C96T3_NARAP
ID C96T3_NARAP Reviewed; 513 AA.
AC A0A140IL92;
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 3 {ECO:0000303|PubMed:26941773};
DE EC=1.14.19.50 {ECO:0000250|UniProtKB:A0A140IL90};
DE AltName: Full=CYP96T3 {ECO:0000303|PubMed:26941773};
DE AltName: Full=Cytochrome P450 96T3 {ECO:0000303|PubMed:26941773};
GN Name=Cyp96T3 {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}.
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DR EMBL; KT693313; AMO65743.1; -; mRNA.
DR AlphaFoldDB; A0A140IL92; -.
DR SMR; A0A140IL92; -.
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 3"
FT /id="PRO_0000450649"
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; 58954 MW; BF3865A090980F03 CRC64;
MATSSSAWLI FSDHYPEILI AIACFLIFSL LLSARSSSED SLPYNWPIFG MLPAIISNSQ
FNDFTTARLR KMGWTFIFKG PWLLDMDYIF TCDPSNINHM FNDNFENYPK GELGKVFDIF
GNNIFNADGD LWHDHRKMAQ TILWDGNYRT MQATFIRNKM DNALIPILDS AASKRKPVDL
QDVFFRFTFD TSCFSVLAAD PESLTMEFPA VPFSKAADQA LDAALTRHIT PRLIWKLKRF
FNVGSERTLA VAWKVIDSYI YDKIAELKAK RKLVGKINSY DAVSFYMDNF NIHDDKFLRD
NAFTYLLAQR NTQSLTMAWL FYALFENPKV ELKILSELKS IVDESSERRF NDGFALFDSN
MIQSAIYLHA TLCEALRIYP PVPFEIKDAH KADVLPSGHK VRAGEKILFS PYAMARMKGI
WGDDCLEFKP ERWITGNGTL KHEPAYKFFA FSAGPRICLG KELSFTQMKM VVATIIYNFH
LQMVKGHVVE QSNSILMDMK HGLMVQVRKR SVM