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C90A1_BRADI
ID   C90A1_BRADI             Reviewed;         498 AA.
AC   I1IUJ6;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Cytochrome P450 90A1 {ECO:0000305};
DE            Short=BdCYP90A1 {ECO:0000303|PubMed:32146811};
DE   AltName: Full=(22S,24R)-22-hydroxyergost-4-en-3-one synthase {ECO:0000303|PubMed:32146811};
DE            EC=1.14.19.- {ECO:0000269|PubMed:32146811};
DE   AltName: Full=3-dehydro-6-deoxoteasterone synthase {ECO:0000303|PubMed:32146811};
DE            EC=1.14.19.- {ECO:0000269|PubMed:32146811};
GN   Name=CYP90A1 {ECO:0000312|EnsemblPlants:KQJ92356};
GN   OrderedLocusNames=BRADI_4g43110v3 {ECO:0000312|EMBL:KQJ92356.1};
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)-22-hydroxycampesterol (22-hydroxyCR, 22-OHCR) to (22S,24R)-22-
CC       hydroxyergost-4-en-3-one (22-hydroxy-campesta-4-en-3-one, 22-OH-4-en-3-
CC       one) and of 6-deoxoteasterone (6-deoxoTE) to 3-dehydro-6-
CC       deoxoteasterone (6-deoxo3DT, 6-deoxo3DHT) (PubMed:32146811).
CC       {ECO:0000269|PubMed:32146811}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(22S)-22-hydroxycampesterol + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (22S)-22-hydroxycampest-4-en-3-one + H(+) + 2 H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69971,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:72330, ChEBI:CHEBI:72331;
CC         Evidence={ECO:0000269|PubMed:32146811};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69972;
CC         Evidence={ECO:0000269|PubMed:32146811};
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:32146811};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69984;
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; CM000883; KQJ92356.1; -; Genomic_DNA.
DR   RefSeq; XP_010238746.1; XM_010240444.2.
DR   STRING; 15368.BRADI4G43110.1; -.
DR   EnsemblPlants; KQJ92356; KQJ92356; BRADI_4g43110v3.
DR   GeneID; 100831598; -.
DR   Gramene; KQJ92356; KQJ92356; BRADI_4g43110v3.
DR   KEGG; bdi:100831598; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_15_5_1; -.
DR   InParanoid; I1IUJ6; -.
DR   OMA; KLWEVYM; -.
DR   OrthoDB; 1247045at2759; -.
DR   UniPathway; UPA00381; -.
DR   Proteomes; UP000008810; Chromosome 4.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0048657; P:anther wall tapetum cell differentiation; 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:0010584; P:pollen exine formation; IEA:EnsemblPlants.
DR   GO; GO:0009911; P:positive regulation of flower development; IEA:EnsemblPlants.
DR   GO; GO:0010224; P:response to UV-B; IEA:EnsemblPlants.
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   PRINTS; PR00385; P450.
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..498
FT                   /note="Cytochrome P450 90A1"
FT                   /id="PRO_0000455306"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          257..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         447
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   498 AA;  55778 MW;  EE47942BE1266032 CRC64;
     MENAGALQLL SAAAAAVAVV VVVALRWLLA RRAAGGWKQR PRLPPGSTGL PLIGETLRLI
     SAYKTPDPEP FIDERVARHG GVFTTHVFGE RTVFSADPAF NRLLLAAEGR AVDCSYPSSI
     TTLLGARSLL LTRGAAHKRL HSLTLTRLGR PASPPLLAHI DRLVLDTMRH WEPAATVRLL
     DEAKKITFNL TVKQLVSIDP GPWTESLRRE YVKLIDGFFS IPFPFASLLP FTTYGQALKS
     RKKVAGALRE VIRKRMEERG EESGATEEAE SKREKKDMVE ELLQAEGGSF SEEEMVDFCL
     SLLVAGYETT SVLMTVAVKF LTETPAALAQ LKEEHENMTN MKGENQPLEW SDYKSMTFTQ
     CVINETLRVA NIISGVFRRA NTDIHFKGYT IPKGCKIFAS FRAVHLNNDH YENARTFDPW
     RWQSNHKLQN EVGANLFTPF GGGPRLCPGY ELARVVISVF LHHLVMRFSW EAAEEDRLVF
     FPTTRTLKGY PINLRQRS
 
 
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