C9B16_SOYBN
ID C9B16_SOYBN Reviewed; 527 AA.
AC E9KBR8; D3U591;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Cytochrome P450 93B16 {ECO:0000305};
DE EC=1.14.19.76 {ECO:0000269|PubMed:20132953};
DE AltName: Full=Flavone synthase II {ECO:0000303|PubMed:20132953};
DE Short=GmFNSII {ECO:0000303|PubMed:20132953};
GN Name=CYP93B16 {ECO:0000303|PubMed:20132953};
GN Synonyms=FNSII-1 {ECO:0000312|EMBL:ADV35712.1};
GN ORFNames=GLYMA_12G067000 {ECO:0000312|EMBL:KRH24861.1};
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20132953; DOI=10.1016/j.phytochem.2010.01.007;
RA Fliegmann J., Furtwangler K., Malterer G., Cantarello C., Schuler G.,
RA Ebel J., Mithofer A.;
RT "Flavone synthase II (CYP93B16) from soybean (Glycine max L.).";
RL Phytochemistry 71:508-514(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Jiang Y.N., Li H., Yao L.M., Wu T.L., Wang B.;
RT "Isolation and characterization of two flavone synthase genes from soybean
RT (Glycine max) and their function in flavone and isoflavone accumulation.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
CC -!- FUNCTION: Functions as flavone synthase II (FNSII) that catalyzes the
CC direct conversion of flavanones to flavones (PubMed:20132953). In
CC vitro, can convert liquiritigenin, naringenin and eriodictyol to 7,4'-
CC dihydroxyflavone, apigenin and luteolin, respectively
CC (PubMed:20132953). {ECO:0000269|PubMed:20132953}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a flavanone + O2 + reduced [NADPH--hemoprotein reductase] = a
CC flavone + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:57680, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:24043, ChEBI:CHEBI:28863, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.19.76;
CC Evidence={ECO:0000269|PubMed:20132953};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57681;
CC Evidence={ECO:0000269|PubMed:20132953};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.2 uM for liquiritigenin {ECO:0000269|PubMed:20132953};
CC KM=2.5 uM for naringenin {ECO:0000269|PubMed:20132953};
CC KM=1.8 uM for eriodictyol {ECO:0000269|PubMed:20132953};
CC pH dependence:
CC Optimum pH is 7.9. {ECO:0000269|PubMed:20132953};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:20132953};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; FJ767774; ACV65037.1; -; mRNA.
DR EMBL; GU568027; ADV35712.1; -; mRNA.
DR EMBL; GU575289; ADV52251.1; -; Genomic_DNA.
DR EMBL; CM000845; KRH24861.1; -; Genomic_DNA.
DR RefSeq; NP_001241007.1; NM_001254078.1.
DR AlphaFoldDB; E9KBR8; -.
DR SMR; E9KBR8; -.
DR STRING; 3847.GLYMA12G07190.1; -.
DR PRIDE; E9KBR8; -.
DR EnsemblPlants; KRH24861; KRH24861; GLYMA_12G067000.
DR GeneID; 100783503; -.
DR Gramene; KRH24861; KRH24861; GLYMA_12G067000.
DR KEGG; gmx:100783503; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; E9KBR8; -.
DR OMA; NANMRMV; -.
DR OrthoDB; 702827at2759; -.
DR BRENDA; 1.14.19.76; 2483.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000008827; Chromosome 12.
DR ExpressionAtlas; E9KBR8; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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; IBA:GO_Central.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IDA:UniProtKB.
DR GO; GO:0051553; P:flavone biosynthetic process; IDA:UniProtKB.
DR GO; GO:0033511; P:luteolin 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 1: Evidence at protein level;
KW Flavonoid biosynthesis; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..527
FT /note="Cytochrome P450 93B16"
FT /id="PRO_0000451629"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 455
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"
FT CONFLICT 8
FT /note="L -> V (in Ref. 1; ACV65037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 59580 MW; BDEBD3EE933F7DFB CRC64;
MISESLLLVF LIVFISASLL KLLFVRENKP KAHLKNPPSP PAIPIIGHLH LLKPLIHHSF
RDLSLRYGPL LSLRIGSVKF IVASTPSLAQ EFLKTNELTY SSRKMNMAIN MVTYHNATFA
FAPYDTYWKF MKKLSTTELL GNKTLGHFLP IRTREVHDII QFLFHKSKAQ ESVNLTEALL
SLSNNVISQM MLSIKSSGTD SQAEQARTLV REVTQIFGEF NVSDFLGFCK NLDLQGFRKR
ALDIHKRYDA LLEKIISDRE ELRRKSKVDG CEDGDDEKVK DFLDILLDVA EQKECEVQLT
RNHVKSLILD YFTAATDTTA ISVEWTIAEL FNNPKVLKKA QEEVDRVTGN TQLVCEADIP
NLPYIHAIIK ETMRLHPPIP MIMRKGIEDC VVNGNMIPKG SIVCVNIWAM GRDPNIWKNP
LEFKPERFLE GEGSAIDTKG HHFELLPFGS GRRGCPGMPL AMRELPTIIG ALIQCFEWKM
LGSQGEILDH GRSLISMDER PGLTAPRAND LIGIPVARLN PTPFRQM
