ID   C96T2_NARPS             Reviewed;         513 AA.
AC   A0A2H5AIZ9;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Noroxomaritidine synthase 2 {ECO:0000303|PubMed:29229969};
DE            EC=1.14.19.50 {ECO:0000250|UniProtKB:A0A140IL90};
DE   AltName: Full=CYP96T2 {ECO:0000303|PubMed:29229969};
DE   AltName: Full=Cytochrome P450 96T2 {ECO:0000303|PubMed:29229969};
GN   Name=Cyp96T2 {ECO:0000303|PubMed:29229969};
OS   Narcissus pseudonarcissus (Daffodil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Amaryllidoideae; Narcissus.
OX   NCBI_TaxID=39639;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], REVIEW ON THE AMARYLLIDACEAE ALKALOID
RP   METABOLISM, PATHWAY, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. King Alfred; TISSUE=Bulb;
RX   PubMed=29229969; DOI=10.1038/s41598-017-17724-0;
RA   Singh A., Desgagne-Penix I.;
RT   "Transcriptome and metabolome profiling of Narcissus pseudonarcissus 'King
RT   Alfred' reveal components of Amaryllidaceae alkaloid metabolism.";
RL   Sci. Rep. 7:17356-17356(2017).
CC   -!- FUNCTION: Cytochrome P450 that catalyzes an intramolecular para-para'
CC       C-C phenol coupling of 4'-O-methylnorbelladine in alkaloids
CC       biosynthesis, including haemanthamine- and crinamine-type alkaloids,
CC       promising anticancer agents. Catalyzes the formation of (10bR,4aS)-
CC       noroxomaritidine and (10bS,4aR)-noroxomaritidine from 4'-O-
CC       methylnorbelladine. {ECO:0000250|UniProtKB:A0A140IL90}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4'-O-methylnorbelladine + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (10bR,4aS)-noroxomaritidine + H(+) + 2 H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51260, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:133993, ChEBI:CHEBI:133995;
CC         EC=1.14.19.50; Evidence={ECO:0000250|UniProtKB:A0A140IL90};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4'-O-methylnorbelladine + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (10bS,4aR)-noroxomaritidine + H(+) + 2 H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51264, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:133993, ChEBI:CHEBI:133996;
CC         EC=1.14.19.50; Evidence={ECO:0000250|UniProtKB:A0A140IL90};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q96242};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000250|UniProtKB:A0A140IL90}.
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000303|PubMed:29229969}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in stems, and, to a lower extent,
CC       in bulbs, roots, leaves and flowers. {ECO:0000269|PubMed:29229969}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; MF416098; AUG71943.1; -; mRNA.
DR   AlphaFoldDB; A0A2H5AIZ9; -.
DR   SMR; A0A2H5AIZ9; -.
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:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Alkaloid metabolism; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..513
FT                   /note="Noroxomaritidine synthase 2"
FT                   /id="PRO_0000450647"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         458
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   513 AA;  58974 MW;  DE2AF8AD5C44EC64 CRC64;
     MATSSSAWLM FSDHYPEILI AIACFLIFSL LLSARSSSKD SLPYNWPIFG MLPAIISNNQ
     FNDFTTARLR KMGWTFIFKG PWLLDMDYIF TCDPSNINHM FNDNFENYPK GELGKVFDIF
     GNNIFNADGD LWHDHRKMAQ TILWDGNYRT MQATFIRNKM DNALIPILDS AACKRKPVDL
     QDVLLRFTFD TSCFSVLAAD PESLTMEFPP VPFSKAADQA LDAALTRHIT PRLIWKLKRF
     FNVGSERTLA VAWKVIDSYI YDKIAELKAK RKLVGKINSY DAVSFYMDNF NIHDDKFLRD
     NAFTYLLAQR NTQSLTMTWL FYALFENPKV ELKILSELKS IVDESSERKF NDGFALFDSN
     MIQSAIYLHA TLCEALRIYP PVPFEIKDAH KADVLPSGHK VRAGEKILFS PYAMARMKGI
     WGDDCLEFKP ERWITGNGTL KHEPAYKFFA FSAGPRICLG KELSFTQMKM VVATIIYNFH
     LQMVKGHVVE QSNSILMDMK HGLMVQVRKR SVM