DET2_SOLLC
ID DET2_SOLLC Reviewed; 257 AA.
AC Q5K2N1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Steroid 5-alpha-reductase DET2 {ECO:0000303|PubMed:15993049};
DE Short=LeDET2 {ECO:0000303|PubMed:15993049};
DE EC=1.3.1.22 {ECO:0000269|PubMed:15993049};
GN Name=DET2 {ECO:0000303|PubMed:15993049};
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, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=cv. Saint Pierre; TISSUE=Leaf;
RX PubMed=15993049; DOI=10.1016/j.jsbmb.2005.04.035;
RA Rosati F., Bardazzi I., De Blasi P., Simi L., Scarpi D., Guarna A.,
RA Serio M., Racchi M.L., Danza G.;
RT "5alpha-Reductase activity in Lycopersicon esculentum: cloning and
RT functional characterization of LeDET2 and evidence of the presence of two
RT isoenzymes.";
RL J. Steroid Biochem. Mol. Biol. 96:287-299(2005).
CC -!- FUNCTION: Involved in a reduction step in the biosynthesis of the plant
CC steroid, brassinolide (BL) (PubMed:15993049). Can use progesterone,
CC testosterone, androstenedione and campestenone as substrate
CC (PubMed:15993049). {ECO:0000269|PubMed:15993049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid +
CC H(+) + NADPH; Xref=Rhea:RHEA:54384, ChEBI:CHEBI:13601,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:47909, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.3.1.22;
CC Evidence={ECO:0000269|PubMed:15993049};
CC -!- ACTIVITY REGULATION: Repressed by steroid (4-MA, VG106, PD91, PD17,
CC Finasteride) and non-steroid (AS601811, AFA27, AFA76, AFA131, AFA192)
CC inhibitors; steroid inhibitors are generally more efficient.
CC {ECO:0000269|PubMed:15993049}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.75 uM for progesterone (expressed in COS-7 cells)
CC {ECO:0000269|PubMed:15993049};
CC KM=26 uM for androstenedione (expressed in COS-7 cells)
CC {ECO:0000269|PubMed:15993049};
CC KM=40 uM for testosterone (expressed in COS-7 cells)
CC {ECO:0000269|PubMed:15993049};
CC Vmax=0.34 nmol/min/mg enzyme with progesterone as substrate
CC (expressed in COS-7 cells) {ECO:0000269|PubMed:15993049};
CC Vmax=0.32 nmol/min/mg enzyme with androstenedione as substrate
CC (expressed in COS-7 cells) {ECO:0000269|PubMed:15993049};
CC Vmax=0.21 nmol/min/mg enzyme with testosterone as substrate
CC (expressed in COS-7 cells) {ECO:0000269|PubMed:15993049};
CC -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC {ECO:0000269|PubMed:15993049}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and hypocotyls and, to a
CC lower extent, in stems, cotyledons, roots, seeds and callus.
CC {ECO:0000269|PubMed:15993049}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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DR EMBL; AJ786362; CAH05260.1; -; mRNA.
DR RefSeq; NP_001234040.1; NM_001247111.2.
DR AlphaFoldDB; Q5K2N1; -.
DR SMR; Q5K2N1; -.
DR STRING; 4081.Solyc10g086500.1.1; -.
DR PaxDb; Q5K2N1; -.
DR EnsemblPlants; Solyc10g086500.1.1; Solyc10g086500.1.1.1; Solyc10g086500.1.
DR GeneID; 543801; -.
DR Gramene; Solyc10g086500.1.1; Solyc10g086500.1.1.1; Solyc10g086500.1.
DR KEGG; sly:543801; -.
DR eggNOG; KOG1638; Eukaryota.
DR HOGENOM; CLU_065395_1_0_1; -.
DR InParanoid; Q5K2N1; -.
DR OMA; HRDYQQR; -.
DR OrthoDB; 1574389at2759; -.
DR PhylomeDB; Q5K2N1; -.
DR BioCyc; MetaCyc:MON-21176; -.
DR BRENDA; 1.3.1.22; 3101.
DR SABIO-RK; Q5K2N1; -.
DR UniPathway; UPA00381; -.
DR Proteomes; UP000004994; Chromosome 10.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IEA:InterPro.
DR GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0050213; F:progesterone 5-alpha-reductase activity; IDA:UniProtKB.
DR GO; GO:0009917; F:sterol 5-alpha reductase activity; IEA:EnsemblPlants.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IEA:EnsemblPlants.
DR InterPro; IPR016636; 3-oxo-5-alpha-steroid_4-DH.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039357; SRD5A/TECR.
DR PANTHER; PTHR10556; PTHR10556; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PIRSF; PIRSF015596; 5_alpha-SR2; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 1: Evidence at protein level;
KW Membrane; NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..257
FT /note="Steroid 5-alpha-reductase DET2"
FT /id="PRO_0000418515"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 257 AA; 29802 MW; 6D3DA1537BCC1CB7 CRC64;
MFSSDENLFN FIVFFILVMA FPTFILCQFF TSPYGKHYTS ADSGTTISPP IAWAFMESPT
LWLTIIVFRL GKNYTNPLAF LLISPYLFHY TNRTIIYPLR LRSRNTKNNF PLNIAVTAFI
FNLLNAYIQS RWVSHYANYQ EDDWFWVRFG IGLVIFGSGM LLNIWADGVL LGLKSQGGGY
KIPRGGLFDY VSSPNYLGEI MEWLGWALMT WSWAGLAFFV YTCANLVPRA VSNHKWYLQK
FGEDYPKNRK AVFPFLY
