ID   EO_SPOLI                Reviewed;         599 AA.
AC   Q95NZ0;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Ecdysone oxidase {ECO:0000303|PubMed:11373299};
DE            EC=1.1.3.16 {ECO:0000269|PubMed:11373299};
OS   Spodoptera littoralis (Egyptian cotton leafworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Amphipyrinae; Spodoptera.
OX   NCBI_TaxID=7109 {ECO:0000312|EMBL:AAK56552.1};
RN   [1] {ECO:0000312|EMBL:AAK56552.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 2-19 AND
RP   98-108, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11373299; DOI=10.1074/jbc.m104291200;
RA   Takeuchi H., Chen J.H., O'Reilly D.R., Turner P.C., Rees H.H.;
RT   "Regulation of ecdysteroid signaling: cloning and characterization of
RT   ecdysone oxidase: a novel steroid oxidase from the cotton leafworm,
RT   Spodoptera littoralis.";
RL   J. Biol. Chem. 276:26819-26828(2001).
CC   -!- FUNCTION: Involved in the inactivation of ecdysteroid molting hormones
CC       by converting ecdysteroids into 3-dehydroecdysteroids.
CC       {ECO:0000269|PubMed:11373299}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ecdysone + O2 = 3-dehydroecdysone + H2O2;
CC         Xref=Rhea:RHEA:11796, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:16688, ChEBI:CHEBI:17058; EC=1.1.3.16;
CC         Evidence={ECO:0000269|PubMed:11373299};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11797;
CC         Evidence={ECO:0000305|PubMed:11373299};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|PIRSR:PIRSR000137-2};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.1 uM for ecdysone (at pH 6.6 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:11373299};
CC         Vmax=0.036 nmol/min/ug enzyme (at pH 6.6 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:11373299};
CC   -!- DEVELOPMENTAL STAGE: Expressed in the midgut at the prepupal stage of
CC       the last larval instar. {ECO:0000269|PubMed:11373299}.
CC   -!- INDUCTION: Induced by RH-5992, which is an ecdysone agonist used as
CC       insecticide. {ECO:0000269|PubMed:11373299}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AY035784; AAK56551.1; -; mRNA.
DR   EMBL; AY035785; AAK56552.1; -; Genomic_DNA.
DR   BioCyc; MetaCyc:MON-18162; -.
DR   BRENDA; 1.1.3.16; 5837.
DR   GO; GO:0047875; F:ecdysone oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; PTHR11552; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..599
FT                   /note="Ecdysone oxidase"
FT                   /id="PRO_0000454216"
FT   ACT_SITE        538
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   BINDING         137..140
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR000137-2"
FT   BINDING         537..538
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   599 AA;  65207 MW;  142391744B6034C1 CRC64;
     MCYAVGGCAG AGPAATYVAA ALQFFAASQC LLQESYPRQA HVTNGSRYDF IVVGGGTAGS
     ALAARLAEEN RFSVLLLEAG PNPPEESIVP GLRQTLKETP YDWNFTTIDD GVTSQALASH
     VQRQPRGKML GGSGSLNDMV YARGHPEDYY EWADIAGDVW NWTNVLDYFK RTEHMTDSNI
     IRNKELMQYH GIGGAIEVSG AHYPDSPNSK LMQAFQELGF AAVDDMTYPY KIGVGKFSHT
     IRGGRRDSSL TAMLNKVKSG KLHVLKNTFA TKILFEGNKA VGIQADSDGR NLFVYAKHEV
     IVSAGTFNTP KLLLLSGVGP SDILNQFDID VVQDLPVGQG LQDHVMVLNF MTAERGTCKL
     SESDGYFNVI KYLYNGSGTL SYSDSIGAYL PQKDKEAHVP YFAIYPSCVP AGQLTSNLCV
     QGIGFTSEIC EKLQKENEMH ELIVAAVVLL KPQSRGHVTL KSLNPDDDPA IYSGTFDHEA
     DMEGFPEAIE KAISLVNTTH FKKLGARVVD LTPESCRGLQ EPQRTRCSVR ALALAAWHAV
     GTARLGAVLD AELRVRGLEG LRVADASVMP TMVRGNTNAP VVMIAEMAAD FIKNQYRDK