ID   C96T2_NARAP             Reviewed;         513 AA.
AC   A0A140IL91;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Noroxomaritidine synthase 2 {ECO:0000303|PubMed:26941773};
DE            EC=1.14.19.50 {ECO:0000250|UniProtKB:A0A140IL90};
DE   AltName: Full=CYP96T2 {ECO:0000303|PubMed:26941773};
DE   AltName: Full=Cytochrome P450 96T2 {ECO:0000303|PubMed:26941773};
GN   Name=Cyp96T2 {ECO:0000303|PubMed:26941773};
OS   Narcissus aff. pseudonarcissus MK-2014 (Daffodil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Amaryllidoideae; Narcissus.
OX   NCBI_TaxID=1540222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=26941773; DOI=10.3389/fpls.2016.00225;
RA   Kilgore M.B., Augustin M.M., May G.D., Crow J.A., Kutchan T.M.;
RT   "CYP96T1 of Narcissus sp. aff. pseudonarcissus catalyzes formation of the
RT   para-para' C-C phenol couple in the Amaryllidaceae alkaloids.";
RL   Front. Plant Sci. 7:225-225(2016).
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KT693312; AMO65742.1; -; mRNA.
DR   AlphaFoldDB; A0A140IL91; -.
DR   SMR; A0A140IL91; -.
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_0000450648"
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;  58975 MW;  C53B07E017C9B8BE CRC64;
     MATSSSAWLM FSDHYPEILI AIACFLIFSL LLSARSSSED 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 NDGFTLFDSN
     MIQSAIYLHA ALCEALRIYP PVPFEIKDAH KADVLPSGHK VRAGEKILFS PYAMARMKGI
     WGDDCLEFKP ERWITGNGTL KHEPAYKFFA FSAGPRICLG KELSFTQMKM VVATIIYNFH
     LQMVKGHVVE QSNSILMDMK HGLMVQVRKR SVM