C93B1_GLYEC
ID C93B1_GLYEC Reviewed; 523 AA.
AC P93149;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Licodione synthase {ECO:0000303|PubMed:9708921};
DE EC=1.14.14.140 {ECO:0000269|PubMed:9708921};
DE AltName: Full=(2S)-flavanone 2-hydroxylase {ECO:0000303|PubMed:9708921};
DE EC=1.14.14.162 {ECO:0000269|PubMed:9708921};
DE AltName: Full=CYP GE-5 {ECO:0000312|EMBL:BAA22423.1};
DE AltName: Full=Cytochrome P450 93B1 {ECO:0000305};
DE AltName: Full=Flavone synthase II {ECO:0000303|PubMed:9708921};
GN Name=CYP93B1 {ECO:0000303|PubMed:9708921};
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=9708921; DOI=10.1016/s0014-5793(98)00781-9;
RA Akashi T., Aoki T., Ayabe S.;
RT "Identification of a cytochrome P450 cDNA encoding (2S)-flavanone 2-
RT hydroxylase of licorice (Glycyrrhiza echinata L. Fabaceae) which represents
RT licodione synthase and flavone synthase II.";
RL FEBS Lett. 431:287-290(1998).
CC -!- FUNCTION: Catalyzes the formation of licodione and 2-hydroxynaringenin
CC from (2S)-liquiritigenin and (2S)-naringenin, respectively
CC (PubMed:9708921). Can also convert eriodictyol to luteolin
CC (PubMed:9708921). {ECO:0000269|PubMed:9708921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=liquiritigenin + O2 + reduced [NADPH--hemoprotein reductase] =
CC 2 H(+) + H2O + licodione + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:15697, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28777, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:77711; EC=1.14.14.140;
CC Evidence={ECO:0000269|PubMed:9708921};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15698;
CC Evidence={ECO:0000269|PubMed:9708921};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a flavanone + O2 + reduced [NADPH--hemoprotein reductase] = a
CC 2-hydroxyflavanone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:57584, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28863, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:141992; EC=1.14.14.162;
CC Evidence={ECO:0000269|PubMed:9708921};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57585;
CC Evidence={ECO:0000269|PubMed:9708921};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-naringenin + O2 + reduced [NADPH--hemoprotein reductase]
CC = (2S)-2-hydroxynaringenin + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:57588, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17846, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:141994;
CC Evidence={ECO:0000269|PubMed:9708921};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57589;
CC Evidence={ECO:0000269|PubMed:9708921};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: By fungal elicitor.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB001380; BAA22423.1; -; mRNA.
DR AlphaFoldDB; P93149; -.
DR SMR; P93149; -.
DR KEGG; ag:BAA22423; -.
DR BRENDA; 1.14.14.162; 2486.
DR UniPathway; UPA00154; -.
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:0033771; F:licodione synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102469; F:naringenin 2-hydroxylase activity; IEA:RHEA.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
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 Flavonoid biosynthesis; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..523
FT /note="Licodione synthase"
FT /id="PRO_0000052191"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 448
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:Q94IP1"
SQ SEQUENCE 523 AA; 59496 MW; 4A776E6C432F527C CRC64;
MEPQLVAVSV LVSALICYFF FRPYFHRYGK NLPPSPFFRL PIIGHMHMLG PLLHQSFHNL
SHRYGPLFSL NFGSVLCVVA STPHFAKQLL QTNELAFNCR IESTAVKKLT YESSLAFAPY
GDYWRFIKKL SMNELLGSRS INNFQHLRAQ ETHQLLRLLS NRARAFEAVN ITEELLKLTN
NVISIMMVGE AEEARDVVRD VTEIFGEFNV SDFIWLFKKM DLQGFGKRIE DLFQRFDTLV
ERIISKREQT RKDRRRNGKK GEQGSGDGIR DFLDILLDCT EDENSEIKIQ RVHIKALIMD
FFTAGTDTTA ISTEWALVEL VKKPSVLQKV REEIDNVVGK DRLVEESDCP NLPYLQAILK
ETFRLHPPVP MVTRRCVAEC TVENYVIPED SLLFVNVWSI GRNPKFWDNP LEFRPERFLK
LEGDSSGVVD VRGSHFQLLP FGSGRRMCPG VSLAMQEVPA LLGAIIQCFD FHVVGPKGEI
LKGDDIVINV DERPGLTAPR AHNLVCVPVD RTSGGGPLKI IEC
