C90D2_BRADI
ID C90D2_BRADI Reviewed; 510 AA.
AC I1HL09;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Cytochrome P450 90D2 {ECO:0000305};
DE Short=BdCYP90D2 {ECO:0000303|PubMed:32146811};
DE AltName: Full=3-dehydro-6-deoxoteasterone synthase {ECO:0000303|PubMed:32146811};
DE Short=6-deoxotyphasterol synthase {ECO:0000303|PubMed:32146811};
DE EC=1.14.14.147 {ECO:0000269|PubMed:32146811};
DE AltName: Full=6-deoxoteasterone synthase {ECO:0000303|PubMed:32146811};
DE EC=1.14.14.- {ECO:0000269|PubMed:32146811};
GN Name=CYP90D2 {ECO:0000303|PubMed:32146811};
GN OrderedLocusNames=BRADI_2g33050v3 {ECO:0000312|EMBL:KQK07095.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Bd21;
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=32146811; DOI=10.1021/acs.jafc.9b07963;
RA Roh J., Moon J., Youn J.-H., Seo C., Park Y.J., Kim S.-K.;
RT "Establishment of biosynthetic pathways to generate castasterone as the
RT biologically active brassinosteroid in Brachypodium distachyon.";
RL J. Agric. Food Chem. 68:3912-3923(2020).
CC -!- FUNCTION: Involved in reduction steps of the biosynthesis of plant
CC campesterol-derivative steroids, ending to castasterone (CS) but
CC missing brassinolide (BL) (PubMed:32146811). Catalyzes the conversion
CC of (22S,24R)-22-hydroxy-5alpha-ergostan-3-one (22-hydroxy-campesta-3-
CC one, 22-OH-3-one) to 3-dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo-
CC 3-DHT), 3-epi-6-deoxocathasterone (3-epi-6-deoxoCT) to 6-
CC deoxotyphasterol (6-deoxoTY) and of 6-deoxocathasterone (6-deoxoCT) to
CC 6-deoxoteasterone (6-deoxoTE) (PubMed:32146811).
CC {ECO:0000269|PubMed:32146811}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-epi-6-deoxocathasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 6-deoxotyphasterol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:27321, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:20717, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:59410; EC=1.14.14.147;
CC Evidence={ECO:0000269|PubMed:32146811};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27322;
CC Evidence={ECO:0000269|PubMed:32146811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(22S,24R)-22-hydroxy-5alpha-ergostan-3-one + O2 + reduced
CC [NADPH--hemoprotein reductase] = 3-dehydro-6-deoxoteasterone + H(+) +
CC H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:27325,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20710,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:59411;
CC EC=1.14.14.147; Evidence={ECO:0000269|PubMed:32146811};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27326;
CC Evidence={ECO:0000269|PubMed:32146811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxycathasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 6-deoxoteasterone + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:69811, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:20714, ChEBI:CHEBI:20716,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:32146811};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69812;
CC Evidence={ECO:0000269|PubMed:32146811};
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:32146811}.
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; CM000881; KQK07095.1; -; Genomic_DNA.
DR RefSeq; XP_003566445.1; XM_003566397.3.
DR STRING; 15368.BRADI2G33050.1; -.
DR EnsemblPlants; KQK07095; KQK07095; BRADI_2g33050v3.
DR GeneID; 100839691; -.
DR Gramene; KQK07095; KQK07095; BRADI_2g33050v3.
DR KEGG; bdi:100839691; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; I1HL09; -.
DR OMA; VFKSHLW; -.
DR OrthoDB; 871849at2759; -.
DR UniPathway; UPA00381; -.
DR Proteomes; UP000008810; Chromosome 2.
DR ExpressionAtlas; I1HL09; 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; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..510
FT /note="Cytochrome P450 90D2"
FT /id="PRO_0000455310"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 444
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 510 AA; 56818 MW; 3BA4FE5D70CA2CBF CRC64;
MEALSMVGSG GVYSWPAALL VAAIVVSASV RWWGIKRQPT TTESKARLPR GSLGWPVVGE
TLAFISAAYS AQPESFVDKR RLLYGKVFKS HLWGSKAVVS SDAEVSRAVL QADASAFVPW
YPSSLMQLMG ESSILVLGGG LQRRVHGLAG AFFKSPQLKA RLTVDMQRRV ADAMDAWQCH
GVVRVQDEAK SIVFEILVKA LIGLEPGQEM HYLKQQFREF IAGLISLPIK LPGTQLYRSI
QAKKRMAKLI QKIVQEKREK RMGGNNNATC KAPRDMIDVL MSNGSEELTD ELISDNMIDF
MIPAEDSVPV LITLAVKYLS ECPLALEQLE EENMELKKRK SAVGGTLEWT DYMSLAFTQH
VITETLRIGN IINGIMRKAV KDVEVKGQLL IPQGWCVFLY FRSVHLDGHI YDDPYAFNPW
RWKERDMMAA SSGFTPFGGG QRLCPGVDLA RLEASIFLHH LVTTFRWEAE DDTVVTFPTV
RLKRGMPIRV SQNIETSGTA TFRSTESASV
