C93C2_GLYUR
ID C93C2_GLYUR Reviewed; 523 AA.
AC G4XV71; G4XV72;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=2-hydroxyisoflavanone synthase;
DE Short=2HI synthase;
DE EC=1.14.14.87 {ECO:0000250|UniProtKB:Q9SXS3};
DE AltName: Full=Cytochrome P450 93C2;
DE AltName: Full=Isoflavonoid synthase;
GN Name=CYP93C2; Synonyms=IFS1, IFS2;
OS Glycyrrhiza uralensis (Chinese licorice) (Glycyrrhiza shiheziensis).
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=74613;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang X.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 2-hydroxyisoflavanone synthase, which catalyzes the
CC hydroxylation associated with 1,2-aryl migration of flavanones.
CC Converts liquiritigenin and naringenin into highly unstable precursors
CC of the isoflavones daidzein and genistein.
CC {ECO:0000250|UniProtKB:Q9SXS3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=liquiritigenin + O2 + reduced [NADPH--hemoprotein reductase] =
CC (2R,3S)-2,4',7-trihydroxyisoflavanone + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:31723, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28777,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:63325;
CC EC=1.14.14.87; Evidence={ECO:0000250|UniProtKB:Q9SXS3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-naringenin + O2 + reduced [NADPH--hemoprotein reductase]
CC = 2-hydroxy-2,3-dihydrogenistein + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:35487, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17846, ChEBI:CHEBI:31080,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.87;
CC Evidence={ECO:0000250|UniProtKB:Q9SXS3};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; JF912327; AEQ39022.1; -; mRNA.
DR EMBL; JF912328; AEQ39023.1; -; mRNA.
DR AlphaFoldDB; G4XV71; -.
DR SMR; G4XV71; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0102668; F:liquiritigenin,NADPH:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102604; F:naringenin,NADPH:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; ISS:UniProtKB.
DR GO; GO:0009717; P:isoflavonoid biosynthetic process; ISS:UniProtKB.
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 Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; NADP; Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..523
FT /note="2-hydroxyisoflavanone synthase"
FT /id="PRO_0000419823"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 450
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 CONFLICT 108
FT /note="P -> S (in Ref. 1; AEQ39023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 59242 MW; 00A36B0F3B5E8AD0 CRC64;
MLVELAITLL VIALFIHLRP TPSAKSKSLR HLPNPPSPKP RLPFVGHLHL LDKPLLHNSL
IDLSKRYGPL YSLYFGSMPT VVVSTPELFK LFLQTHEASS FNTRFQTPAI RRLTYDNSVA
MVPFGPYWKF IRKLIMNDLL NATTVNKLRP LRSQEIRKVL RVMALSAESQ VPLNVTEELL
KWTNSTISRM MLGEAEEIRD IARDVLKIFG EYSLTDFIWP LKKLKVGQYE KRIDDIFNRF
DPVIERVIKK RQEIRKKRKE RNGEVEEGEQ SVVFLDTLLD FAEDETMEIK ITKEQIKGLV
VDFFSAGTDS TAVATEWALS ELINNPRVLQ KAREEVDAVV GKDRLVDEAD VQNLPYIRSI
VKETFRMHPP LPVVKRKCVQ ECEIDGYAIP EGALILFNVW AVGRDPKYWD RPTEFRPERF
LENVGEGDQA VDLRGQHFQL LPFGSGRRMC PGVNLATAGM ATLLASVIQC FDLSVVGPQG
KILKGNDAKV SMEESAGLTV PRAHNLVCVP VARSSAVPKL FSS
