ID   C82A1_PEA               Reviewed;         544 AA.
AC   Q43068;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cytochrome P450 82A1;
DE            EC=1.14.-.-;
DE   AltName: Full=CYPLXXXII;
DE   Flags: Fragment;
GN   Name=CYP82A1; Synonyms=CYP82;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Stem;
RX   PubMed=8819874; DOI=10.1104/pp.110.3.1035;
RA   Frank M.R., Deyneka J.M., Schuler M.A.;
RT   "Cloning of wound-induced cytochrome P450 monooxygenases expressed in
RT   pea.";
RL   Plant Physiol. 110:1035-1046(1996).
RN   [2]
RP   SEQUENCE REVISION TO 47-48; 127; 198-199; 304; 311; 333-335 AND 454.
RA   Frank M.R.;
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC   -!- INDUCTION: By wounding.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U29333; AAC49188.2; -; mRNA.
DR   PIR; T06523; T06523.
DR   AlphaFoldDB; Q43068; -.
DR   SMR; Q43068; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   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   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           <1..544
FT                   /note="Cytochrome P450 82A1"
FT                   /id="PRO_0000052162"
FT   BINDING         481
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"
FT   NON_TER         1
SQ   SEQUENCE   544 AA;  62055 MW;  DE006067C33DADE5 CRC64;
     FVLNYLNTTT IAFISLISLL FFLFRFSKVS HTKEPPIISG SWPLLGHLPL MRNTQTPHKT
     LGALVDKYGP IFTIKLGATN ALVLSNWELA KECFTKNDIV VSSRPKPVAV ELMSYNQAFI
     GWAPYGAYWR QLRKIVTLEI LSNRRIELLS HIRVSEVQTS IKELVNVWSN QISSQYGLLD
     DTKSSSTNDE PSTTDYVSVE LKKWFAQLTL NMVLRMVVGK RCFGDVDVEN KEEAKRFLEN
     IRDFMRLIGT FTVGDGVPFL KWLDLGGHEK EMKKCAKKFD VMLNEWLEEH REKKGLGSED
     KVVGERDFMD AMLLVLKDKP IEGFDVDTII KATTLELILG GSDTTAGTLT WAMCLLLKHP
     HVLEKLKEEL NTYIGKERCV NESDINKLVY LHAIIKETLR LYPPAPFSSP REFTEDCTIG
     GYHIKKGTRL MPNLWKIHRD PSVWPDPLEF KPERFLSTHK DVDVRGQNFE LLPFGSGRRM
     CAGMSLGLHM VHYILANFLH SFEILNPSPE SIDVTEVLEF VTTKATPLEV LVKPCLSFKC
     YESM