ID   C81E1_GLYEC             Reviewed;         499 AA.
AC   P93147;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Isoflavone 2'-hydroxylase;
DE            EC=1.14.14.90 {ECO:0000269|PubMed:9790908};
DE   AltName: Full=CYP GE-3;
DE   AltName: Full=Cytochrome P450 81E1;
DE   AltName: Full=Cytochrome P450 91A4;
GN   Name=CYP81E1; Synonyms=CYP91A4;
OS   Glycyrrhiza echinata (Licorice).
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; Galegeae; Glycyrrhiza.
OX   NCBI_TaxID=46348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Akashi T., Aoki T., Kameya N., Nakamura I., Ayabe S.;
RT   "Two new cytochrome P450 cDNAs from elicitor-induced Licorice (Glycyrrhiza
RT   echinata L.) cells.";
RL   (er) Plant Gene Register PGR97-167(1997).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9790908; DOI=10.1006/bbrc.1998.9414;
RA   Akashi T., Aoki T., Ayabe S.;
RT   "CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata L.),
RT   encodes isoflavone 2'-hydroxylase.";
RL   Biochem. Biophys. Res. Commun. 251:67-70(1998).
CC   -!- FUNCTION: Catalyzes the hydroxylation of isoflavones, daidzein and
CC       formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and
CC       2'-hydroxyformononetin, respectively. {ECO:0000269|PubMed:9790908}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-unsubstituted isoflavone + O2 + reduced [NADPH--
CC         hemoprotein reductase] = a 2'-hydroxyisoflavone + H(+) + H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:18849,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28206,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:136891;
CC         EC=1.14.14.90; Evidence={ECO:0000269|PubMed:9790908};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC   -!- INDUCTION: By fungal elicitor.
CC   -!- MISCELLANEOUS: Involved in the biosynthesis of isoflavonoid-derived
CC       antimicrobial compounds of legumes.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB001379; BAA22422.1; -; mRNA.
DR   AlphaFoldDB; P93147; -.
DR   SMR; P93147; -.
DR   KEGG; ag:BAA22422; -.
DR   BRENDA; 1.14.14.90; 2486.
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:0033773; F:isoflavone 2'-hydroxylase activity; IEA:UniProtKB-EC.
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   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..499
FT                   /note="Isoflavone 2'-hydroxylase"
FT                   /id="PRO_0000052160"
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"
SQ   SEQUENCE   499 AA;  57192 MW;  4D03AFAC818C04DB CRC64;
     MEILSLLSYS VFYLALFFIF NIVIRARKFK NLPPGPPSLP IIGNLHHLKR PLHRTFKGLS
     EKYGHVFSLW FGSRLVVVVS SASEFQQCFT KNDVVLANRP RFLSGKYIFY NYTTLGSTSY
     GEHWRNLRRI TALDVLSNHR INSFSGIRRD ETQRLITRLA DDSSTNFAEM ELSSRLYDMT
     FNNIMRMISG KRYYGEDCDT SDLQEASQFR DMVSELLQLS GANNKTDFMP LLRFLDFENL
     EKRLKDISGK TDAFLRGLIE EHRTKKERAN TMIDHLLNLQ DSQPEYYTDQ IIKGLALAML
     LAGTDSSAVT LEWSMSNLLN HPEVLKKVKD ELDTHVGQDR LVDESDLPKL TYLKNVINET
     LRLYTPAPLL LPHSTSDECN IGGYKVPQDT IVLINAWAIH RDPELWTEAT TFKPERFEKK
     GELEKLIAFG MGRRACPGEG LAIRAISMTL ALLIQCFDWK LINGDKIDLA ERDGFTLTKL
     VPLKAMCKSR PVINKVFKQ