7KI18; -.
DR PaxDb; 67767-A0A0J7KI18; -.
DR OrthoDB; 2596785at2759; -.
DR Proteomes; UP000036403; 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; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_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; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Luminescence {ECO:0000256|ARBA:ARBA00023223};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:KMQ89861.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000313|EMBL:KMQ89861.1}; Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Photoprotein {ECO:0000256|ARBA:ARBA00023262};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403}.
FT DOMAIN 7..282
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 333..409
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 425 AA; 47040 MW; 9E255C7966914441 CRC64;
MDLQTALHVM QLTTPKIIFC SEKPVNIILS AMKESNCNPT VVVFDDHPDA IAFSDILSMY
SDAEVANFRY VELDDIMQTA CIVHSSGTTG MPKGVEISNY CLLLISEDTN MDLTNAVLTW
FSSLYWISGI LMNLKSIAQG AKVILYPEFD EEMTCLLIEK YKVTVIFLST SMINRFLKAG
YIRKYSLLSL KNIICGGAIL KPKTQKEMKC ILPHVEMLQG YGMTELGGLA ALQLPHHKAG
SCGTVVENVQ MKVVDPENGN VLGPNNPGEL WITTAIIMNG YYRNPEATKS TVDEEGWLHS
GDVGYFDEDG ELFIIDRIKE LIKYRGYQIS PGEVEGVLMS HPAVMEAAVI GVPHAVDDEH
PVAYVTKMPG AKVTEQELID LVANSMMDQY KLRAGVIFLD AFPYTGSGKI ARKELKTMAK
ILAIE
//