ID   DIOX2_PAPSO             Reviewed;         364 AA.
AC   D4N501;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Probable 2-oxoglutarate/Fe(II)-dependent dioxygenase;
DE            EC=1.14.11.-;
GN   Name=DIOX2;
OS   Papaver somniferum (Opium poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=3469;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=20228795; DOI=10.1038/nchembio.317;
RA   Hagel J.M., Facchini P.J.;
RT   "Dioxygenases catalyze the O-demethylation steps of morphine biosynthesis
RT   in opium poppy.";
RL   Nat. Chem. Biol. 6:273-275(2010).
CC   -!- FUNCTION: Non-heme dioxygenase active on an unknown substrate. No
CC       activity with (S)-reticuline, salutaridine, papaverine, (S)-
CC       corytuberine, oripavine, (S)-scoulerine, pavine, noscapine, codeine or
CC       thebaine. {ECO:0000269|PubMed:20228795}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- MISCELLANEOUS: No detectable effect on alkaloid content in RNAi
CC       specific mutant.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GQ500140; ADD85330.1; -; mRNA.
DR   AlphaFoldDB; D4N501; -.
DR   SMR; D4N501; -.
DR   PRIDE; D4N501; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.330; -; 1.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Transferase.
FT   CHAIN           1..364
FT                   /note="Probable 2-oxoglutarate/Fe(II)-dependent
FT                   dioxygenase"
FT                   /id="PRO_0000401478"
FT   DOMAIN          214..314
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         238
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         240
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         295
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         305
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   364 AA;  40845 MW;  6948A208427076ED CRC64;
     METAKLMKLG NGMSIPSVQE LAKLTLAEIP SRYICTVENL QLPVGASVID DHETVPVIDI
     ENLISSEPVT EKLELDRLHS ACKEWGFFQV VNHGVDTSLV DNVKSDIQGF FNLSMNEKIK
     YGQKDGDVEG FGQAFVASED QTLDWADIFM ILTLPLHLRK PHLFSKLPLP LRETIESYSS
     EMKKLSMVLF EKMEKALQVQ AVEIKEISEV FKDMTQVMRM NYYPPCPQPE LAIGLTPHSD
     FGGLTILLQL NEVEGLQIKN EGRWISVKPL PNAFVVNVGD VLEIMTNGMY RSVDHRAVVN
     STKERLSIAT FHDPNLESEI GPISSLITPN TPALFRSGST YGELVEEFHS RKLDGKSFLD
     SMRM