ID   C81E8_MEDTR             Reviewed;         499 AA.
AC   Q6WNQ8;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Cytochrome P450 81E8 {ECO:0000303|PubMed:14617078};
DE            EC=1.14.13.- {ECO:0000305};
GN   Name=CYP81E8 {ECO:0000303|PubMed:14617078};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000312|EMBL:AAQ20042.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=14617078; DOI=10.1046/j.1365-313x.2003.01893.x;
RA   Liu C.J., Huhman D., Sumner L.W., Dixon R.A.;
RT   "Regiospecific hydroxylation of isoflavones by cytochrome P450 81E enzymes
RT   from Medicago truncatula.";
RL   Plant J. 36:471-484(2003).
CC   -!- FUNCTION: Probable monooxygenases exhibiting no activity with
CC       isoflavones such as formononetin, biochanin A, pseudobaptigenin,
CC       daidzein, genistein, isoformononetin and prunetin, or with flavonoids
CC       including naringenin, liquiritigenin, apigenin, luteolin, or
CC       kaempferol. {ECO:0000269|PubMed:14617078}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000255|RuleBase:RU000461}.
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DR   EMBL; AY278229; AAQ20042.1; -; mRNA.
DR   AlphaFoldDB; Q6WNQ8; -.
DR   SMR; Q6WNQ8; -.
DR   STRING; 3880.AES94616; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   ExpressionAtlas; Q6WNQ8; differential.
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   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; NADP; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..499
FT                   /note="Cytochrome P450 81E8"
FT                   /id="PRO_0000430743"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         436
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"
SQ   SEQUENCE   499 AA;  57301 MW;  78190C308D51F447 CRC64;
     MTTFYLSLII SLFFLIITLK VFFNTSRKFK NLPPGPQCLP IIGNLHQLKQ PLHHTFHTLS
     QKYGQIFSLW FGSRLVVVVS SLTIAQECFT KNDIVLANRP HFLTGKYIGY NNTTVAQSPY
     GDHWRNLRRI LSIEILSSHR LNSFLEIRRD EIMRLIQKLA QKSYNGFTEV ELRPMFSEMT
     FNTIMRMVSG KRYYGNDCDV SDVEEARLFR GIIKEVVSLG GANNVGDFLG FLRWFDFDGL
     EKRLKKISKR TDAFLQGLID EHRFGKRNSN TMIDHLLTQQ QSQPEYYTDQ IIKGLMVVML
     LAGTDTSSVT IEWAMSNLLN HPEIMKKAKN ELDTHIGHDR QVDEHDISKL PYLQSIVYET
     LRLHAAAPLL VPHLSSEDFS LGGYNIPQNT ILMVNAWVIH RDPNLWSDPT CFKPERFEKE
     GEVNKLLSFG LGRRACPGEN LSQRTEGLTL GLLIQCFEWK RIGEEKIDMV EAKGITAGKK
     TSLNAMCKVR HPLKINDVF