C90D2_ORYSJ
ID C90D2_ORYSJ Reviewed; 490 AA.
AC Q94IW5; Q0JPW7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cytochrome P450 90D2 {ECO:0000303|PubMed:14615594};
DE Short=OsCYP90D2 {ECO:0000303|PubMed:14615594};
DE AltName: Full=3-dehydro-6-deoxoteasterone synthase {ECO:0000303|PubMed:14615594};
DE EC=1.14.19.- {ECO:0000269|PubMed:14615594};
DE AltName: Full=3-dehydroteasterone synthase {ECO:0000303|PubMed:14615594};
DE EC=1.14.19.- {ECO:0000269|PubMed:14615594};
DE AltName: Full=C6-oxidase {ECO:0000303|PubMed:14615594};
GN Name=CYP90D2 {ECO:0000303|PubMed:14615594};
GN Synonyms=D2 {ECO:0000303|PubMed:14615594};
GN OrderedLocusNames=Os01g0197100 {ECO:0000305}, LOC_Os01g10040 {ECO:0000305};
GN ORFNames=P0419B01.11 {ECO:0000312|EMBL:BAS70868.1};
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(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 FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, INDUCTION,
RP MUTAGENESIS OF PRO-305, AND DISRUPTION PHENOTYPE.
RX PubMed=14615594; DOI=10.1105/tpc.014712;
RA Hong Z., Ueguchi-Tanaka M., Umemura K., Uozu S., Fujioka S., Takatsuto S.,
RA Yoshida S., Ashikari M., Kitano H., Matsuoka M.;
RT "A rice brassinosteroid-deficient mutant, ebisu dwarf (d2), is caused by a
RT loss of function of a new member of cytochrome P450.";
RL Plant Cell 15:2900-2910(2003).
CC -!- FUNCTION: Catalyzes the C6-oxidation step in brassinosteroids
CC biosynthesis (PubMed:14615594). May convert 6-deoxoteasterone (6-
CC deoxoTE) to 3-dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo3DHT), and
CC teasterone (TE) to 3-dehydroteasterone (3DT, 3-DHT) (PubMed:14615594).
CC Involved in the elongation of leaf sheaths and stems (PubMed:14615594).
CC {ECO:0000269|PubMed:14615594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxoteasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 3-dehydro-6-deoxoteasterone + H(+) + 2 H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69983, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20710,
CC ChEBI:CHEBI:20716, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:14615594};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69984;
CC Evidence={ECO:0000269|PubMed:14615594};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC {ECO:0000269|PubMed:14615594}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels leaf blades, shoot apex and
CC elongating stem. {ECO:0000269|PubMed:14615594}.
CC -!- INDUCTION: Down-regulated by brassinolide (BL) in ebisu dwarf (d2)
CC mutant. {ECO:0000269|PubMed:14615594}.
CC -!- DISRUPTION PHENOTYPE: Plants show abnormalities in growth: inhibition
CC of second internode elongation, shortened leaf sheaths, erect leaves,
CC and deficiency in skotomorphogenesis. Treatment with exogenous
CC brassinolide (BL) rescues the abnormal phenotype.
CC {ECO:0000269|PubMed:14615594}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AP003244; BAB56089.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04211.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS70868.1; -; Genomic_DNA.
DR RefSeq; XP_015611433.1; XM_015755947.1.
DR AlphaFoldDB; Q94IW5; -.
DR SMR; Q94IW5; -.
DR STRING; 4530.OS01T0197100-00; -.
DR PaxDb; Q94IW5; -.
DR PRIDE; Q94IW5; -.
DR EnsemblPlants; Os01t0197100-01; Os01t0197100-01; Os01g0197100.
DR GeneID; 4327329; -.
DR Gramene; Os01t0197100-01; Os01t0197100-01; Os01g0197100.
DR KEGG; osa:4327329; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q94IW5; -.
DR OMA; DANHHES; -.
DR OrthoDB; 871849at2759; -.
DR PlantReactome; R-OSA-1119456; Brassinosteroid biosynthesis II.
DR UniPathway; UPA00381; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; Q94IW5; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IBA:GO_Central.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
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 SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Brassinosteroid biosynthesis; Heme; Iron; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..490
FT /note="Cytochrome P450 90D2"
FT /id="PRO_0000052187"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 437
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"
FT MUTAGEN 305
FT /note="P->S: In d2-2; dwarf and defective in
FT brassinosteroid biosynthesis."
FT /evidence="ECO:0000269|PubMed:14615594"
SQ SEQUENCE 490 AA; 54825 MW; 9EC2853BBAFBB88F CRC64;
MVSAAAGWAA PAFAVAAVVI WVVLCSELLR RRRRGAGSGK GDAAAAARLP PGSFGWPVVG
ETLEFVSCAY SPRPEAFVDK RRKLHGSAVF RSHLFGSATV VTADAEVSRF VLQSDARAFV
PWYPRSLTEL MGKSSILLIN GALQRRVHGL VGAFFKSSHL KSQLTADMRR RLSPALSSFP
DSSLLHVQHL AKSVVFEILV RGLIGLEAGE EMQQLKQQFQ EFIVGLMSLP IKLPGTRLYR
SLQAKKKMAR LIQRIIREKR ARRAAASPPR DAIDVLIGDG SDELTDELIS DNMIDLMIPA
EDSVPVLITL AVKFLSECPL ALHQLEEENI QLKRRKTDMG ETLQWTDYMS LSFTQHVITE
TLRLGNIIGG IMRKAVRDVE VKGHLIPKGW CVFVYFRSVH LDDTLYDEPY KFNPWRWKEK
DMSNGSFTPF GGGQRLCPGL DLARLEASIF LHHLVTSFRW VAEEDHIVNF PTVRLKRGMP
IRVTAKEDDD
