C80B3_PAPSO
ID C80B3_PAPSO Reviewed; 481 AA.
AC Q9SP06; Q9M7I3;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=(S)-N-methylcoclaurine 3'-hydroxylase isozyme 1 {ECO:0000305};
DE EC=1.14.14.102 {ECO:0000250|UniProtKB:O64899};
DE AltName: Full=Cytochrome P450 80B1 {ECO:0000303|PubMed:15849302};
DE AltName: Full=Cytochrome P450 80B3 {ECO:0000303|PubMed:17189709};
DE Flags: Fragment;
GN Name=CYP80B3 {ECO:0000303|PubMed:17189709};
GN Synonyms=CYP80B1 {ECO:0000303|PubMed:15849302}, NMCH1 {ECO:0000305};
OS Papaver somniferum (Opium poppy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Papaver.
OX NCBI_TaxID=3469 {ECO:0000312|EMBL:AAF05621.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang F.-C., Kutchan T.M.;
RT "Distribution of morphinan and benzophenanthridine alkaloid gene transcript
RT accumulation in the opium poppy Papaver somniferum.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY ELICITOR, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RC STRAIN=cv. Marianne;
RX PubMed=15849302; DOI=10.1104/pp.105.059287;
RA Alcantara J., Bird D.A., Franceschi V.R., Facchini P.J.;
RT "Sanguinarine biosynthesis is associated with the endoplasmic reticulum in
RT cultured opium poppy cells after elicitor treatment.";
RL Plant Physiol. 138:173-183(2005).
RN [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Marianne;
RX PubMed=16813579; DOI=10.1111/j.1365-313x.2006.02801.x;
RA Samanani N., Alcantara J., Bourgault R., Zulak K.G., Facchini P.J.;
RT "The role of phloem sieve elements and laticifers in the biosynthesis and
RT accumulation of alkaloids in opium poppy.";
RL Plant J. 47:547-563(2006).
RN [4]
RP FUNCTION, AND NOMENCLATURE.
RX PubMed=17189709; DOI=10.1016/j.ymben.2006.10.004;
RA Frick S., Kramell R., Kutchan T.M.;
RT "Metabolic engineering with a morphine biosynthetic P450 in opium poppy
RT surpasses breeding.";
RL Metab. Eng. 9:169-176(2007).
RN [5]
RP FUNCTION.
RX PubMed=22725256; DOI=10.1111/j.1365-313x.2012.05084.x;
RA Desgagne-Penix I., Facchini P.J.;
RT "Systematic silencing of benzylisoquinoline alkaloid biosynthetic genes
RT reveals the major route to papaverine in opium poppy.";
RL Plant J. 72:331-344(2012).
CC -!- FUNCTION: Involved in the biosynthesis of benzylisoquinoline alkaloids.
CC Catalyzes the 3'-hydroxylation of (S)-N-methylcoclaurine.
CC {ECO:0000269|PubMed:15849302, ECO:0000269|PubMed:17189709,
CC ECO:0000269|PubMed:22725256}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-N-methylcoclaurine + O2 + reduced [NADPH--hemoprotein
CC reductase] = (S)-3'-hydroxy-N-methylcoclaurine + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:16649,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57993, ChEBI:CHEBI:58010, ChEBI:CHEBI:58210;
CC EC=1.14.14.102; Evidence={ECO:0000250|UniProtKB:O64899};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)-
CC reticuline from (S)-norcoclaurine: step 3/4.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:15849302}. Note=Like CYP80B3b (AC I3V6B1), the
CC full-length CYP80B3 is probably anchored to the membrane by a signal
CC anchor. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Localized to the sieve elements in the root and
CC hypocotyl. {ECO:0000269|PubMed:16813579}.
CC -!- DEVELOPMENTAL STAGE: Increases rapidly between 1 and 3 days after seed
CC germination. {ECO:0000269|PubMed:16813579}.
CC -!- INDUCTION: Up-regulated upon elicitor treatment (at protein level).
CC {ECO:0000269|PubMed:15849302}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000255|RuleBase:RU000461}.
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DR EMBL; AF134590; AAF61400.1; -; mRNA.
DR EMBL; AF191772; AAF05621.1; -; mRNA.
DR AlphaFoldDB; Q9SP06; -.
DR SMR; Q9SP06; -.
DR UniPathway; UPA00306; UER00443.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050593; F:N-methylcoclaurine 3'-monooxygenase activity; IMP:UniProtKB.
DR GO; GO:1901012; P:(S)-reticuline biosynthetic process; IMP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; IDA:UniProtKB.
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; Endoplasmic reticulum; Heme; Iron; Metal-binding;
KW Monooxygenase; Oxidoreductase.
FT CHAIN <1..481
FT /note="(S)-N-methylcoclaurine 3'-hydroxylase isozyme 1"
FT /id="PRO_0000433982"
FT BINDING 423
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:P04798"
FT CONFLICT 125
FT /note="E -> D (in Ref. 1; AAF61400)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="R -> S (in Ref. 1; AAF61400)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="F -> L (in Ref. 1; AAF61400)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAF05621.1"
SQ SEQUENCE 481 AA; 54242 MW; 079A943A81ABED2E CRC64;
SLVAVVITTF LYLIFRDSSP KGLPPGPKPW PIVGNLLQLG EKPHSQFAQL AETYGDLFSL
KLGSETVVVA STPLAASEIL KTHDRVLSGR YVFQSFRVKE HVENSIVWSE CNETWKKLRK
VCRTELFTQK MIESQAEVRE SKAMEMVEYL KKNVGNEVKI AEVVFGTLVN IFGNLIFSQN
IFKLGDESSG SVEMKEHLWR MLELGNSTNP ADYFPFLGKF DLFGQSKDVA DCLQGIYSVW
GAMLKERKIA KQHNNSKKND FVEILLDSGL DDQQINALLM EIFGAGTETS ASTIEWALSE
LTKNPQVTAN MRLELLSVVG KRPVKESDIP NMPYLQAFVK ETLRLHPATP LLLPRRALET
CKVLNYTIPK ECQIMVNAWG IGRDPKRWTD PLKFSPERFL NSSIDFKGND FELIPFGAGR
RICPGVPLAT QFISLIVSSL VQNFDWGFPK GMDPSQLIME EKFGLTLQKE PPLYIVPKTR
D
