C85A1_SOLLC
ID C85A1_SOLLC Reviewed; 464 AA.
AC Q43147;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Cytochrome P450 85A1 {ECO:0000303|PubMed:15710611};
DE Short=LeCYP85A1 {ECO:0000303|PubMed:15710611};
DE AltName: Full=C6-oxidase {ECO:0000303|PubMed:11402205};
DE AltName: Full=Castasterone synthase CYP85A1 {ECO:0000303|PubMed:15710611};
DE EC=1.14.14.- {ECO:0000269|PubMed:15710611};
DE AltName: Full=Protein DWARF {ECO:0000303|PubMed:8672892, ECO:0000303|PubMed:9990098};
GN Name=CYP85A1 {ECO:0000303|PubMed:15710611};
GN Synonyms=CYP85 {ECO:0000303|PubMed:8672892}, D {ECO:0000303|PubMed:8672892,
GN ECO:0000303|PubMed:9990098};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8672892; DOI=10.2307/3870208;
RA Bishop G.J., Harrison K., Jones J.J.G.D.;
RT "The tomato Dwarf gene isolated by heterologous transposon tagging encodes
RT the first member of a new cytochrome P450 family.";
RL Plant Cell 8:959-969(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=9990098; DOI=10.1073/pnas.96.4.1761;
RA Bishop G.J., Nomura T., Yokota T., Harrison K., Noguchi T., Fujioka S.,
RA Takatsuto S., Jones J.D., Kamiya Y.;
RT "The tomato DWARF enzyme catalyses C-6 oxidation in brassinosteroid
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1761-1766(1999).
RN [3]
RP FUNCTION.
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, 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 [5]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=15807787; DOI=10.1111/j.1365-313x.2005.02376.x;
RA Montoya T., Nomura T., Yokota T., Farrar K., Harrison K., Jones J.J.G.D.,
RA Kaneta T., Kamiya Y., Szekeres M., Bishop G.J.;
RT "Patterns of Dwarf expression and brassinosteroid accumulation in tomato
RT reveal the importance of brassinosteroid synthesis during fruit
RT development.";
RL Plant J. 42:262-269(2005).
CC -!- FUNCTION: Catalyzes the C6-oxidation step in brassinosteroids
CC biosynthesis (PubMed:15710611). Converts 6-deoxocastasterone (6-
CC deoxoCS) to castasterone (CS) (PubMed:15710611, PubMed:9990098). May
CC also convert 6-deoxoteasterone (6-deoxoTE) to teasterone (TE), 3-
CC dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo3DHT) to 3-
CC dehydroteasterone (3DT, 3-DHT), and 6-deoxotyphasterol (6-deoxoTY) to
CC typhasterol (TY), but not castasterone (CS) to brassinolide (BL)
CC (PubMed:15710611). {ECO:0000269|PubMed:11402205,
CC ECO:0000269|PubMed:15710611, ECO:0000269|PubMed:9990098}.
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:15710611};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69876;
CC Evidence={ECO:0000269|PubMed:15710611};
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:15710611};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69880;
CC Evidence={ECO:0000269|PubMed:15710611};
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:15710611};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70032;
CC Evidence={ECO:0000269|PubMed:15710611};
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:15710611, ECO:0000269|PubMed:9990098}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in sub-meristematic regions of shoot and
CC root apexes, in zones undergoing lateral root formation, in fruits, and
CC in all flower parts, with a high expression in young flower buds and at
CC the joint in the pedicel. {ECO:0000269|PubMed:15710611,
CC ECO:0000269|PubMed:15807787}.
CC -!- DEVELOPMENTAL STAGE: Strong expression in the locular jelly during seed
CC development. {ECO:0000269|PubMed:15807787}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; U54770; AAB17070.1; -; mRNA.
DR PIR; T07859; T07859.
DR RefSeq; NP_001234263.1; NM_001247334.2.
DR AlphaFoldDB; Q43147; -.
DR SMR; Q43147; -.
DR STRING; 4081.Solyc02g089160.2.1; -.
DR PaxDb; Q43147; -.
DR PRIDE; Q43147; -.
DR EnsemblPlants; Solyc02g089160.3.1; Solyc02g089160.3.1; Solyc02g089160.3.
DR GeneID; 100037489; -.
DR Gramene; Solyc02g089160.3.1; Solyc02g089160.3.1; Solyc02g089160.3.
DR KEGG; sly:100037489; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q43147; -.
DR OMA; WTATRDR; -.
DR OrthoDB; 574756at2759; -.
DR PhylomeDB; Q43147; -.
DR UniPathway; UPA00381; -.
DR Proteomes; UP000004994; Chromosome 2.
DR ExpressionAtlas; Q43147; baseline and differential.
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:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IBA:GO_Central.
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; Heme; Iron; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..464
FT /note="Cytochrome P450 85A1"
FT /id="PRO_0000052171"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 414
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 464 AA; 53706 MW; D2B21AAAB7B14E94 CRC64;
MAFFLIFLSS FFGLCIFCTA LLRWNQVKYN QKNLPPGTMG WPLFGETTEF LKLGPSFMKN
QRARYGSFFK SHILGCPTIV SMDSELNRYI LVNEAKGLVP GYPQSMIDIL GKCNIAAVNG
SAHKYMRGAL LSLISPTMIR DQLLPKIDEF MRSHLTNWDN KVIDIQEKTN KMAFLSSLKQ
IAGIESTSLA QEFMSEFFNL VLGTLSLPIN LPNTNYHRGF QARKIIVNLL RTLIEERRAS
KEIQHDMLGY LMNEEATRFK LTDDEMIDLI ITILYSGYET VSTTSMMAVK YLHDHPKVLE
ELRKEHMAIR EKKKPEDPID YNDYRSMRFT RAVILETSRL ATIVNGVLRK TTQDMEINGY
IIPKGWRIYV YTRELNYDPR LYPDPYSFNP WRWMDKSLEH QNSFLVFGGG TRQCPGKELG
VAEISTFLHY FVTKYRWEEI GGDKLMKFPR VEAPNGLRIR VSAH
