C90B1_ARATH
ID C90B1_ARATH Reviewed; 513 AA.
AC O64989; Q9SCQ9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cytochrome P450 90B1 {ECO:0000303|PubMed:9490746};
DE Short=AtCYP90B1 {ECO:0000303|PubMed:9490746};
DE AltName: Full=(22S)-22-hydroxycampesterol synthase {ECO:0000303|PubMed:16460510};
DE EC=1.14.14.- {ECO:0000269|PubMed:16460510};
DE AltName: Full=6-deoxycathasterone synthase {ECO:0000303|PubMed:9490746};
DE EC=1.14.14.- {ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746};
DE AltName: Full=Cathasterone synthase {ECO:0000303|PubMed:9490746};
DE EC=1.14.14.- {ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746};
DE AltName: Full=Protein DWARF 4 {ECO:0000303|PubMed:9490746};
DE Short=Dwarf4 {ECO:0000303|PubMed:9490746};
DE AltName: Full=Steroid 22-alpha-hydroxylase {ECO:0000303|PubMed:9490746};
GN Name=CYP90B1 {ECO:0000303|PubMed:9490746};
GN Synonyms=DWF4 {ECO:0000303|PubMed:9490746};
GN OrderedLocusNames=At3g50660 {ECO:0000312|Araport:AT3G50660};
GN ORFNames=T3A5.40 {ECO:0000312|EMBL:CAB62435.1};
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], MUTAGENESIS OF 324-ILE--PHE-326,
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Wassilewskija-2;
RX PubMed=9490746; DOI=10.2307/3870701;
RA Choe S., Dilkes B.P., Fujioka S., Takatsuto S., Sakurai A., Feldmann K.A.;
RT "The DWF4 gene of Arabidopsis encodes a cytochrome P450 that mediates
RT multiple 22alpha-hydroxylation steps in brassinosteroid biosynthesis.";
RL Plant Cell 10:231-243(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 TISSUE SPECIFICITY.
RX PubMed=12529536; DOI=10.1104/pp.013029;
RA Shimada Y., Goda H., Nakamura A., Takatsuto S., Fujioka S., Yoshida S.;
RT "Organ-specific expression of brassinosteroid-biosynthetic genes and
RT distribution of endogenous brassinosteroids in Arabidopsis.";
RL Plant Physiol. 131:287-297(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16460510; DOI=10.1111/j.1365-313x.2005.02639.x;
RA Fujita S., Ohnishi T., Watanabe B., Yokota T., Takatsuto S., Fujioka S.,
RA Yoshida S., Sakata K., Mizutani M.;
RT "Arabidopsis CYP90B1 catalyses the early C-22 hydroxylation of C27, C28 and
RT C29 sterols.";
RL Plant J. 45:765-774(2006).
CC -!- FUNCTION: Catalyzes the C22-alpha-hydroxylation step in
CC brassinosteroids biosynthesis (PubMed:9490746, PubMed:16460510).
CC Converts campesterol (CR) to (22S)-22-hydroxycampesterol (22-OHCR, 22-
CC hydroxyCR), campestanol (CN) to 6-deoxycathasterone (6-deoxoCT), and 6-
CC oxocampestanol (6-oxoCN) to cathasterone (CT) (PubMed:9490746,
CC PubMed:16460510). Can also use cholesterol and cholestanol as
CC substrates (PubMed:9490746, PubMed:16460510).
CC {ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746}.
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:16460510};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69836;
CC Evidence={ECO:0000269|PubMed:16460510};
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:16460510,
CC ECO:0000269|PubMed:9490746};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69832;
CC Evidence={ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC (22S)-22-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:69839, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:1301, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:16460510};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69840;
CC Evidence={ECO:0000269|PubMed:16460510};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholestanol + O2 + reduced [NADPH--hemoprotein reductase] =
CC (22S)-22-hydroxycholestanol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:69871, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:86570, ChEBI:CHEBI:188465;
CC Evidence={ECO:0000269|PubMed:16460510};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69872;
CC Evidence={ECO:0000269|PubMed:16460510};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-oxocampestanol + O2 + reduced [NADPH--hemoprotein reductase]
CC = cathasterone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:70003, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:20747, ChEBI:CHEBI:23057, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:16460510,
CC ECO:0000269|PubMed:9490746};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70004;
CC Evidence={ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.35 uM for campesterol (at pH 7.25 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16460510};
CC KM=3.0 uM for campestanol (at pH 7.25 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16460510};
CC Note=kcat is 1.8 min(-1) for campesterol (at pH 7.25 and 30 degrees
CC Celsius) (PubMed:16460510). kcat is 0.049 min(-1) for campestanol (at
CC pH 7.25 and 30 degrees Celsius) (PubMed:16460510).
CC {ECO:0000269|PubMed:16460510};
CC -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC {ECO:0000269|PubMed:16460510, ECO:0000269|PubMed:9490746}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves, shoots, and roots, with
CC a higher expression in siliques and apical shoots.
CC {ECO:0000269|PubMed:12529536}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF044216; AAC05093.1; -; Genomic_DNA.
DR EMBL; AL132979; CAB62435.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78691.1; -; Genomic_DNA.
DR EMBL; AY090266; AAL90927.1; -; mRNA.
DR EMBL; AF412114; AAL06567.1; -; mRNA.
DR PIR; T46143; T46143.
DR RefSeq; NP_190635.1; NM_114926.4.
DR AlphaFoldDB; O64989; -.
DR SMR; O64989; -.
DR STRING; 3702.AT3G50660.1; -.
DR PaxDb; O64989; -.
DR PRIDE; O64989; -.
DR ProteomicsDB; 239121; -.
DR EnsemblPlants; AT3G50660.1; AT3G50660.1; AT3G50660.
DR GeneID; 824229; -.
DR Gramene; AT3G50660.1; AT3G50660.1; AT3G50660.
DR KEGG; ath:AT3G50660; -.
DR Araport; AT3G50660; -.
DR TAIR; locus:2101704; AT3G50660.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; O64989; -.
DR OMA; FHWKLAA; -.
DR OrthoDB; 574756at2759; -.
DR BioCyc; ARA:AT3G50660-MON; -.
DR BioCyc; MetaCyc:AT3G50660-MON; -.
DR BRENDA; 1.14.99.B1; 399.
DR SABIO-RK; O64989; -.
DR UniPathway; UPA00381; -.
DR PRO; PR:O64989; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O64989; baseline and differential.
DR Genevisible; O64989; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IMP:TAIR.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IBA:GO_Central.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IGI:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0010358; P:leaf shaping; IMP:TAIR.
DR GO; GO:0009741; P:response to brassinosteroid; IMP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
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 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..513
FT /note="Cytochrome P450 90B1"
FT /id="PRO_0000052185"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 252..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 462
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 324..326
FT /note="Missing: In dwf4-2; dwarf plant."
FT /evidence="ECO:0000269|PubMed:9490746"
FT CONFLICT 492
FT /note="K -> Q (in Ref. 1; AAC05093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 58868 MW; B1639BDD9A5D7C93 CRC64;
MFETEHHTLL PLLLLPSLLS LLLFLILLKR RNRKTRFNLP PGKSGWPFLG ETIGYLKPYT
ATTLGDFMQQ HVSKYGKIYR SNLFGEPTIV SADAGLNRFI LQNEGRLFEC SYPRSIGGIL
GKWSMLVLVG DMHRDMRSIS LNFLSHARLR TILLKDVERH TLFVLDSWQQ NSIFSAQDEA
KKFTFNLMAK HIMSMDPGEE ETEQLKKEYV TFMKGVVSAP LNLPGTAYHK ALQSRATILK
FIERKMEERK LDIKEEDQEE EEVKTEDEAE MSKSDHVRKQ RTDDDLLGWV LKHSNLSTEQ
ILDLILSLLF AGHETSSVAI ALAIFFLQAC PKAVEELREE HLEIARAKKE LGESELNWDD
YKKMDFTQCV INETLRLGNV VRFLHRKALK DVRYKGYDIP SGWKVLPVIS AVHLDNSRYD
QPNLFNPWRW QQQNNGASSS GSGSFSTWGN NYMPFGGGPR LCAGSELAKL EMAVFIHHLV
LKFNWELAED DKPFAFPFVD FPNGLPIRVS RIL
