ID   DIOX3_PAPSO             Reviewed;         360 AA.
AC   D4N502;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Codeine O-demethylase;
DE            EC=1.14.11.32 {ECO:0000269|PubMed:20228795};
GN   Name=CODM; Synonyms=DIOX3;
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], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
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 catalyzing the conversion of codeine to
CC       morphine. Catalyzes also, with lower efficiency, the 3-O-demethylation
CC       of thebaine to oripavine and of (S)-scoulerine to 3-O-
CC       demethylscoulerine. No activity with (S)-reticuline, salutaridine,
CC       papaverine, (S)-corytuberine, oripavine, pavine or noscapine.
CC       {ECO:0000269|PubMed:20228795}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + codeine + O2 = CO2 + formaldehyde + morphine
CC         + succinate; Xref=Rhea:RHEA:27413, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:57871, ChEBI:CHEBI:58097;
CC         EC=1.14.11.32; Evidence={ECO:0000269|PubMed:20228795};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000269|PubMed:20228795};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000269|PubMed:20228795};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- ACTIVITY REGULATION: Moderate substrate inhibition. Not inhibited in
CC       vitro by acylcyclohexanediones. {ECO:0000269|PubMed:20228795}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=20.5 uM for codeine {ECO:0000269|PubMed:20228795};
CC         KM=41.9 uM for thebaine {ECO:0000269|PubMed:20228795};
CC         KM=19.0 uM for 2-oxoglutarate {ECO:0000269|PubMed:20228795};
CC   -!- PATHWAY: Alkaloid biosynthesis; morphine biosynthesis. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; GQ500141; ADD85331.1; -; mRNA.
DR   AlphaFoldDB; D4N502; -.
DR   SMR; D4N502; -.
DR   EnsemblPlants; RZC46917; RZC46917; C5167_039857.
DR   EnsemblPlants; RZC46920; RZC46920; C5167_039865.
DR   Gramene; RZC46917; RZC46917; C5167_039857.
DR   Gramene; RZC46920; RZC46920; C5167_039865.
DR   KEGG; ag:ADD85331; -.
DR   OMA; FFMFTLP; -.
DR   SABIO-RK; D4N502; -.
DR   UniPathway; UPA00852; -.
DR   GO; GO:0102805; F:codeine O-demethylase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0102803; F:thebane O-demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0097295; P:morphine biosynthetic process; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Alkaloid metabolism; Dioxygenase; Iron; Metal-binding; Methyltransferase;
KW   Oxidoreductase; Transferase.
FT   CHAIN           1..360
FT                   /note="Codeine O-demethylase"
FT                   /id="PRO_0000401479"
FT   DOMAIN          211..311
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         220
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:D4N500"
FT   BINDING         235
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         237
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         292
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         302
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         304
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:D4N500"
SQ   SEQUENCE   360 AA;  40849 MW;  86CB76391D1F8EE5 CRC64;
     METPILIKLG NGLSIPSVQE LAKLTLAEIP SRYTCTGESP LNNIGASVTD DETVPVIDLQ
     NLLSPEPVVG KLELDKLHSA CKEWGFFQLV NHGVDALLMD NIKSEIKGFF NLPMNEKTKY
     GQQDGDFEGF GQPYIESEDQ RLDWTEVFSM LSLPLHLRKP HLFPELPLPF RETLESYLSK
     MKKLSTVVFE MLEKSLQLVE IKGMTDLFED GLQTMRMNYY PPCPRPELVL GLTSHSDFSG
     LTILLQLNEV EGLQIRKEER WISIKPLPDA FIVNVGDILE IMTNGIYRSV EHRAVVNSTK
     ERLSIATFHD SKLESEIGPI SSLVTPETPA LFKRGRYEDI LKENLSRKLD GKSFLDYMRM