C85A3_SOLLC
ID C85A3_SOLLC Reviewed; 467 AA.
AC Q50LE0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Cytochrome P450 85A3 {ECO:0000303|PubMed:15710611};
DE Short=LeCYP85A3 {ECO:0000303|PubMed:15710611};
DE AltName: Full=Brassinolide synthase CYP85A3 {ECO:0000303|PubMed:15710611};
DE EC=1.14.14.- {ECO:0000269|PubMed:15710611};
DE AltName: Full=C6-oxidase;
DE AltName: Full=Castasterone synthase CYP85A3 {ECO:0000303|PubMed:15710611};
DE EC=1.14.14.- {ECO:0000269|PubMed:15710611};
GN Name=CYP85A3 {ECO:0000303|PubMed:15710611};
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], FUNCTION, TISSUE SPECIFICITY, CATALYTIC
RP 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).
CC -!- FUNCTION: Catalyzes the C6-oxidation step in brassinosteroids
CC biosynthesis (PubMed:15710611). Converts 6-deoxocastasterone (6-
CC deoxoCS) to castasterone (CS), and castasterone (CS) to brassinolide
CC (BL) (PubMed:15710611). {ECO:0000269|PubMed:15710611}.
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=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:15710611};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69924;
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}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in fruits. {ECO:0000269|PubMed:15710611}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB190445; BAD98244.1; -; mRNA.
DR RefSeq; NP_001234520.1; NM_001247591.1.
DR AlphaFoldDB; Q50LE0; -.
DR SMR; Q50LE0; -.
DR STRING; 4081.Solyc02g065750.1.1; -.
DR PaxDb; Q50LE0; -.
DR PRIDE; Q50LE0; -.
DR EnsemblPlants; Solyc02g065750.2.1; Solyc02g065750.2.1; Solyc02g065750.2.
DR GeneID; 100136888; -.
DR Gramene; Solyc02g065750.2.1; Solyc02g065750.2.1; Solyc02g065750.2.
DR KEGG; sly:100136888; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q50LE0; -.
DR OMA; NCNVIDI; -.
DR OrthoDB; 574756at2759; -.
DR PhylomeDB; Q50LE0; -.
DR BioCyc; MetaCyc:MON-9503; -.
DR UniPathway; UPA00381; -.
DR Proteomes; UP000004994; Chromosome 2.
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 Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..467
FT /note="Cytochrome P450 85A3"
FT /id="PRO_0000052174"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 417
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 467 AA; 53795 MW; 7DBDF8E16C3B11AC CRC64;
MAIFLIIFVV FFGFCILSTP LFRWIDIVYN KKNLPPGTMG WPIFGETREF LNQGPNFMKN
QRARYGNFFK SHILGCPTVV SMDAGLNVYI LNNEAKGLIP GYPQSMLDIL GKCNIAAVHG
ATHKYIRGAL LSLINPTMIK DHILPKIDKF MRSHLSGWDN CNVIDIQQMT KEMAFFSSLD
QIGGFATSSS IAQEFRAGFL NIALGTISLP INFPTTNYYR GLQGRKTIVK LLRKIIEDRR
GSKKIQQDML GLMMNEEAKN RYTLSDEELI DQIITIMYSG FETVSTTSMM AVKYLHDHPK
ALEEIRKEHF AIREKKSLED PIDYNDFKAM RFTRAVIYET LRLATIVNGV LRKTTQDMEL
NGYMIPKGWR IYVYTRELNY DPLIYPDPYT FNPWRWLENN LDHQSSFLMF GGGTRLCPGK
ELGVAEISTF LHYFVTRYRW EEVGGNKLMK FPRVEALNGL WIKVSAY
