ID   COR15_PAPSO             Reviewed;         321 AA.
AC   B9VRJ2;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=NADPH-dependent codeinone reductase 1-5;
DE            EC=1.1.1.247;
GN   Name=COR1.5;
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 [GENOMIC DNA].
RX   PubMed=20487152; DOI=10.1111/j.1556-4029.2010.01423.x;
RA   Lee E.J., Hwang I.K., Kim N.Y., Lee K.L., Han M.S., Lee Y.H., Kim M.Y.,
RA   Yang M.S.;
RT   "An assessment of the utility of universal and specific genetic markers for
RT   Opium poppy identification.";
RL   J. Forensic Sci. 55:1202-1208(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Liang Q.Q., Wei Y.J., Zhang J.W., Chen Z.G., Jia X.X., He Q.X.;
RT   "Cloning of COR Gene of Opium Poppy and Construction of its RNAi Expression
RT   Vector.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11079569;
RX   DOI=10.1002/1522-2683(20001001)21:16<3500::aid-elps3500>3.0.co;2-o;
RA   Decker G., Wanner G., Zenk M.H., Lottspeich F.;
RT   "Characterization of proteins in latex of the opium poppy (Papaver
RT   somniferum) using two-dimensional gel electrophoresis and
RT   microsequencing.";
RL   Electrophoresis 21:3500-3516(2000).
CC   -!- FUNCTION: Reduces codeinone to codeine in the penultimate step in
CC       morphine biosynthesis. Can use morphinone, hydrocodone and
CC       hydromorphone as substrate during reductive reaction with NADPH as
CC       cofactor, and morphine and dihydrocodeine as substrate during oxidative
CC       reaction with NADP as cofactor (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=codeine + NADP(+) = codeinone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:19209, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:57871, ChEBI:CHEBI:58349, ChEBI:CHEBI:58473;
CC         EC=1.1.1.247;
CC   -!- PATHWAY: Alkaloid biosynthesis; morphine biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11079569}.
CC       Note=Present in the cytosolic part of laticifer cells that secrete
CC       latex.
CC   -!- TISSUE SPECIFICITY: Latex secreting cells (laticifer cells).
CC       {ECO:0000269|PubMed:11079569}.
CC   -!- MISCELLANEOUS: Useful marker for the forensic DNA analysis of opium
CC       poppy. {ECO:0000305|PubMed:20487152}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase 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; FJ596160; ACM44062.1; -; Genomic_DNA.
DR   EMBL; FJ624147; ACN53513.1; -; mRNA.
DR   AlphaFoldDB; B9VRJ2; -.
DR   SMR; B9VRJ2; -.
DR   UniPathway; UPA00852; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0047036; F:codeinone reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd19124; AKR_AKR4A_4B; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044497; AKR4A/B.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   1: Evidence at protein level;
KW   Alkaloid metabolism; Cytoplasm; NADP; Oxidoreductase.
FT   CHAIN           1..321
FT                   /note="NADPH-dependent codeinone reductase 1-5"
FT                   /id="PRO_0000418595"
FT   ACT_SITE        56
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         214..273
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            86
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  35794 MW;  0E8252B0222BADB3 CRC64;
     MESNGVPMIT LSSGIRMPAL GMGTVETMEK GTEREKLAFL KAIEVGYRHF DTAAAYQTEE
     CLGEAIAEAL QLGLIKSRDE LFITSKLWCA DAHADLVLPA LQNSLRNLKL DYLDLYLIHH
     PVSLKPGKFV NEIPKDHILP MDYKSVWAAM EECQTLGFTR AIGVCNFSCK KLQELMATAN
     SPPVVNQVEM SPTLHQKNLR EYCKANNIMI TAHSVLGAVG AAWGTKAVMH SKVLHQIAVA
     RGKSVAQVSM RWVYQQGASL VVKSFNEARM KENLKIFDWE LTAEDMEKIS EIPQSRTSSA
     AFLLSPTGPF KTEEEFWDEK D