C93C1_SOYBN
ID C93C1_SOYBN Reviewed; 521 AA.
AC Q9SWR5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=2-hydroxyisoflavanone synthase;
DE EC=1.14.14.87 {ECO:0000250|UniProtKB:Q9SXS3};
DE AltName: Full=Cytochrome P450 93C1v2;
DE AltName: Full=Isoflavone synthase 2;
GN Name=IFS2; Synonyms=CYP93C1v2;
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], AND FUNCTION.
RX PubMed=10375412; DOI=10.1006/abbi.1999.1238;
RA Steele C.L., Gijzen M., Qutob D., Dixon R.A.;
RT "Molecular characterization of the enzyme catalyzing the aryl migration
RT reaction of isoflavonoid biosynthesis in soybean.";
RL Arch. Biochem. Biophys. 367:146-150(1999).
CC -!- FUNCTION: Involved in isoflavonoid biosynthesis. Converts
CC liquiritigenin to 2-hydroxyisoflavanone which spontaneously dehydrates
CC to daidzein. {ECO:0000269|PubMed:10375412}.
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: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}. Microsome membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF135484; AAD38929.1; -; mRNA.
DR RefSeq; NP_001238515.1; NM_001251586.1.
DR AlphaFoldDB; Q9SWR5; -.
DR SMR; Q9SWR5; -.
DR STRING; 3847.GLYMA13G24200.1; -.
DR EnsemblPlants; KRH20368; KRH20368; GLYMA_13G173500.
DR GeneID; 606705; -.
DR Gramene; KRH20368; KRH20368; GLYMA_13G173500.
DR KEGG; gmx:606705; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q9SWR5; -.
DR OrthoDB; 702827at2759; -.
DR BRENDA; 1.14.14.87; 2483.
DR Proteomes; UP000008827; Chromosome 13.
DR Genevisible; Q9SWR5; GM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; IDA: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; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..521
FT /note="2-hydroxyisoflavanone synthase"
FT /id="PRO_0000395198"
FT TRANSMEM 2..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 449
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 521 AA; 58869 MW; 29608940197120AB CRC64;
MLLELALGLL VLALFLHLRP TPTAKSKALR HLPNPPSPKP RLPFIGHLHL LKDKLLHYAL
IDLSKKHGPL FSLYFGSMPT VVASTPELFK LFLQTHEATS FNTRFQTSAI RRLTYDSSVA
MVPFGPYWKF VRKLIMNDLL NATTVNKLRP LRTQQIRKFL RVMAQGAEAQ KPLDLTEELL
KWTNSTISMM MLGEAEEIRD IAREVLKIFG EYSLTDFIWP LKHLKVGKYE KRIDDILNKF
DPVVERVIKK RREIVRRRKN GEVVEGEVSG VFLDTLLEFA EDETMEIKIT KDHIKGLVVD
FFSAGTDSTA VATEWALAEL INNPKVLEKA REEVYSVVGK DRLVDEVDTQ NLPYIRAIVK
ETFRMHPPLP VVKRKCTEEC EINGYVIPEG ALILFNVWQV GRDPKYWDRP SEFRPERFLE
TGAEGEAGPL DLRGQHFQLL PFGSGRRMCP GVNLATSGMA TLLASLIQCF DLQVLGPQGQ
ILKGGDAKVS MEERAGLTVP RAHSLVCVPL ARIGVASKLL S
