C80G2_COPJA
ID C80G2_COPJA Reviewed; 486 AA.
AC A8CDR5;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Corytuberine synthase {ECO:0000312|EMBL:BAF80448.1};
DE EC=1.14.19.51 {ECO:0000269|PubMed:18230623};
DE AltName: Full=Cytochrome P450 80G2;
GN Name=CYP80G2 {ECO:0000312|EMBL:BAF80448.1};
OS Coptis japonica (Japanese goldthread).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Coptidoideae;
OC Coptis.
OX NCBI_TaxID=3442;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND MUTAGENESIS OF PRO-290.
RC STRAIN=cv. dissecta;
RX PubMed=18230623; DOI=10.1074/jbc.m705082200;
RA Ikezawa N., Iwasa K., Sato F.;
RT "Molecular cloning and characterization of CYP80G2, a cytochrome P450 that
RT catalyzes an intramolecular C-C phenol coupling of (S)-reticuline in
RT magnoflorine biosynthesis, from cultured Coptis japonica cells.";
RL J. Biol. Chem. 283:8810-8821(2008).
CC -!- FUNCTION: Cytochrome P450 that catalyzes an intramolecular C-C phenol
CC coupling of (S)-reticuline in magnoflorine biosynthesis. Catalyzes the
CC formation of (S)-corytuberine from (S)-reticuline, and also, with a
CC lover efficiency, the 4'-O-demethylation of codamine to produce
CC orientaline, and subsequent C-C-phenol coupling of orientaline. Can
CC also use (R,S)-norreticuline, (R,S)-orientaline, (S)-N-methylcoclaurine
CC and (S)-coclaurine as substrates, but not (R,S)-6-O-
CC methyllaudanosoline, (R,S)-6-O-methylnorlaudanosoline, (R,S)-laudanine,
CC (R,S)-norlaudanine, (R,S)-4'-O-methyllaudanosoline, (R,S)-
CC pseudocodamine, (R,S)-norpseudocodamine, (R,S)-laudanosine, (R,S)-
CC norlaudanosine, (R,S)-laudanosoline or (R,S)-norlaudanosoline.
CC {ECO:0000269|PubMed:18230623}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-reticuline + O2 + reduced [NADPH--hemoprotein reductase] =
CC (S)-corytuberine + 2 H(+) + 2 H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51540, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:57873, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:81200; EC=1.14.19.51;
CC Evidence={ECO:0000269|PubMed:18230623};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:18230623};
CC -!- ACTIVITY REGULATION: Inhibited by ketoconazole.
CC {ECO:0000269|PubMed:18230623}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34.1 uM for (R,S)-reticuline {ECO:0000269|PubMed:18230623};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:18230623}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB288053; BAF80448.1; -; mRNA.
DR AlphaFoldDB; A8CDR5; -.
DR SMR; A8CDR5; -.
DR KEGG; ag:BAF80448; -.
DR BRENDA; 1.14.19.51; 1610.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102963; F:(S)-corytuberine synthase activity; IEA:UniProtKB-EC.
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:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound 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; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..486
FT /note="Corytuberine synthase"
FT /id="PRO_0000439853"
FT TRANSMEM 6..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 428
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"
FT MUTAGEN 290
FT /note="P->A,G: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:18230623"
SQ SEQUENCE 486 AA; 55012 MW; 98B128F61F1E3F1E CRC64;
MDLQIALFSL IPVILVFILL LKPKYKNLPP GPHPWPLIGN LPILFTNTEV PLHITLANMA
RTHGPIMILW LGTQPTVMAS TAEAAMEILK THDRIFSARH IRMSFRLKHH IKYSLVWSDC
TDYWKLLRKI VRTEIFSPKM LQAQSHVREQ KVAELIDFLR SKEGQVVKIS QFVFGTLLNI
LGNVVFSKDV FVYGDETDKG GIQNLIREML MIGAEPNVAE FYPSLEELDL QGLKKKCDER
FIRVMKMWEG TVKERKANRN EESKDMLDVL LANDFNDAQI NALFLETFGP GSETSSATIE
WVIAELIKSP KEMAKVRKEL NEVVGTSTIK ESDLPQLPYL QACIKEAMRL HPAAPFLLPR
RAAETCEVMG YTIPKNSQVL VNAYAIGRDP KSWKDPSTFW PERFLESDVD FHGAHYQFIP
FGSGRRTCVG MPLATRTIPL IVGSLVHNYD FGLPGGNRPE DLKMNEMLSL TLAIDPSLCV
VPKARA
