EO_DROME
ID EO_DROME Reviewed; 657 AA.
AC Q9VY01;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ecdysone oxidase {ECO:0000303|PubMed:15813704};
DE EC=1.1.3.16 {ECO:0000269|PubMed:15813704};
GN Name=Eo {ECO:0000303|PubMed:15813704, ECO:0000312|FlyBase:FBgn0030597};
GN Synonyms=EObeta1 {ECO:0000312|FlyBase:FBgn0030597};
GN ORFNames=CG9504 {ECO:0000312|FlyBase:FBgn0030597};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:ACY46089.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=15813704; DOI=10.1042/bj20050498;
RA Takeuchi H., Rigden D.J., Ebrahimi B., Turner P.C., Rees H.H.;
RT "Regulation of ecdysteroid signalling during Drosophila development:
RT identification, characterization and modelling of ecdysone oxidase, an
RT enzyme involved in control of ligand concentration.";
RL Biochem. J. 389:637-645(2005).
CC -!- FUNCTION: Involved in the inactivation of ecdysteroid molting hormones
CC by converting ecdysteroids into 3-dehydroecdysteroids.
CC {ECO:0000269|PubMed:15813704}.
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:15813704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11797;
CC Evidence={ECO:0000305|PubMed:15813704};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PIRSR:PIRSR000137-2};
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the late stage of the last
CC instar larval stage and the pre-pupal stage (PubMed:15813704). Detected
CC at 4h into the last larval instar; however, expression levels are low
CC during the feeding stage (PubMed:15813704). Levels increase from 16 h,
CC reach a peak at 48h, quickly decrease just before puparium formation,
CC and rise again after pupariation (PubMed:15813704). Highly expressed in
CC midgut in the third instar larvae (PubMed:15813704).
CC {ECO:0000269|PubMed:15813704}.
CC -!- INDUCTION: Induced by RH-0345, which is an ecdysone agonist used as
CC insecticide. {ECO:0000269|PubMed:15813704}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48405.2; -; Genomic_DNA.
DR EMBL; BT100214; ACY46089.1; -; mRNA.
DR RefSeq; NP_572986.1; NM_132758.2.
DR AlphaFoldDB; Q9VY01; -.
DR SMR; Q9VY01; -.
DR STRING; 7227.FBpp0073792; -.
DR PaxDb; Q9VY01; -.
DR EnsemblMetazoa; FBtr0073975; FBpp0073792; FBgn0030597.
DR GeneID; 32423; -.
DR KEGG; dme:Dmel_CG9504; -.
DR UCSC; CG9504-RA; d. melanogaster.
DR CTD; 103971; -.
DR FlyBase; FBgn0030597; Eo.
DR VEuPathDB; VectorBase:FBgn0030597; -.
DR eggNOG; KOG1238; Eukaryota.
DR GeneTree; ENSGT00940000168245; -.
DR HOGENOM; CLU_002865_7_1_1; -.
DR InParanoid; Q9VY01; -.
DR OMA; LHDHGML; -.
DR OrthoDB; 798314at2759; -.
DR PhylomeDB; Q9VY01; -.
DR BioCyc; MetaCyc:MON-18163; -.
DR BioGRID-ORCS; 32423; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32423; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030597; Expressed in Malpighian tubule and 6 other tissues.
DR ExpressionAtlas; Q9VY01; baseline and differential.
DR GO; GO:0047875; F:ecdysone oxidase activity; IDA:FlyBase.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008205; P:ecdysone metabolic process; IDA:FlyBase.
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.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..657
FT /note="Ecdysone oxidase"
FT /id="PRO_0000454215"
FT ACT_SITE 578
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 299
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|PIRSR:PIRSR000137-2"
FT BINDING 577..578
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|PIRSR:PIRSR000137-2"
SQ SEQUENCE 657 AA; 72560 MW; 4D4D0C00BDC49068 CRC64;
MGDQRVHKPR TAKTRTLRVN RILLPMLLLF SGETTSVVTQ LFSVDSSGLG ISLMQSVAIA
LNASSLALAN NTAWPLQHEP PEDRLEIESY DYIVVGAGSA GSIVASRLSE LCQVKVLLLE
EGQLPPLESE IFGLTGALHH DERYMFLEEA VPNPKCCQAM ASMHGCVWWH GRMMGGGGAI
NGNIFIPGSR ENFRRWNSTG WDWTQVHKTY SRLQQRLNPS YLQPNKLNLK LANLIYSGSA
ELGVPRMKQP LIAGATFGYT HHVPVTVNQR RRASSARLYL ANDQVNRRGN LKVIRGAQVQ
RVLLNAAGSR ATGVIYTLNG VEHTAKTLGE VILSAGTLNS AKLLLLSGIG PREELQRWNI
TTHQDLPVGR NLQDHGMMPL FLLFGSNCAV NSTRDPTENP YAPVSITQYL LDNQKGPLAS
GFYMMGYINS SSPSSSRGEP DLHVVAHTLL PKGSTGSFGY LGFRPELIQA QQDILQKGDL
LQIMGSLLRP LSHGKVSLSS KNSADQAKIE NHYGEAVEDQ QTLLRYVRYI QKLSKTRPFR
RCGLRLWKPP LHECDTLAAD SDDYWLCYIR YFYVGAWHSV GTCRMAPRKG VDSQENGGVV
DERLRVHGVK GLRVVDASIM PELPAGNTNG PAMMIGEKGA QMILDDREAN NEVIQEC
