C75B4_ORYSJ
ID C75B4_ORYSJ Reviewed; 535 AA.
AC Q8LM92;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Flavonoid 3'-monooxygenase CYP75B4 {ECO:0000305};
DE EC=1.14.14.82 {ECO:0000269|PubMed:26082402};
DE AltName: Full=Chrysoeriol 5'-hydroxylase {ECO:0000303|PubMed:26082402};
DE AltName: Full=Cytochrome P450 75B4 {ECO:0000303|PubMed:26082402};
DE AltName: Full=Flavonoid 3'-hydroxylase CYP75B4 {ECO:0000303|PubMed:26082402};
GN Name=CYP75B4 {ECO:0000303|PubMed:26082402};
GN OrderedLocusNames=Os10g0317900 {ECO:0000312|EMBL:BAF26247.1},
GN LOC_Os10g16974 {ECO:0000312|EMBL:ABG66003.1}; ORFNames=OSJNBb0079E01.10;
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=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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 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 [6]
RP FUNCTION.
RX PubMed=26082402; DOI=10.1104/pp.15.00566;
RA Lam P.Y., Liu H., Lo C.;
RT "Completion of tricin biosynthesis pathway in rice: cytochrome P450 75B4 is
RT a unique chrysoeriol 5'-hydroxylase.";
RL Plant Physiol. 168:1527-1536(2015).
CC -!- FUNCTION: Catalyzes the 3'-hydroxylation of the flavonoid B-ring to the
CC 3',4'-hydroxylated state. Catalyzes in vitro 3'-hydroxylation of
CC different flavonoids. Catalyzes the conversion of apigenin to luteolin,
CC naringenin to eriodictyol, and kaempferol to quercetin. Possesses
CC specific 5'-hydroxylase activity toward chrysoeriol (a 3'-methoxylated
CC flavone) and is indispensable for tricin formation. Converts
CC chrysoeriol to selgin, a precursor of tricin, suggesting that
CC chrysoeriol, instead of tricetin, is an intermediate in tricin
CC biosynthesis. {ECO:0000269|PubMed:26082402}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-unsubstituted flavone + O2 + reduced [NADPH--hemoprotein
CC reductase] = a 3'-hydroxyflavone + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:16337, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27741, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:138726; EC=1.14.14.82;
CC Evidence={ECO:0000269|PubMed:26082402};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AC119149; AAM74394.1; -; Genomic_DNA.
DR EMBL; DP000086; ABG66003.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF26247.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT10298.1; -; Genomic_DNA.
DR EMBL; AK070442; BAG91954.1; -; mRNA.
DR RefSeq; XP_015612714.1; XM_015757228.1.
DR AlphaFoldDB; Q8LM92; -.
DR SMR; Q8LM92; -.
DR STRING; 4530.OS10T0317900-01; -.
DR CarbonylDB; Q8LM92; -.
DR PaxDb; Q8LM92; -.
DR PRIDE; Q8LM92; -.
DR EnsemblPlants; Os10t0317900-01; Os10t0317900-01; Os10g0317900.
DR GeneID; 4348299; -.
DR Gramene; Os10t0317900-01; Os10t0317900-01; Os10g0317900.
DR KEGG; osa:4348299; -.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; Q8LM92; -.
DR OMA; TSGRPTM; -.
DR OrthoDB; 702827at2759; -.
DR BioCyc; MetaCyc:MON-20525; -.
DR BRENDA; 1.14.14.82; 8948.
DR PlantReactome; R-OSA-1119322; Leucodelphinidin biosynthesis.
DR PlantReactome; R-OSA-1119415; Leucopelargonidin and leucocyanidin biosynthesis.
DR PlantReactome; R-OSA-9609573; Tricin biosynthesis.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR ExpressionAtlas; Q8LM92; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016711; F:flavonoid 3'-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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 2: Evidence at transcript level;
KW Flavonoid biosynthesis; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..535
FT /note="Flavonoid 3'-monooxygenase CYP75B4"
FT /id="PRO_0000440771"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 469
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:P04798"
SQ SEQUENCE 535 AA; 58519 MW; 9AB17D2B9A86B6F1 CRC64;
MEVAAMEIST SLLLTTVALS VIVCYALVFS RAGKARAPLP LPPGPRGWPV LGNLPQLGGK
THQTLHEMTK VYGPLIRLRF GSSDVVVAGS APVAAQFLRT HDANFSSRPR NSGGEHMAYN
GRDVVFGPYG PRWRAMRKIC AVNLFSARAL DDLRAFRERE AVLMVRSLAE ASAAPGSSSP
AAVVLGKEVN VCTTNALSRA AVGRRVFAAG AGEGAREFKE IVLEVMEVGG VLNVGDFVPA
LRWLDPQGVV ARMKKLHRRF DDMMNAIIAE RRAGSLLKPT DSREEGKDLL GLLLAMVQEQ
EWLAAGEDDR ITDTEIKALI LNLFVAGTDT TSTIVEWTMA ELIRHPDILK HAQEELDVVV
GRDRLLSESD LSHLTFFHAI IKETFRLHPS TPLSLPRMAS EECEIAGYRI PKGAELLVNV
WGIARDPAIW PDPLEYKPSR FLPGGTHTDV DVKGNDFGLI PFGAGRRICA GLSWGLRMVT
MTAATLVHAF DWQLPADQTP DKLNMDEAFT LLLQRAEPLV VHPVPRLLPS AYNIA
