C82Y1_PAPSO
ID C82Y1_PAPSO Reviewed; 556 AA.
AC I3PLR1;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=(S)-N-methylcanadine 1-hydroxylase CYP82Y1 {ECO:0000305};
DE EC=1.14.14.166 {ECO:0000269|PubMed:24324259, ECO:0000269|PubMed:27378283};
DE AltName: Full=Cytochrome P450 82Y1 {ECO:0000303|PubMed:22653730};
GN Name=CYP82Y1 {ECO:0000303|PubMed:22653730};
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], AND TISSUE SPECIFICITY.
RX PubMed=22653730; DOI=10.1126/science.1220757;
RA Winzer T., Gazda V., He Z., Kaminski F., Kern M., Larson T.R., Li Y.,
RA Meade F., Teodor R., Vaistij F.E., Walker C., Bowser T.A., Graham I.A.;
RT "A Papaver somniferum 10-gene cluster for synthesis of the anticancer
RT alkaloid noscapine.";
RL Science 336:1704-1708(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24324259; DOI=10.1074/jbc.m113.505099;
RA Dang T.T., Facchini P.J.;
RT "CYP82Y1 is N-methylcanadine 1-hydroxylase, a key noscapine biosynthetic
RT enzyme in opium poppy.";
RL J. Biol. Chem. 289:2013-2026(2014).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27378283; DOI=10.1038/ncomms12137;
RA Li Y., Smolke C.D.;
RT "Engineering biosynthesis of the anticancer alkaloid noscapine in yeast.";
RL Nat. Commun. 7:12137-12137(2016).
RN [4]
RP FUNCTION.
RX PubMed=29610307; DOI=10.1073/pnas.1721469115;
RA Li Y., Li S., Thodey K., Trenchard I., Cravens A., Smolke C.D.;
RT "Complete biosynthesis of noscapine and halogenated alkaloids in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E3922-E3931(2018).
CC -!- FUNCTION: Cytochrome P450 involved in the biosynthesis of the
CC benzylisoquinoline alkaloid noscapine (PubMed:24324259,
CC PubMed:27378283, PubMed:29610307). Converts (S)-N-methylcanadine to
CC (S)-1-hydroxy-N-methylcanadine (PubMed:24324259, PubMed:27378283).
CC {ECO:0000269|PubMed:24324259, ECO:0000269|PubMed:27378283,
CC ECO:0000269|PubMed:29610307}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-N-methylcanadine + O2 + reduced [NADPH--hemoprotein
CC reductase] = (S)-1-hydroxy-N-methylcanadine + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:57376, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16512,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:141633;
CC EC=1.14.14.166; Evidence={ECO:0000269|PubMed:24324259,
CC ECO:0000269|PubMed:27378283};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57377;
CC Evidence={ECO:0000305|PubMed:24324259};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.5 uM for (S)-N-methylcanadine {ECO:0000269|PubMed:24324259};
CC Vmax=98 pmol/min/mg enzyme with (S)-N-methylcanadine as substrate
CC {ECO:0000269|PubMed:24324259};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in capsules (PubMed:22653730).
CC Expressed is stems (PubMed:22653730). {ECO:0000269|PubMed:22653730}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; JQ659005; AFB74617.1; -; Genomic_DNA.
DR AlphaFoldDB; I3PLR1; -.
DR SMR; I3PLR1; -.
DR EnsemblPlants; RZC84733; RZC84733; C5167_047515.
DR Gramene; RZC84733; RZC84733; C5167_047515.
DR KEGG; ag:AFB74617; -.
DR BioCyc; MetaCyc:MON-20623; -.
DR BRENDA; 1.14.14.166; 4515.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0033075; P:isoquinoline alkaloid biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..556
FT /note="(S)-N-methylcanadine 1-hydroxylase CYP82Y1"
FT /id="PRO_0000447598"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 500
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q96242"
SQ SEQUENCE 556 AA; 62928 MW; 5C1BD6551B78722E CRC64;
MAYLMIKKSI YLFFDQPTAV GTLILAFLLT LSPVIIYYEQ KKRGLRRNRT AITTTPLPEA
SGAWPVIGHL LLFMNENDLN HVTLGHMADK YGPIFSLRFG RHRTLVVSSW EMVKECFTGT
NDKLFSNRPS SLAVKLMFYD TESYGFAPYG KYWRELRKIS THKLLSNQQL EKFKHLRISE
VDNSFKKLHE LCSNNKQGGD TTYVASLVRM DDWFAYLTFN VIGRIVSGFQ SNAVAGATNS
QEKYKLAIDE VSNLMATFAV SDVVPRLGWI DRLTGLTGKM KNCGKKLDAV VGDAVEDHRQ
KKLKISRNNT GALTEHEEED FIDVCLSIME QSQIPGNHPE ISVKSIALDM LSGGSDTTKL
IMTWTLSLLL NHPDILDKAK EEVDTYFGKK KISDNTPVVD AADVPNLVYI QAIIKESMRL
YPASTLMERM TSDDCDVGGF HVPAGTRLWV NVWKMQRDPR VWKDPLVFLP ERFLSNDKGM
VDVKGQNYEL IPFGTGRRIC PGASFALEVL HLVLTRLILE FEMKAPEGKI DMRARPGFFH
NKVVPLDVQL TPRTLD
