C82A2_SOYBN
ID C82A2_SOYBN Reviewed; 522 AA.
AC O81972;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cytochrome P450 82A2;
DE EC=1.14.-.-;
DE AltName: Full=Cytochrome P450 CP4;
GN Name=CYP82A2;
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}.
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; Y10491; CAA71515.1; -; mRNA.
DR PIR; T07118; T07118.
DR RefSeq; NP_001240077.1; NM_001253148.1.
DR AlphaFoldDB; O81972; -.
DR SMR; O81972; -.
DR STRING; 3847.GLYMA13G36110.2; -.
DR PRIDE; O81972; -.
DR EnsemblPlants; KRH22207; KRH22207; GLYMA_13G285300.
DR EnsemblPlants; KRH22208; KRH22208; GLYMA_13G285300.
DR EnsemblPlants; KRH22209; KRH22209; GLYMA_13G285300.
DR GeneID; 100798546; -.
DR Gramene; KRH22207; KRH22207; GLYMA_13G285300.
DR Gramene; KRH22208; KRH22208; GLYMA_13G285300.
DR Gramene; KRH22209; KRH22209; GLYMA_13G285300.
DR KEGG; gmx:100798546; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; O81972; -.
DR OMA; KQWFENL; -.
DR OrthoDB; 702827at2759; -.
DR Proteomes; UP000008827; Chromosome 13.
DR Genevisible; O81972; 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..522
FT /note="Cytochrome P450 82A2"
FT /id="PRO_0000052163"
FT BINDING 459
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 522 AA; 58716 MW; 953E7AD79AC93FCA CRC64;
MELVLNSTTI GVGVVSLILL LYLFLRGGSW KSGEEGPPTV AGAWPIIGHL PLLLGSKTPH
KTLGDLADKY GPIFSIKIGA KNAVVVSNWE MAKECYTTND IAVSSLPDLI SANLLCYNRS
MIVVAPYGPY WRQLRKILMS EFLSPSRVEQ LHHVRVSEVQ SSITELFRDW RSNKNVQSGF
ATVELKQWFS LLVFNMILRM VCGKRYFSAS TSDDEKANRC VKAVDEFVRL AATFTVGDAI
PYLRWFDFGG YENDMRETGK ELDEIIGEWL DEHRQKRKMG ENVQDLMSVL LSLLEGKTIE
GMNVDIVIKS FVLTVIQAGT EASITTLIWA TSLILNNPSV LEKLKAELDI QVGKERYICE
SDLSKLTYLQ AVVKETLRLY PPAPLSRPRE FEEDCTIGGY TVKKGTRLIT NLSKIHTDHN
VWSNPLEFKP ERFLTTDKDI DMKGQHFQLL PFGGGRRICP GINLGLQTVR LTLASFLHSF
EILNPSTEPL DMTEVFRATN TKATPLEILI KPRLSPSCYE SI