C90A1_ARATH
ID C90A1_ARATH Reviewed; 472 AA.
AC Q42569;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cytochrome P450 90A1 {ECO:0000303|PubMed:8612270};
DE Short=AtCYP90A1 {ECO:0000303|PubMed:8612270};
DE AltName: Full=(22R,23R)-22,23-dihydroxy-campest-4-en-3-one synthase {ECO:0000303|PubMed:22822057};
DE EC=1.14.19.- {ECO:0000269|PubMed:22822057};
DE AltName: Full=(22S,24R)-22-hydroxy-5alpha-ergostan-3-one synthase {ECO:0000303|PubMed:22822057};
DE EC=1.14.19.- {ECO:0000269|PubMed:22822057};
DE AltName: Full=(22S,24R)-22-hydroxyergost-4-en-3-one synthase {ECO:0000303|PubMed:22822057};
DE EC=1.14.19.- {ECO:0000269|PubMed:22822057};
DE AltName: Full=3-dehydro-6-deoxoteasterone synthase {ECO:0000303|PubMed:22822057};
DE EC=1.14.19.- {ECO:0000269|PubMed:22822057};
DE AltName: Full=Protein CONSTITUTIVE PHOTOMORPHOGENESIS AND DWARFISM {ECO:0000303|PubMed:22822057, ECO:0000303|PubMed:8612270};
GN Name=CYP90A1 {ECO:0000303|PubMed:8612270};
GN Synonyms=CPD {ECO:0000303|PubMed:22822057, ECO:0000303|PubMed:8612270},
GN CYP90 {ECO:0000303|PubMed:8612270};
GN OrderedLocusNames=At5g05690 {ECO:0000312|Araport:AT5G05690};
GN ORFNames=MJJ3.9 {ECO:0000312|EMBL:BAB09663.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8612270; DOI=10.1016/s0092-8674(00)81094-6;
RA Szekeres M., Nemeth K., Koncz-Kalman Z., Mathur J., Kauschmann A.,
RA Altmann T., Redei G.P., Nagy F., Schell J., Koncz C.;
RT "Brassinosteroids rescue the deficiency of CYP90, a cytochrome P450,
RT controlling cell elongation and de-etiolation in Arabidopsis.";
RL Cell 85:171-182(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=22822057; DOI=10.1074/jbc.m112.392720;
RA Ohnishi T., Godza B., Watanabe B., Fujioka S., Hategan L., Ide K.,
RA Shibata K., Yokota T., Szekeres M., Mizutani M.;
RT "CYP90A1/CPD, a brassinosteroid biosynthetic cytochrome P450 of
RT Arabidopsis, catalyzes C-3 oxidation.";
RL J. Biol. Chem. 287:31551-31560(2012).
CC -!- FUNCTION: Catalyzes C3-oxidation steps in brassinosteroids biosynthesis
CC (PubMed:22822057). Converts (22S)-22-hydroxycampesterol (22-OHCR) to
CC (22S,24R)-22-hydroxyergost-4-en-3-one (22-hydroxy-campesta-4-en-3-one,
CC 22-OH-4-en-3-one), 6-deoxocathasterone (6-deoxoCT) to (22S,24R)-22-
CC hydroxy-5alpha-ergostan-3-one (22-hydroxy-campesta-3-one, 22-OH-3-one),
CC (22R,23R)-22,23-dihydroxycampesterol (22,23-diOHCR) to (22R,23R)-22,23-
CC dihydroxy-campest-4-en-3-one (22,23-diOH-4-en-3-one), and 6-
CC deoxoteasterone (6-deoxoTE) to 3-dehydro-6-deoxoteasterone (6-deoxo3DT,
CC 6-deoxo-3-DHT) (PubMed:22822057). {ECO:0000269|PubMed:22822057}.
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:22822057};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69972;
CC Evidence={ECO:0000269|PubMed:22822057};
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:22822057};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69984;
CC Evidence={ECO:0000269|PubMed:22822057};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxycathasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = (22S,24R)-22-hydroxy-5alpha-ergostan-3-one + H(+) + 2
CC H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69975,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20714,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:59411;
CC Evidence={ECO:0000269|PubMed:22822057};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(22R,23R)-22,23-dihydroxycampesterol + O2 + reduced [NADPH--
CC hemoprotein reductase] = (22R,23R)-22,23-dihydroxycampest-4-en-3-one
CC + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:69979, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:80401,
CC ChEBI:CHEBI:80402; Evidence={ECO:0000269|PubMed:22822057};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69980;
CC Evidence={ECO:0000269|PubMed:22822057};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.96 uM for (22S)-22-hydroxycampesterol
CC {ECO:0000269|PubMed:22822057};
CC KM=1.90 uM for (22R,23R)-22,23-dihydroxycampesterol
CC {ECO:0000269|PubMed:22822057};
CC Note=kcat is 0.74 min(-1) for (22S)-22-hydroxycampesterol
CC (PubMed:22822057). kcat is 0.11 min(-1) for (22R,23R)-22,23-
CC dihydroxycampesterol (PubMed:22822057).
CC {ECO:0000269|PubMed:22822057};
CC -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC {ECO:0000269|PubMed:22822057}.
CC -!- INTERACTION:
CC Q42569; Q9M391: At3g54130; NbExp=3; IntAct=EBI-17071660, EBI-25520805;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q42569-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Dwarf plants containing severely reduced levels
CC of castasterone (CS) and brassinolide (BL) and of their precursor
CC molecules. {ECO:0000269|PubMed:22822057}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X87367; CAA60793.1; -; mRNA.
DR EMBL; X87368; CAA60794.1; -; Genomic_DNA.
DR EMBL; AB005237; BAB09663.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90909.1; -; Genomic_DNA.
DR EMBL; AY042837; AAK68777.1; -; mRNA.
DR EMBL; AY052726; AAK96630.1; -; mRNA.
DR EMBL; AY063722; AAL36072.1; -; mRNA.
DR EMBL; AY081480; AAM10042.1; -; mRNA.
DR EMBL; AY087526; AAM65068.1; -; mRNA.
DR PIR; S55379; S55379.
DR RefSeq; NP_196188.1; NM_120651.3. [Q42569-1]
DR AlphaFoldDB; Q42569; -.
DR SMR; Q42569; -.
DR BioGRID; 15732; 3.
DR IntAct; Q42569; 2.
DR STRING; 3702.AT5G05690.1; -.
DR iPTMnet; Q42569; -.
DR PaxDb; Q42569; -.
DR PRIDE; Q42569; -.
DR EnsemblPlants; AT5G05690.1; AT5G05690.1; AT5G05690. [Q42569-1]
DR GeneID; 830453; -.
DR Gramene; AT5G05690.1; AT5G05690.1; AT5G05690. [Q42569-1]
DR KEGG; ath:AT5G05690; -.
DR Araport; AT5G05690; -.
DR TAIR; locus:2166439; AT5G05690.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q42569; -.
DR OMA; KLWEVYM; -.
DR PhylomeDB; Q42569; -.
DR BioCyc; ARA:AT5G05690-MON; -.
DR BioCyc; MetaCyc:AT5G05690-MON; -.
DR UniPathway; UPA00381; -.
DR PRO; PR:Q42569; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q42569; baseline and differential.
DR Genevisible; Q42569; AT.
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; IMP:TAIR.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IMP:TAIR.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IEP:TAIR.
DR GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
DR GO; GO:0009911; P:positive regulation of flower development; IGI:TAIR.
DR GO; GO:0010224; P:response to UV-B; IGI:TAIR.
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 Alternative splicing; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..472
FT /note="Cytochrome P450 90A1"
FT /id="PRO_0000052184"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 418
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 472 AA; 53785 MW; 41A73F46D64E343F CRC64;
MAFTAFLLLL SSIAAGFLLL LRRTRYRRMG LPPGSLGLPL IGETFQLIGA YKTENPEPFI
DERVARYGSV FMTHLFGEPT IFSADPETNR FVLQNEGKLF ECSYPASICN LLGKHSLLLM
KGSLHKRMHS LTMSFANSSI IKDHLMLDID RLVRFNLDSW SSRVLLMEEA KKITFELTVK
QLMSFDPGEW SESLRKEYLL VIEGFFSLPL PLFSTTYRKA IQARRKVAEA LTVVVMKRRE
EEEEGAERKK DMLAALLAAD DGFSDEEIVD FLVALLVAGY ETTSTIMTLA VKFLTETPLA
LAQLKEEHEK IRAMKSDSYS LEWSDYKSMP FTQCVVNETL RVANIIGGVF RRAMTDVEIK
GYKIPKGWKV FSSFRAVHLD PNHFKDARTF NPWRWQSNSV TTGPSNVFTP FGGGPRLCPG
YELARVALSV FLHRLVTGFS WVPAEQDKLV FFPTTRTQKR YPIFVKRRDF AT
