C90A3_ORYSI
ID C90A3_ORYSI Reviewed; 501 AA.
AC B8BJ22;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Cytochrome P450 90A3 {ECO:0000250|UniProtKB:Q2RAP4};
DE Short=OsCYP90A3 {ECO:0000250|UniProtKB:Q2RAP4};
DE EC=1.14.99.- {ECO:0000250|UniProtKB:Q2RAP4};
GN Name=CYP90A3 {ECO:0000250|UniProtKB:Q2RAP4};
GN ORFNames=OsI_35071 {ECO:0000312|EMBL:EEC67657.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
CC -!- FUNCTION: Catalyzes the C23-alpha-hydroxylation step in brassinosteroid
CC biosynthesis (By similarity). Converts 6-deoxocathasterone (6-deoxoCT)
CC to 6-deoxoteasterone (6-deoxoTE) in the late C6-oxidation pathway and
CC cathasterone (CT) to teasterone (TE) in the early C6-oxidation pathway
CC of brassinolide (BL) biosynthesis (By similarity).
CC {ECO:0000250|UniProtKB:Q2RAP4}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC {ECO:0000250|UniProtKB:Q2RAP4}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000136; EEC67657.1; -; Genomic_DNA.
DR STRING; 39946.B8BJ22; -.
DR EnsemblPlants; BGIOSGA034516-TA; BGIOSGA034516-PA; BGIOSGA034516.
DR Gramene; BGIOSGA034516-TA; BGIOSGA034516-PA; BGIOSGA034516.
DR HOGENOM; CLU_001570_15_5_1; -.
DR OMA; KLWEVYM; -.
DR UniPathway; UPA00381; -.
DR Proteomes; UP000007015; Chromosome 11.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0080132; F:fatty acid alpha-hydroxylase activity; IEA:EnsemblPlants.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016132; P:brassinosteroid 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 3: Inferred from homology;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..501
FT /note="Cytochrome P450 90A3"
FT /id="PRO_0000455308"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 446
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 501 AA; 55735 MW; D0D4F07387057092 CRC64;
MAAAPVLLLA AAAAVVVVAM VLRWLLLLGG PAAGRLGKRA LMPPGSTGLP LIGETLRLIS
AYKTPNPEPF IDERVARHGG VFTTHVFGER TVFSADPAFN RLLLAAEGRA VHSSYPSSIA
TLLGARSLLL TRGAAHKRLH SLTLTRLGRP ASPPLLAHID RLVLATMRQW EPAATVRLMD
EAKKITFNLT VKQLVSIEPG PWTESLRREY VKLIDGFFSI PFPLANLLPF TTYGQALKAR
KKVADALREV IKKRMEEKAE NGGSIGDDEG KKEKKDMVEE LLEAEGGSFS EEEMVDFCLS
LLVAGYETTS VLMTLAVKFL TETPAALAEL KEEHANIRDM KGKKQPLEWS DYKSMPFTQC
VINETLRVGN IISGVFRRAN TDIHYKDYTI PKGCKIFASF RAVHLNNEHY ENARTFNPWR
WQINNKLQNA VGANIFTPFG GGPRLCPGYE LARVVVSIFL HHLVTRFSWE ETEEDRLVFF
PTTRTLKGYP INLRLLSESI C