C93G1_ORYSJ
ID C93G1_ORYSJ Reviewed; 516 AA.
AC Q0JFI2; Q7XTC1;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cytochrome P450 93G1 {ECO:0000303|PubMed:24843076};
DE EC=1.14.19.76 {ECO:0000269|PubMed:24843076};
DE AltName: Full=Flavone synthase II {ECO:0000303|PubMed:24843076};
DE Short=OsFNSII {ECO:0000303|PubMed:24843076};
GN Name=CYP93G1 {ECO:0000303|PubMed:24843076};
GN OrderedLocusNames=Os04g0101400 {ECO:0000312|EMBL:BAF13905.1},
GN LOC_Os04g01140 {ECO:0000305};
GN ORFNames=B1160F02.15 {ECO:0000312|EMBL:CAE75984.1},
GN OsJ_13492 {ECO:0000312|EMBL:EAZ29419.1},
GN OSJNBa0068L06.2 {ECO:0000312|EMBL:CAE01576.2};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24843076; DOI=10.1104/pp.114.239723;
RA Lam P.Y., Zhu F.Y., Chan W.L., Liu H., Lo C.;
RT "Cytochrome P450 93G1 is a flavone synthase II that channels flavanones to
RT the biosynthesis of tricin O-linked conjugates in rice.";
RL Plant Physiol. 165:1315-1327(2014).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28385728; DOI=10.1104/pp.16.01973;
RA Lam P.Y., Tobimatsu Y., Takeda Y., Suzuki S., Yamamura M., Umezawa T.,
RA Lo C.;
RT "Disrupting flavone synthase II alters lignin and improves biomass
RT digestibility.";
RL Plant Physiol. 174:972-985(2017).
CC -!- FUNCTION: Functions as flavone synthase II (FNSII) that catalyzes the
CC direct conversion of flavanones to flavones (PubMed:24843076). In
CC vitro, can convert naringenin and eriodictyol to apigenin and luteolin,
CC respectively (PubMed:24843076). Acts as a key branch point enzyme that
CC channels flavanones to the biosynthesis of soluble tricin O-linked
CC conjugates (PubMed:24843076, PubMed:28385728).
CC {ECO:0000269|PubMed:24843076, ECO:0000269|PubMed:28385728}.
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:24843076};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57681;
CC Evidence={ECO:0000269|PubMed:24843076};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 uM for naringenin {ECO:0000269|PubMed:24843076};
CC KM=1.5 uM for eriodictyol {ECO:0000269|PubMed:24843076};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction in plant height
CC (PubMed:28385728). In cell wall, altered content and composition of
CC lignins derived from typical monolignols (PubMed:28385728).
CC {ECO:0000269|PubMed:28385728}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE01576.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAE75984.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAZ29419.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL606442; CAE01576.2; ALT_INIT; Genomic_DNA.
DR EMBL; BX842604; CAE75984.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008210; BAF13905.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS87506.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ29419.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK100972; BAG94859.1; -; mRNA.
DR RefSeq; XP_015636893.1; XM_015781407.1.
DR AlphaFoldDB; Q0JFI2; -.
DR SMR; Q0JFI2; -.
DR STRING; 4530.OS04T0101400-01; -.
DR PaxDb; Q0JFI2; -.
DR PRIDE; Q0JFI2; -.
DR EnsemblPlants; Os04t0101400-01; Os04t0101400-01; Os04g0101400.
DR GeneID; 4334886; -.
DR Gramene; Os04t0101400-01; Os04t0101400-01; Os04g0101400.
DR KEGG; osa:4334886; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q0JFI2; -.
DR OMA; TSIIRMA; -.
DR OrthoDB; 702827at2759; -.
DR BioCyc; MetaCyc:MON-20524; -.
DR BRENDA; 1.14.19.76; 4460.
DR PlantReactome; R-OSA-9609573; Tricin biosynthesis.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
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..516
FT /note="Cytochrome P450 93G1"
FT /id="PRO_0000440768"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 454
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 516 AA; 57110 MW; A87B536B62C0DD01 CRC64;
MASLMEVQVP LLGMGTTMGA LALALVVVVV VHVAVNAFGR RRLPPSPASL PVIGHLHLLR
PPVHRTFHEL AARLGPLMHV RLGSTHCVVA SSAEVAAELI RSHEAKISER PLTAVARQFA
YESAGFAFAP YSPHWRFMKR LCMSELLGPR TVEQLRPVRR AGLVSLLRHV LSQPEAEAVD
LTRELIRMSN TSIIRMAAST VPSSVTEEAQ ELVKVVAELV GAFNADDYIA LCRGWDLQGL
GRRAADVHKR FDALLEEMIR HKEEARMRKK TDTDVGSKDL LDILLDKAED GAAEVKLTRD
NIKAFIIDVV TAGSDTSAAM VEWMVAELMN HPEALRKVRE EIEAVVGRDR IAGEGDLPRL
PYLQAAYKET LRLRPAAPIA HRQSTEEIQI RGFRVPAQTA VFINVWAIGR DPAYWEEPLE
FRPERFLAGG GGEGVEPRGQ HFQFMPFGSG RRGCPGMGLA LQSVPAVVAA LLQCFDWQCM
DNKLIDMEEA DGLVCARKHR LLLHAHPRLH PFPPLL
