C90B1_BRADI
ID C90B1_BRADI Reviewed; 507 AA.
AC I1H7R8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Cytochrome P450 90B1 {ECO:0000305};
DE Short=BdCYP90B1 {ECO:0000303|PubMed:32146811};
DE AltName: Full=(22S)-22-hydroxycampesterol synthase {ECO:0000303|PubMed:32146811};
DE EC=1.14.14.- {ECO:0000269|PubMed:32146811};
DE AltName: Full=6-deoxycathasterone synthase {ECO:0000303|PubMed:32146811};
DE EC=1.14.14.- {ECO:0000269|PubMed:32146811};
GN Name=CYP90B1 {ECO:0000303|PubMed:32146811};
GN OrderedLocusNames=BRADI_1g69040v3 {ECO:0000312|EMBL:KQK22730.1};
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 campesterol (CR) to (22S)-22-hydroxycampesterol (22-OHCR, 22-
CC hydroxyCR) and of campestanol (CN) to 6-deoxycathasterone (6-deoxoCT)
CC (PubMed:32146811). {ECO:0000269|PubMed:32146811}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=campesterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC (22S)-22-hydroxycampesterol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:69835, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:28623, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:72331;
CC Evidence={ECO:0000269|PubMed:32146811};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69836;
CC Evidence={ECO:0000269|PubMed:32146811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=campestanol + O2 + reduced [NADPH--hemoprotein reductase] = 6-
CC deoxycathasterone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:69831, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:20714, ChEBI:CHEBI:36799, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:32146811};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69832;
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; CM000880; KQK22730.1; -; Genomic_DNA.
DR RefSeq; XP_003558427.1; XM_003558379.3.
DR STRING; 15368.BRADI1G69040.1; -.
DR EnsemblPlants; KQK22730; KQK22730; BRADI_1g69040v3.
DR GeneID; 100837605; -.
DR Gramene; KQK22730; KQK22730; BRADI_1g69040v3.
DR KEGG; bdi:100837605; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; I1H7R8; -.
DR OMA; FHWKLAA; -.
DR OrthoDB; 574756at2759; -.
DR UniPathway; UPA00381; -.
DR Proteomes; UP000008810; Chromosome 1.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblPlants.
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; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0010012; F:steroid 22-alpha hydroxylase activity; IEA:EnsemblPlants.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IBA:GO_Central.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0010358; P:leaf shaping; IEA:EnsemblPlants.
DR GO; GO:0009741; P:response to brassinosteroid; IEA:EnsemblPlants.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; IEA:EnsemblPlants.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
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.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..507
FT /note="Cytochrome P450 90B1"
FT /id="PRO_0000455304"
FT TRANSMEM 12..32
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 507 AA; 57945 MW; D027D60B6DBE1A35 CRC64;
MAAMMASITS ELLFFLPYIL LALLTFYTTT VAKCHRWRRT EEKRRCPNLP PGAIGWPFIG
ETFGYLRAHP ATSVGRFMEE HIARYGKIYR SSLFGDRTVV SADAGLNRYI LQNEGKLFEC
SYPRSIGGIL GKWSMLVLVG DPHREMRAIS LNFLSSLRLR AVLLPEVERH TLLVLRHWPS
ASPAVFSAQH EAKKFTFNLM AKNIMSMDPG EEETERLRLE YITFMKGVVS APLNFPGTAY
WKALKSRATI LGVIERKMED RLQKMNKEDS SIEEDDLLGW AMKQSNLSKE QILDLLLSLL
FAGHETSSMA LALAIFFLEG CPKAVQELRE EHLEIARRQR LRGECKLSWE DYKDMVFTQC
VINETLRLGN VVRFLHRKVI RDVHYKGYDI PSGWKILPVL AAVHLDSSLY EDPSRFNPWR
WKGNASGVAQ SGNFMPYGGG TRLCAGSELA KLEMAIFLHH LVLNFRWELA EPDQAFVYPF
VDFPKGLPIR VHRIAQEEEK SVLTVDI
