EO_BOMMO
ID EO_BOMMO Reviewed; 668 AA.
AC H6AGY0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Ecdysone oxidase {ECO:0000303|PubMed:22215981};
DE Short=BmEO {ECO:0000303|PubMed:22215981};
DE EC=1.1.3.16 {ECO:0000269|PubMed:22215981, ECO:0000305|PubMed:26041352, ECO:0000305|PubMed:30262999};
GN Name=EO {ECO:0000303|PubMed:22215981};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000312|EMBL:AEM17059.1};
RN [1] {ECO:0000312|EMBL:AEM17059.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=22215981; DOI=10.7150/ijbs.8.125;
RA Sun W., Shen Y.H., Qi D.W., Xiang Z.H., Zhang Z.;
RT "Molecular cloning and characterization of Ecdysone oxidase and 3-
RT dehydroecdysone-3alpha-reductase involved in the ecdysone inactivation
RT pathway of silkworm, Bombyx mori.";
RL Int. J. Biol. Sci. 8:125-138(2012).
RN [2] {ECO:0000312|EMBL:AIO02855.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D872 {ECO:0000312|EMBL:AIO02870.1},
RC Dongting {ECO:0000312|EMBL:AIO02861.1},
RC Furonghuiluan {ECO:0000312|EMBL:AIO02865.1},
RC Luoni6 {ECO:0000312|EMBL:AIO02867.1}, Ping {ECO:0000312|EMBL:AIO02868.1},
RC Sulian1 {ECO:0000312|EMBL:AIO02864.1}, and
RC WuG {ECO:0000312|EMBL:AIO02855.1};
RX PubMed=25213334; DOI=10.1093/molbev/msu261;
RA Sun W., Shen Y.H., Han M.J., Cao Y.F., Zhang Z.;
RT "An adaptive transposable element insertion in the regulatory region of the
RT EO gene in the domesticated silkworm, Bombyx mori.";
RL Mol. Biol. Evol. 31:3302-3313(2014).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26041352; DOI=10.1098/rspb.2015.0513;
RA Li Z., You L., Zeng B., Ling L., Xu J., Chen X., Zhang Z., Palli S.R.,
RA Huang Y., Tan A.;
RT "Ectopic expression of ecdysone oxidase impairs tissue degeneration in
RT Bombyx mori.";
RL Proc. R. Soc. B 282:20150513-20150513(2015).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30262999; DOI=10.7150/ijbs.26227;
RA Wang C.F., Zhang Z., Sun W.;
RT "Ecdysone oxidase and 3-dehydroecdysone-3beta-reductase contribute to the
RT synthesis of ecdysone during early embryonic development of the silkworm.";
RL Int. J. Biol. Sci. 14:1472-1482(2018).
CC -!- FUNCTION: Involved in the inactivation of ecdysteroid molting hormones
CC by converting ecdysteroids into 3-dehydroecdysteroids.
CC {ECO:0000269|PubMed:22215981, ECO:0000269|PubMed:26041352,
CC ECO:0000269|PubMed:30262999}.
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:22215981, ECO:0000305|PubMed:26041352,
CC ECO:0000305|PubMed:30262999};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11797;
CC Evidence={ECO:0000305|PubMed:22215981};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PIRSR:PIRSR000137-2};
CC -!- DEVELOPMENTAL STAGE: Expressed in the midgut goblet cell cavities at
CC the 5th instar larval stage (at protein level) (PubMed:26041352). At
CC the pupal stage, expressed in the midgut and to a lesser extent in the
CC fat body, hemocyte, head and testis (PubMed:26041352, PubMed:30262999).
CC At the pupal stage, highly expressed in ovary (PubMed:30262999).
CC Expressed at the late 4th instar larval stage, and disappears during
CC the 4th molting stage (PubMed:22215981). Highly expressed at the early
CC 5th instar larval stage, then expression remains low during the feeding
CC stage, and increases at the wandering stage (PubMed:22215981). During
CC pupal development, expression begins at prepupal stage 1 (PP1),
CC increases until P4 pupal stage, then decreases after P6 pupal stage
CC (PubMed:26041352). During egg maturation, expressed at low level during
CC the vitellogenic stages and increases at the onset of choriogenesis
CC (PubMed:30262999). {ECO:0000269|PubMed:22215981,
CC ECO:0000269|PubMed:26041352, ECO:0000269|PubMed:30262999}.
CC -!- DISRUPTION PHENOTYPE: Causes large body size and prolongs the final
CC instar larval stage (PubMed:26041352). In the midgut of instar larval
CC stage (L5D4), causes an increase of ecdysteroid levels, up-regulation
CC of IRS and PI3K mRNA levels and down-regulation of TSC1 and TSC2 mRNA
CC levels (PubMed:26041352). RNAi-mediated knockdown at the pupal stage,
CC does not affect growth or ovary development (PubMed:30262999). However,
CC the ovary has decreased levels of 3-dehydroecdysone without affecting
CC ecdysone levels (PubMed:30262999). Also, hatching rate is reduced and,
CC laid eggs have lower levels of 20-hydroxyecdysone and are arrested at
CC the organogenesis stage (PubMed:30262999).
CC {ECO:0000269|PubMed:26041352, ECO:0000269|PubMed:30262999}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000255|RuleBase:RU003968}.
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DR EMBL; JF433972; AEM17059.1; -; mRNA.
DR EMBL; KF717653; AIO02855.1; -; Genomic_DNA.
DR EMBL; KF717659; AIO02861.1; -; Genomic_DNA.
DR EMBL; KF717662; AIO02864.1; -; Genomic_DNA.
DR EMBL; KF717663; AIO02865.1; -; Genomic_DNA.
DR EMBL; KF717665; AIO02867.1; -; Genomic_DNA.
DR EMBL; KF717666; AIO02868.1; -; Genomic_DNA.
DR EMBL; KF717668; AIO02870.1; -; Genomic_DNA.
DR RefSeq; NP_001243996.1; NM_001257067.1.
DR RefSeq; XP_012545508.1; XM_012690054.1.
DR GeneID; 100862708; -.
DR KEGG; bmor:100862708; -.
DR HOGENOM; CLU_970522_0_0_1; -.
DR OrthoDB; 798314at2759; -.
DR BioCyc; MetaCyc:MON-16688; -.
DR BRENDA; 1.1.3.16; 890.
DR Proteomes; UP000005204; Unplaced.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; 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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..668
FT /note="Ecdysone oxidase"
FT /id="PRO_0000454217"
FT ACT_SITE 537
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 270
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|PIRSR:PIRSR000137-2"
FT BINDING 536..537
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|PIRSR:PIRSR000137-2"
SQ SEQUENCE 668 AA; 72596 MW; 0A7DCACC5EF326C8 CRC64;
MVCGLTSCLG SGAAGGLFSS AVQFFAATQC LVGETWPKDS VLQNGSRYDF IIVGAGTAGS
ALAARLSEVA NFSVLLLEAG GDPPIEAIIP AFRETLKASS VDWNFTSVEN NITSQALKRG
IEQQPRGKML GGSGSLNHMV YARGFPSDYH EWASIAGETW NWTNVLKYFM KTEHMTDTNI
VNNPELMVYH GRGGAIEVSG TNEVMFSIKK FLQAFEELGF KTVPDMTYPN SIGAGCFSHT
IRNGERDSSL RALLNNANST SLHILKDTFV TKIIIENGTA IGIEAVKDDK TFLFYADREV
ILSAGTFNTP KLLMLSGVGR SEHLRSLGID VVADLPVGSN LHDHAMVLAF LVADNGTCVS
DEAENSMEAI KYLYDRTGFL AKADNMAAYL PLSSSEPTVP EFALYPTCIP QFSPFRSGCL
TLGLNEDLCT ELHNLNQEYE LVTIAAVLLK PKSRGKVELN SINPFDDPLI YAGTFSEEQD
LDHFPRLIKM AWSIADTNYF RSKNARVIKP WVEACSNLTE SAWIKCMSRA MVTSAWHSVG
TAAMGTVVDG DLKVLGINGL RVVDASVMPK IIRGNTNAPV VMIAEIAADL IKEHYSVSRT
GTNLNNMTIG NLTASSMPNI SQPNINLADV IENNDMINSS LIEVEITNVE IITTTDRQSD
IDDTVNVA
