ID   C82E3_TOBAC             Reviewed;         518 AA.
AC   Q38Q84;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Cytochrome P450 82E3 {ECO:0000303|PubMed:16192354};
DE            Short=NtabCYP82E3 {ECO:0000303|PubMed:17102129};
DE            EC=1.14.14.- {ECO:0000269|PubMed:17102129};
GN   Name=CYP82E3 {ECO:0000303|PubMed:17102129};
GN   ORFNames=LOC107820314 {ECO:0000312|RefSeq:XP_016502060.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Burley;
RX   PubMed=16192354; DOI=10.1073/pnas.0506581102;
RA   Siminszky B., Gavilano L., Bowen S.W., Dewey R.E.;
RT   "Conversion of nicotine to nornicotine in Nicotiana tabacum is mediated by
RT   CYP82E4, a cytochrome P450 monooxygenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:14919-14924(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90;
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [3]
RP   FUNCTION, MUTAGENESIS OF CYS-330, PATHWAY, AND TISSUE SPECIFICITY.
RX   PubMed=17102129; DOI=10.1074/jbc.m609512200;
RA   Gavilano L.B., Coleman N.P., Bowen S.W., Siminszky B.;
RT   "Functional analysis of nicotine demethylase genes reveals insights into
RT   the evolution of modern tobacco.";
RL   J. Biol. Chem. 282:249-256(2007).
CC   -!- FUNCTION: No nicotine N-demethylase activity.
CC       {ECO:0000269|PubMed:16192354, ECO:0000269|PubMed:17102129}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC       {ECO:0000269|PubMed:17102129}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in green leaves.
CC       {ECO:0000269|PubMed:17102129}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. CYP82E2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; DQ131888; ABA07807.1; -; mRNA.
DR   RefSeq; NP_001312992.1; NM_001326063.1.
DR   RefSeq; XP_016502060.1; XM_016646574.1.
DR   SMR; Q38Q84; -.
DR   GeneID; 107820314; -.
DR   KEGG; nta:107820314; -.
DR   OMA; WRNMRSL; -.
DR   OrthoDB; 702827at2759; -.
DR   BRENDA; 1.14.14.1; 3645.
DR   UniPathway; UPA00107; -.
DR   Proteomes; UP000084051; Unplaced.
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:0098542; P:defense response to other organism; IBA:GO_Central.
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; Heme; Iron; Isopeptide bond; Membrane; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..518
FT                   /note="Cytochrome P450 82E3"
FT                   /id="PRO_0000455783"
FT   TRANSMEM        2..22
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:P04798"
FT   CROSSLNK        254
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZU1"
FT   MUTAGEN         330
FT                   /note="C->W: Confers nicotine N-demethylase (NND)
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:17102129"
SQ   SEQUENCE   518 AA;  59532 MW;  9768CDF6A31C99A2 CRC64;
     MVFPVEAIVG LVTFTFLFYF LWTKKSQKPS KPLPPKIPGG WPVIGHLFYF DDDGDDRPLA
     RKLGDLADKY GPVFTFRLGL PLVLVVSSYE AIKDCFSTND AIFSNRPAFL YGEYLGYKNA
     MLFLANYGSY WRKNRKLIIQ EVLSASRLEK FKHVRFARIQ TSIKNLYTRI DGNSSTINLT
     DWLEELNFGL IVKMIAGKNY ESGKGDEQVE RFKKAFKDFM ILSMEFVLWD AFPIPLFKWV
     DFQGHVKAMK RTFKDIDSVF QNWLEEHIKK REKIMEVGTE GNEQDFIDVV LSKMSNEYLG
     EGYSRDTVIK ATVFSLVLDA ADTVALHINC GMALLINNQN ALKKAQEEID TKVGKDRWVE
     ESDIKDLVYL QAIVKEVLRL YPPGPLLVPH ENVEDCVVSG YHIPKGTRLF ANVMKLQRDP
     KLWSNPDKFN PERFIARDID FHGQHYEYIP FGSGRRSCPG MTYALQVEHL TMAHLIQGFN
     YRTPTDEPLD MKEGAGITIR KVNPVKVIIT PRLAPELY