COR13_PAPSO
ID COR13_PAPSO Reviewed; 321 AA.
AC Q9SQ68;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=NADPH-dependent codeinone reductase 1-3;
DE EC=1.1.1.247;
GN Name=COR1.3;
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], PROTEIN SEQUENCE OF 130-135; 172-177; 233-243
RP AND 245-248, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY,
RP AND CATALYTIC ACTIVITY.
RX PubMed=10417697; DOI=10.1046/j.1365-313x.1999.00470.x;
RA Unterlinner B., Lenz R., Kutchan T.M.;
RT "Molecular cloning and functional expression of codeinone reductase: the
RT penultimate enzyme in morphine biosynthesis in the opium poppy Papaver
RT somniferum.";
RL Plant J. 18:465-475(1999).
RN [2]
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. {ECO:0000269|PubMed:10417697}.
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; Evidence={ECO:0000269|PubMed:10417697};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=187 uM for codeine (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC KM=48 uM for codeinone (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC KM=205 uM for NADPH (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC KM=45 uM for NADP (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC KM=200 uM for morphine (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC KM=628 uM for dihydrocodeine (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC KM=143 uM for morphinone (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC KM=55 uM for hydrocodone (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC KM=90 uM for hydromorphone (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC pH dependence:
CC Optimum pH is 6.8 for reduction (forward reaction) and 9.0 for
CC oxidation (reverse reaction). {ECO:0000269|PubMed:10417697};
CC Temperature dependence:
CC Optimum temperature is 28 degrees Celsius for reduction (forward
CC reaction) and 30 degrees Celsius for reduction (reverse reaction).
CC {ECO:0000269|PubMed:10417697};
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). Expressed
CC constitutively in all organs. {ECO:0000269|PubMed:10417697,
CC ECO:0000269|PubMed:11079569}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AF108434; AAF13738.1; -; mRNA.
DR PDB; 7MBF; X-ray; 2.40 A; A/B/C/D/E/F=1-321.
DR PDBsum; 7MBF; -.
DR AlphaFoldDB; Q9SQ68; -.
DR SMR; Q9SQ68; -.
DR PRIDE; Q9SQ68; -.
DR UniPathway; UPA00852; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0047036; F:codeinone reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
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 3D-structure; Alkaloid metabolism; Cytoplasm; Direct protein sequencing;
KW NADP; Oxidoreductase.
FT CHAIN 1..321
FT /note="NADPH-dependent codeinone reductase 1-3"
FT /id="PRO_0000418593"
FT REGION 300..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:7MBF"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:7MBF"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:7MBF"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:7MBF"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:7MBF"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:7MBF"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:7MBF"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:7MBF"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:7MBF"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:7MBF"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:7MBF"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:7MBF"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:7MBF"
FT HELIX 313..317
FT /evidence="ECO:0007829|PDB:7MBF"
SQ SEQUENCE 321 AA; 35797 MW; 2C6969133A95D42B CRC64;
MESNGVPMIT LSSGIRMPAL GMGTAETMVK GTEREKLAFL KAIEVGYRHF DTAAAYQSEE
CLGEAIAEAL QLGLIKSRDE LFITSKLWCA DAHADLVLPA LQNSLRNLKL DYLDLYLIHH
PVSLKPGKFV NEIPKDHILP MDYKSVWAAM EECQTLGFTR AIGVCNFSCK KLQELMAAAK
IPPVVNQVEM SPTLHQKNLR EYCKANNIMI TAHSVLGAIC APWGSNAVMD SKVLHQIAVA
RGKSVAQVSM RWVYQQGASL VVKSFNEGRM KENLKIFDWE LTAENMEKIS EIPQSRTSSA
DFLLSPTGPF KTEEEFWDEK D
