C82A3_SOYBN
ID C82A3_SOYBN Reviewed; 527 AA.
AC O49858;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome P450 82A3;
DE EC=1.14.-.-;
DE AltName: Full=Cytochrome P450 CP6;
GN Name=CYP82A3;
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Harosoy 63;
RX PubMed=9648734; DOI=10.1007/s004380050736;
RA Schopfer C.R., Ebel J.;
RT "Identification of elicitor-induced cytochrome P450s of soybean (Glycine
RT max L.) using differential display of mRNA.";
RL Mol. Gen. Genet. 258:315-322(1998).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC -!- INDUCTION: By fungal elicitor.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; Y10982; CAA71876.1; -; mRNA.
DR PIR; T07748; T07748.
DR RefSeq; NP_001240972.1; NM_001254043.1.
DR AlphaFoldDB; O49858; -.
DR SMR; O49858; -.
DR STRING; 3847.GLYMA13G04670.1; -.
DR PRIDE; O49858; -.
DR EnsemblPlants; KRH18576; KRH18576; GLYMA_13G068800.
DR GeneID; 100789386; -.
DR Gramene; KRH18576; KRH18576; GLYMA_13G068800.
DR KEGG; gmx:100789386; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; O49858; -.
DR OMA; HAFDFSI; -.
DR OrthoDB; 702827at2759; -.
DR Proteomes; UP000008827; Chromosome 13.
DR Genevisible; O49858; GM.
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 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 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..527
FT /note="Cytochrome P450 82A3"
FT /id="PRO_0000052164"
FT BINDING 464
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"
SQ SEQUENCE 527 AA; 59823 MW; CA3429E87B202210 CRC64;
MDLLLNCLNL NTIAIASILS LIFLCLFLYR KNSRGKDAPV VSGAWPILGH LSLLNGSQTP
HKVLGALADK YGPLFTIKLG MKPALVLSNW EMSKELFTTN DLAVSSRPKL VAVEVMSYNQ
AFVGLAPYGP YWRELRKIVT FEFLSNRRIE QRNHIRVSEV RTSIKELFDI WSNGNKNESR
YTLVDIKQWL AYLTFNMVVR MVVGKRYFGV MHVEGKDKAQ RFMKNIREFM NLMGTFTVAD
GVPCLRWLDL GGHEKAMKAN AKEVDKLLSE WLEEHRQKKL LGENVESDRD FMDVMISALN
GAQIGAFDAD TICKATSLEL ILGGTDSTAV TLTWALSLLL RNPLALGKAK EEIDMQIGKD
EYIRESDISK LVYLQAIVKE TLRLYPPAPF SSPREFTENC ILGGYHIKKG TRLIHNLWKI
HRDPSVWSDP LEFKPERFLT THKDVDLRGH NFELLPFGSG RRVCAGMSLG LNMVHFTLAN
LLHSFDILNP SAEPVDMTEF FGFTNTKATP LEILVKPRQS PNYYETL
