C85A2_ARATH
ID C85A2_ARATH Reviewed; 465 AA.
AC Q940V4; Q8LFX3; Q9LH81;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cytochrome P450 85A2;
DE Short=AtCYP85A2;
DE AltName: Full=28-norcastasterone synthase {ECO:0000303|PubMed:22170941};
DE EC=1.14.14.- {ECO:0000269|PubMed:22170941};
DE AltName: Full=28-nordeoxoteasterone synthase {ECO:0000303|PubMed:22170941};
DE EC=1.14.14.- {ECO:0000269|PubMed:22170941};
DE AltName: Full=28-norteasterone synthase {ECO:0000303|PubMed:22170941};
DE EC=1.14.14.- {ECO:0000269|PubMed:22170941};
DE AltName: Full=28-nortyphasterol synthase {ECO:0000303|PubMed:22170941};
DE EC=1.14.14.- {ECO:0000269|PubMed:22170941};
DE AltName: Full=3-dehydroteasterone synthase {ECO:0000303|PubMed:11402205};
DE EC=1.14.14.- {ECO:0000269|PubMed:11402205};
DE AltName: Full=Brassinolide synthase {ECO:0000303|PubMed:15710611};
DE EC=1.14.14.- {ECO:0000269|PubMed:15710611};
DE AltName: Full=Brassinosteroid-6-oxidase 2 {ECO:0000303|PubMed:12529536};
DE Short=BR6ox 2 {ECO:0000303|PubMed:12529536};
DE AltName: Full=C6-oxidase 2 {ECO:0000303|PubMed:12529536};
DE AltName: Full=Castasterone synthase {ECO:0000303|PubMed:11402205};
DE EC=1.14.14.- {ECO:0000269|PubMed:11402205};
DE AltName: Full=Teasterone synthase {ECO:0000303|PubMed:11402205};
DE EC=1.14.14.- {ECO:0000269|PubMed:11402205};
DE AltName: Full=Typhasterol synthase {ECO:0000303|PubMed:11402205};
DE EC=1.14.14.- {ECO:0000269|PubMed:11402205};
GN Name=CYP85A2; Synonyms=BR6OX2 {ECO:0000303|PubMed:12529536};
GN OrderedLocusNames=At3g30180 {ECO:0000312|Araport:AT3G30180};
GN ORFNames=T20F20.9 {ECO:0000312|EMBL:BAB02270.1},
GN T20F20_6 {ECO:0000312|EMBL:BAB02270.1};
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 [MRNA], FUNCTION, INDUCTION, AND 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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, AND PATHWAY.
RX PubMed=11402205; DOI=10.1104/pp.126.2.770;
RA Shimada Y., Fujioka S., Miyauchi N., Kushiro M., Takatsuto S., Nomura T.,
RA Yokota T., Kamiya Y., Bishop G.J., Yoshida S.;
RT "Brassinosteroid-6-oxidases from Arabidopsis and tomato catalyze multiple
RT C-6 oxidations in brassinosteroid biosynthesis.";
RL Plant Physiol. 126:770-779(2001).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=15710611; DOI=10.1074/jbc.m414592200;
RA Nomura T., Kushiro T., Yokota T., Kamiya Y., Bishop G.J., Yamaguchi S.;
RT "The last reaction producing brassinolide is catalyzed by cytochrome P-
RT 450s, CYP85A3 in tomato and CYP85A2 in Arabidopsis.";
RL J. Biol. Chem. 280:17873-17879(2005).
RN [8]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=18685225; DOI=10.1271/bbb.80192;
RA Katsumata T., Hasegawa A., Fujiwara T., Komatsu T., Notomi M., Abe H.,
RA Natsume M., Kawaide H.;
RT "Arabidopsis CYP85A2 catalyzes lactonization reactions in the biosynthesis
RT of 2-deoxy-7-oxalactone brassinosteroids.";
RL Biosci. Biotechnol. Biochem. 72:2110-2117(2008).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=22170941; DOI=10.1093/jxb/err354;
RA Joo S.-H., Kim T.-W., Son S.-H., Lee W.S., Yokota T., Kim S.-K.;
RT "Biosynthesis of a cholesterol-derived brassinosteroid, 28-norcastasterone,
RT in Arabidopsis thaliana.";
RL J. Exp. Bot. 63:1823-1833(2012).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-462, ISOPRENYLATION AT
RP CYS-462, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27455172; DOI=10.1038/nplants.2016.114;
RA Northey J.G., Liang S., Jamshed M., Deb S., Foo E., Reid J.B., McCourt P.,
RA Samuel M.A.;
RT "Farnesylation mediates brassinosteroid biosynthesis to regulate abscisic
RT acid responses.";
RL Nat. Plants 2:16114-16114(2016).
RN [11]
RP TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RX PubMed=32333772; DOI=10.1093/pcp/pcaa053;
RA Hamasaki H., Ayano M., Nakamura A., Fujioka S., Asami T., Takatsuto S.,
RA Yoshida S., Oka Y., Matsui M., Shimada Y.;
RT "Light activates brassinosteroid biosynthesis to promote hook opening and
RT petiole development in Arabidopsis thaliana.";
RL Plant Cell Physiol. 61:1239-1251(2020).
CC -!- FUNCTION: Catalyzes the C6-oxidation step and lactonization in
CC brassinosteroids biosynthesis (PubMed:15710611). Converts 6-
CC deoxocastasterone (6-deoxoCS) to castasterone (CS), and castasterone to
CC brassinolide (BL) (PubMed:15710611). May also convert 6-deoxoteasterone
CC (6-deoxoTE) to teasterone (TE), 3-dehydro-6-deoxoteasterone (6-
CC deoxo3DT, 6-deoxo-3-DHT) to 3-dehydroteasterone (3DT, 3-DHT), and 6-
CC deoxotyphasterol (6-deoxoTY) to typhasterol (TY). Seems also able to
CC convert teasterone (TE) and typhasterol (TY) to 7-oxateasterone (7-
CC OXTE) and 7-oxatyphasterol (7-OXTY), respectively (PubMed:18685225).
CC Catalyzes the conversion of 6-deoxo-28-norteasterone (6-deoxo-28-norTE)
CC to 28-norteasterone (28-norTE), 6-deoxo-28-nordeoxoteasterone (6-deoxo-
CC 28-nor-3-DHT) to 28-nordeoxoteasterone (28-nor-3-DHT), 6-deoxo-28-
CC nortyphasterol (6-deoxo-28-norTY) to 28-nortyphasterol (28-norTY) and
CC 6-deoxo-28-norcastasterone (6-deoxo-28-norCS) to 28-norcastasterone
CC (28-norCS) (PubMed:22170941). Involved in a negative regulation of
CC responses to abscisic acid (ABA) and drought tolerance
CC (PubMed:27455172). {ECO:0000269|PubMed:11402205,
CC ECO:0000269|PubMed:12529536, ECO:0000269|PubMed:15710611,
CC ECO:0000269|PubMed:18685225, ECO:0000269|PubMed:22170941,
CC ECO:0000269|PubMed:27455172}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxoteasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 6alpha-hydroxyteasterone + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69959, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20716,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188499;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69960;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6alpha-hydroxytyphasterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] +
CC teasterone; Xref=Rhea:RHEA:69963, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:26863, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:188495; Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69964;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-6-deoxoteasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 3-dehydro-6alpha-hydroxyteasterone + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69947,
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:188496;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69948;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-6alpha-hydroxyteasterone + O2 + reduced [NADPH--
CC hemoprotein reductase] = 3-dehydroteasterone + H(+) + 2 H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69951,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20000,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188496;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69952;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxotyphasterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 6alpha-hydroxytyphasterol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69939, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20717,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188495;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69940;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6alpha-hydroxytyphasterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] +
CC typhasterol; Xref=Rhea:RHEA:69943, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:27173, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:188495; Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69944;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxocastasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 6alpha-hydroxycastasterone + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69875, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20712,
CC ChEBI:CHEBI:20760, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69876;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6alpha-hydroxycastasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = castasterone + H(+) + 2 H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:69879, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:20760, ChEBI:CHEBI:23051,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69880;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=castasterone + O2 + reduced [NADPH--hemoprotein reductase] =
CC brassinolide + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:69923, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:23051, ChEBI:CHEBI:28277, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69924;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-6-deoxoteasterone + 2 O2 + 2 reduced [NADPH--
CC hemoprotein reductase] = 3-dehydroteasterone + 2 H(+) + 3 H2O + 2
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70039,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20000,
CC ChEBI:CHEBI:20710, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70040;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxocastasterone + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = castasterone + 2 H(+) + 3 H2O + 2 oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:70031, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:20712, ChEBI:CHEBI:23051,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70032;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxoteasterone + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein
CC reductase] + teasterone; Xref=Rhea:RHEA:70043, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:20716, ChEBI:CHEBI:26863,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70044;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxotyphasterol + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein
CC reductase] + typhasterol; Xref=Rhea:RHEA:70035, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:20717, ChEBI:CHEBI:27173,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70036;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxo-28-norteasterone + 2 O2 + 2 reduced [NADPH--
CC hemoprotein reductase] = 28-norteasterone + 2 H(+) + 3 H2O + 2
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70111,
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:188985, ChEBI:CHEBI:188988;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70112;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxo-28-norteasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 6alpha-hydroxy-28-norteasterone + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70115, Rhea:RHEA-
CC 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:188985, ChEBI:CHEBI:188987;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70116;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6alpha-hydroxy-28-norteasterone + O2 + reduced [NADPH--
CC hemoprotein reductase] = 28-norteasterone + H(+) + 2 H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70119, Rhea:RHEA-
CC 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:188987, ChEBI:CHEBI:188988;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70120;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxo-28-nortyphasterol + 2 O2 + 2 reduced [NADPH--
CC hemoprotein reductase] = 28-nortyphasterol + 2 H(+) + 3 H2O + 2
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70135,
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:188992, ChEBI:CHEBI:188994;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70136;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxo-28-nortyphasterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 6alpha-hydroxy-28-nortyphasterol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70139, Rhea:RHEA-
CC 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:188992, ChEBI:CHEBI:188993;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70140;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6alpha-hydroxy-28-nortyphasterol + O2 + reduced [NADPH--
CC hemoprotein reductase] = 28-nortyphasterol + H(+) + 2 H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70143, Rhea:RHEA-
CC 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:188993, ChEBI:CHEBI:188994;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70144;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxo-28-norcastasterone + 2 O2 + 2 reduced [NADPH--
CC hemoprotein reductase] = 28-norcastasterone + 2 H(+) + 3 H2O + 2
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70147,
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:188995, ChEBI:CHEBI:188997;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70148;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxo-28-norcastasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 6alpha-hydroxy-28-norcastasterone + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70151,
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:188995, ChEBI:CHEBI:188996;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70152;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6alpha-hydroxy-28-norcastasterone + O2 + reduced [NADPH--
CC hemoprotein reductase] = 28-norcastasterone + H(+) + 2 H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70155, Rhea:RHEA-
CC 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:188996, ChEBI:CHEBI:188997;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70156;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-6-deoxo-28-norteasterone + 2 O2 + 2 reduced [NADPH--
CC hemoprotein reductase] = 6-dehydro-28-norteasterone + 2 H(+) + 3 H2O
CC + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70123,
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:188989, ChEBI:CHEBI:188991;
CC Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70124;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-6-deoxo-28-norteasterone + O2 + reduced [NADPH--
CC hemoprotein reductase] = 3-dehydro-6alpha-hydroxy-28-norteasterone +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:70127, 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:188989,
CC ChEBI:CHEBI:188990; Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70128;
CC Evidence={ECO:0000269|PubMed:11402205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-6alpha-hydroxy-28-norteasterone + O2 + reduced
CC [NADPH--hemoprotein reductase] = 6-dehydro-28-norteasterone + H(+) +
CC 2 H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:70131, 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:188990,
CC ChEBI:CHEBI:188991; Evidence={ECO:0000269|PubMed:11402205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70132;
CC Evidence={ECO:0000269|PubMed:11402205};
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:11402205, ECO:0000269|PubMed:15710611,
CC ECO:0000269|PubMed:22170941}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:27455172}. Note=Concentrates in endoplasmic
CC reticulum subdomains adjacent to chloroplasts when farnesylated.
CC {ECO:0000269|PubMed:27455172}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, hypocotyls, leaves, siliques,
CC shoots, and roots, with a higher expression in apical shoots.
CC {ECO:0000269|PubMed:12529536, ECO:0000269|PubMed:32333772}.
CC -!- INDUCTION: Repressed by brassinolide (BL) treatment (PubMed:12529536).
CC Induced rapidly and transiently in seedlings hooks, petioles and
CC cotyledons but fades out of hypocotyls after exposure to light
CC (PubMed:32333772). {ECO:0000269|PubMed:12529536,
CC ECO:0000269|PubMed:32333772}.
CC -!- PTM: Isoprenylated (farnesylated); this addition of a 15-carbon
CC farnesyl isoprenoid to the carboxy terminus is required for endoplasmic
CC reticulum localization and essential for the biosynthesis of
CC brassinolide. {ECO:0000269|PubMed:27455172}.
CC -!- DISRUPTION PHENOTYPE: Reduced brassinolide accumulation but increased
CC responsiveness to abscisic acid (ABA) and overall drought tolerance.
CC {ECO:0000269|PubMed:27455172}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM61160.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB087801; BAC55065.1; -; mRNA.
DR EMBL; AP002060; BAB02270.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77620.1; -; Genomic_DNA.
DR EMBL; AY052655; AAK96559.1; -; mRNA.
DR EMBL; AY063728; AAL36078.1; -; mRNA.
DR EMBL; AY084595; AAM61160.1; ALT_INIT; mRNA.
DR RefSeq; NP_566852.1; NM_113917.4.
DR AlphaFoldDB; Q940V4; -.
DR SMR; Q940V4; -.
DR BioGRID; 8036; 12.
DR IntAct; Q940V4; 12.
DR STRING; 3702.AT3G30180.1; -.
DR PaxDb; Q940V4; -.
DR PRIDE; Q940V4; -.
DR ProteomicsDB; 240568; -.
DR EnsemblPlants; AT3G30180.1; AT3G30180.1; AT3G30180.
DR GeneID; 822709; -.
DR Gramene; AT3G30180.1; AT3G30180.1; AT3G30180.
DR KEGG; ath:AT3G30180; -.
DR Araport; AT3G30180; -.
DR TAIR; locus:2098802; AT3G30180.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q940V4; -.
DR OMA; PEDPIDC; -.
DR OrthoDB; 574756at2759; -.
DR PhylomeDB; Q940V4; -.
DR BioCyc; ARA:AT3G30180-MON; -.
DR BioCyc; MetaCyc:AT3G30180-MON; -.
DR UniPathway; UPA00381; -.
DR PRO; PR:Q940V4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q940V4; baseline and differential.
DR Genevisible; Q940V4; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102734; F:brassinolide synthase activity; IMP:UniProtKB.
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; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IDA:TAIR.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IBA:GO_Central.
DR GO; GO:0018343; P:protein farnesylation; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
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 Brassinosteroid biosynthesis; Endoplasmic reticulum; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Lipoprotein; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Prenylation; Reference proteome;
KW Steroid biosynthesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..465
FT /note="Cytochrome P450 85A2"
FT /id="PRO_0000052170"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 462..465
FT /note="Farnesylation CAAX motif"
FT /evidence="ECO:0000269|PubMed:27455172"
FT BINDING 415
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 LIPID 462
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:27455172"
FT MUTAGEN 462
FT /note="C->S: Lost isoprenylation (farnesylation) leading to
FT a reduced brassinolide accumulation but increased
FT responsiveness to abscisic acid (ABA) and overall drought
FT tolerance."
FT /evidence="ECO:0000269|PubMed:27455172"
FT CONFLICT 221
FT /note="V -> F (in Ref. 1; BAB02270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 53815 MW; 280A21D0712FCA11 CRC64;
MGIMMMILGL LVIIVCLCTA LLRWNQMRYS KKGLPPGTMG WPIFGETTEF LKQGPDFMKN
QRLRYGSFFK SHILGCPTIV SMDAELNRYI LMNESKGLVA GYPQSMLDIL GTCNIAAVHG
PSHRLMRGSL LSLISPTMMK DHLLPKIDDF MRNYLCGWDD LETVDIQEKT KHMAFLSSLL
QIAETLKKPE VEEYRTEFFK LVVGTLSVPI DIPGTNYRSG VQARNNIDRL LTELMQERKE
SGETFTDMLG YLMKKEDNRY LLTDKEIRDQ VVTILYSGYE TVSTTSMMAL KYLHDHPKAL
EELRREHLAI RERKRPDEPL TLDDIKSMKF TRAVIFETSR LATIVNGVLR KTTHDLELNG
YLIPKGWRIY VYTREINYDT SLYEDPMIFN PWRWMEKSLE SKSYFLLFGG GVRLCPGKEL
GISEVSSFLH YFVTKYRWEE NGEDKLMVFP RVSAPKGYHL KCSPY
