COR14_PAPSO
ID COR14_PAPSO Reviewed; 321 AA.
AC Q9SQ67; B9VRJ3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=NADPH-dependent codeinone reductase 1-4;
DE EC=1.1.1.247;
GN Name=COR1.4;
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, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
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 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 [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. {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=140 uM for codeine (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC KM=50 uM for codeinone (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC KM=197 uM for NADPH (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10417697};
CC KM=55 uM for NADP (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 -!- 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}.
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DR EMBL; AF108435; AAF13739.1; -; mRNA.
DR EMBL; FJ596161; ACM44063.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9SQ67; -.
DR SMR; Q9SQ67; -.
DR EnsemblPlants; RZC68126; RZC68126; C5167_031384.
DR Gramene; RZC68126; RZC68126; C5167_031384.
DR OMA; QIAMERG; -.
DR BioCyc; MetaCyc:MON-12302; -.
DR BRENDA; 1.1.1.247; 4515.
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 Alkaloid metabolism; Cytoplasm; Direct protein sequencing; NADP;
KW Oxidoreductase.
FT CHAIN 1..321
FT /note="NADPH-dependent codeinone reductase 1-4"
FT /id="PRO_0000418594"
FT REGION 299..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 CONFLICT 145
FT /note="T -> S (in Ref. 1; AAF13739)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="D -> A (in Ref. 1; AAF13739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35764 MW; 2B8D306B2D921087 CRC64;
MESNGVPMIT LSSGIRMPAL GMGTAETMVK GTEREKLAFL KAIEVGYRHF DTAAAYQSEE
CLGEAIAEAL QLGLIKSRDE LFITSKLWCA DAHADLVLPA LQNSLRNLKL EYLDLYLIHH
PVSLKPGKFV NEIPKDHILP MDYKTVWAAM EECQTLGFTR AIGVSNFSCK KLQELMAAAK
IPPVVNQVEM SPTLHQKNLR EYCKANNIMI TAHSVLGAIG APWGSNAVMD SKVLHQIAVA
RGKSVAQVSM RWVYQQGASL VVKSFNEGRM KENLKIFDWE LTAEDMEKIS EIPQSRTSSA
DFLLSPTGPF KTEEEFWDEK D
