ID   C90A4_ORYSI             Reviewed;         501 AA.
AC   A2ZHX7;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Cytochrome P450 90A4 {ECO:0000250|UniProtKB:Q5CCK1};
DE            Short=OsCYP90A4 {ECO:0000250|UniProtKB:Q5CCK1};
DE            EC=1.14.99.- {ECO:0000250|UniProtKB:Q5CCK1};
GN   Name=CYP90A4 {ECO:0000250|UniProtKB:Q5CCK1};
GN   ORFNames=OsI_37414 {ECO:0000312|EMBL:EAY82211.1};
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 to 6-
CC       deoxoteasterone in the late C6-oxidation pathway and cathasterone to
CC       teasterone (TE) in the early C6-oxidation pathway of brassinolide (BL)
CC       biosynthesis (By similarity). {ECO:0000250|UniProtKB:P04798}.
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:P04798}.
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; CM000137; EAY82211.1; -; Genomic_DNA.
DR   STRING; 39946.A2ZHX7; -.
DR   EnsemblPlants; BGIOSGA036662-TA; BGIOSGA036662-PA; BGIOSGA036662.
DR   Gramene; BGIOSGA036662-TA; BGIOSGA036662-PA; BGIOSGA036662.
DR   HOGENOM; CLU_001570_15_5_1; -.
DR   OMA; IEPCEWT; -.
DR   UniPathway; UPA00381; -.
DR   Proteomes; UP000007015; Chromosome 12.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 90A4"
FT                   /id="PRO_0000455309"
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;  55641 MW;  C6C7CA6BD36710D8 CRC64;
     MAAAALLLLA AAAAAVVVAM ALRWLLLLGG PAAGRQGKRA RMPPGSTGLP LIGETLRLIS
     AYKTPNPEPF IDERVARHGG VFTTHVFGER TVFSADPAFN RLLLAAEGRA VHSSYPSSIA
     TLLGARSLLL TRGAAHKRLH SLTLTRLGRP ASPPLLAHID RLVLATMRQW EPAATVRLMD
     EAKKITFNLT VKQLVSIEPG PWTESLRREY VKLIDGFFSI PFPLACLLPF TTYGQALKAR
     KKVAGALREV IKKRMEEKAE NGGSIGDDEG KKEKKDMVEE LLQAEGGSFS EEEMVDFCLS
     LLVAGYETTS VLMTLAVKFL TETPAALAEL KEEHANIRDM KGKNQPLEWS DYKSMPFTQC
     VINETLRVGN IISGVFRRAN TDIHYKDYTI PKGCKIFASF RAVHLNNEHY ENARTFNPWR
     WQINNKLQNA VGANIFTPFG GGPRLCPGYE LARVVVSIFL HHLVTRFSWE ETEEDRLVFF
     PTTRTLKGYP INLRLLSESI C