C93G2_ORYSJ
ID C93G2_ORYSJ Reviewed; 518 AA.
AC Q5VRI5;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cytochrome P450 93G2 {ECO:0000303|PubMed:20647377};
DE EC=1.14.14.162 {ECO:0000269|PubMed:20647377};
DE AltName: Full=Flavanone 2-hydroxylase {ECO:0000303|PubMed:20647377};
DE Short=OsF2H {ECO:0000303|PubMed:20647377};
GN Name=CYP93G2 {ECO:0000303|PubMed:20647377};
GN OrderedLocusNames=Os06g0102100 {ECO:0000312|EMBL:BAF18447.1},
GN LOC_Os06g01250 {ECO:0000305};
GN ORFNames=OSJNBa0075G19.13 {ECO:0000312|EMBL:BAD67942.1};
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=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 [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20647377; DOI=10.1104/pp.110.161042;
RA Du Y., Chu H., Chu I.K., Lo C.;
RT "CYP93G2 is a flavanone 2-hydroxylase required for C-glycosylflavone
RT biosynthesis in rice.";
RL Plant Physiol. 154:324-333(2010).
CC -!- FUNCTION: Functions as flavanone 2-hydroxylase that catalyzes the
CC direct conversion of flavanones to 2-hydroxyflavanones
CC (PubMed:20647377). In vitro, can convert naringenin and eriodictyol to
CC the corresponding 2-hydroxyflavanones (PubMed:20647377). Generates 2-
CC hydroxyflavanone substrates for C-glycosylflavone biosynthesis by the
CC glycosyltransferase CGT (PubMed:20647377).
CC {ECO:0000269|PubMed:20647377}.
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:20647377};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57585;
CC Evidence={ECO:0000269|PubMed:20647377};
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:20647377};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57589;
CC Evidence={ECO:0000269|PubMed:20647377};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-eriodictyol + O2 + reduced [NADPH--hemoprotein reductase]
CC = (2S)-2-hydroxyeriodictyol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:57596, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:28412, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:141995;
CC Evidence={ECO:0000269|PubMed:20647377};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57597;
CC Evidence={ECO:0000269|PubMed:20647377};
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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AP002842; BAD67942.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18447.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS95702.1; -; Genomic_DNA.
DR EMBL; AK099468; BAG94143.1; -; mRNA.
DR EMBL; AK105993; BAG97488.1; -; mRNA.
DR RefSeq; XP_015642954.1; XM_015787468.1.
DR AlphaFoldDB; Q5VRI5; -.
DR SMR; Q5VRI5; -.
DR STRING; 4530.OS06T0102100-01; -.
DR PaxDb; Q5VRI5; -.
DR PRIDE; Q5VRI5; -.
DR EnsemblPlants; Os06t0102100-01; Os06t0102100-01; Os06g0102100.
DR GeneID; 4339836; -.
DR Gramene; Os06t0102100-01; Os06t0102100-01; Os06g0102100.
DR KEGG; osa:4339836; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q5VRI5; -.
DR OMA; NANMRMV; -.
DR OrthoDB; 702827at2759; -.
DR BioCyc; MetaCyc:MON-15865; -.
DR BRENDA; 1.14.14.162; 4460.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0102472; F:eriodictyol 2-hydroxylase activity; IEA:RHEA.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0102469; F:naringenin 2-hydroxylase activity; IEA:RHEA.
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: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; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..518
FT /note="Cytochrome P450 93G2"
FT /id="PRO_0000440769"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 453
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 518 AA; 56681 MW; 730FF16B52AE410E CRC64;
MEEGVVGGGG AAVLVALLVT VVLAVMRSAG SRSSKRGRLP PSPMALPIIG HLHLIRPPPH
RAFDRILARH GPLVYLRLGP STHCVVIGSA DVARDFLKFE ASIPERPPTA VTRQLAYGKA
GFAFAPYGAY WRFVKRLCMS ELLGPRTVEL LRPVRAAELA DVLRAAQSAA ERGEGVDMSH
ELVRMANNSI MRMVASALPG EMAEAARDCA KQVAELVGAF NAEDFVAVCR GWDLQGIGRR
TNEVHARFDA LLETIIEAKE EARRRSLRLG RRESSSKDLL DMLMDAAEDD TAEVKLTRDN
IKAFVLDIFT AGSDTTATTV EWMLAELVNH PECMAKLRGE LDAVVGRSRL VGEQDVARLP
YLQAVLKETL RLRPPAVFAQ RVTVEPVQVR GYTIPTDTQV FFNIFSIGRD ATYWDQPLHF
RPDRFLPDGA GATVDPKGQH PQLMPFGSGR RACPGMGLAM QAVPAFLAAL VQCFDWAPPP
SQPLPLDMEE AAGLVSARKH PLLLLPTPRI QPLPSFYS
