Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Steroid 5-alpha-reductase DET2

Gene

DET2

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in a reduction step in the biosynthesis of the plant steroid, brassinolide. Can use progesterone, testosterone, androstenedione and campestenone as substrate.1 Publication

Catalytic activityi

A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta(4)-steroid + NADPH.1 Publication

Enzyme regulationi

Repressed by steroid (4-MA, VG106, PD91, PD17, Finasteride) and non-steroid (AS601811, AFA27, AFA76, AFA131, AFA192) inhibitors; steroid inhibitors are generally more efficient.1 Publication

Kineticsi

  1. KM=0.75 µM for progesterone (expressed in COS-7 cells, PubMed:15993049)1 Publication
  2. KM=26 µM for androstenedione (expressed in COS-7 cells, PubMed:15993049)1 Publication
  3. KM=40 µM for testosterone (expressed in COS-7 cells, PubMed:15993049)1 Publication
  1. Vmax=0.34 nmol/min/mg enzyme with progesterone as substrate (expressed in COS-7 cells, PubMed:15993049)1 Publication
  2. Vmax=0.32 nmol/min/mg enzyme with androstenedione as substrate (expressed in COS-7 cells, PubMed:15993049)1 Publication
  3. Vmax=0.21 nmol/min/mg enzyme with testosterone as substrate (expressed in COS-7 cells, PubMed:15993049)1 Publication

Pathway:ibrassinosteroid biosynthesis

This protein is involved in the pathway brassinosteroid biosynthesis, which is part of Plant hormone biosynthesis.
View all proteins of this organism that are known to be involved in the pathway brassinosteroid biosynthesis and in Plant hormone biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • brassinosteroid biosynthetic process Source: UniProtKB-UniPathway
  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.3.1.22. 3101.
UniPathwayiUPA00381.

Names & Taxonomyi

Protein namesi
Recommended name:
Steroid 5-alpha-reductase DET2 (EC:1.3.1.22)
Short name:
LeDET2
Gene namesi
Name:DET2
OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifieri4081 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
ProteomesiUP000004994 Componenti: Chromosome 10

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121HelicalSequence AnalysisAdd
BLAST
Transmembranei47 – 6721HelicalSequence AnalysisAdd
BLAST
Transmembranei78 – 9720HelicalSequence AnalysisAdd
BLAST
Transmembranei110 – 13021HelicalSequence AnalysisAdd
BLAST
Transmembranei151 – 17121HelicalSequence AnalysisAdd
BLAST
Transmembranei200 – 22021HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257Steroid 5-alpha-reductase DET2PRO_0000418515Add
BLAST

Expressioni

Tissue specificityi

Mostly expressed in leaves and hypocotyls and, to a lower extent, in stems, cotyledons, roots, seeds and callus.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi4081.Solyc10g086500.1.1.

Family & Domainsi

Sequence similaritiesi

Belongs to the steroid 5-alpha reductase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiQ5K2N1.
KOiK09591.
OMAiRGWFFPL.

Family and domain databases

InterProiIPR016636. 3-oxo-5-alpha-steroid_4-DH.
IPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015596. 5_alpha-SR2. 1 hit.
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5K2N1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSSDENLFN FIVFFILVMA FPTFILCQFF TSPYGKHYTS ADSGTTISPP
60 70 80 90 100
IAWAFMESPT LWLTIIVFRL GKNYTNPLAF LLISPYLFHY TNRTIIYPLR
110 120 130 140 150
LRSRNTKNNF PLNIAVTAFI FNLLNAYIQS RWVSHYANYQ EDDWFWVRFG
160 170 180 190 200
IGLVIFGSGM LLNIWADGVL LGLKSQGGGY KIPRGGLFDY VSSPNYLGEI
210 220 230 240 250
MEWLGWALMT WSWAGLAFFV YTCANLVPRA VSNHKWYLQK FGEDYPKNRK

AVFPFLY
Length:257
Mass (Da):29,802
Last modified:February 15, 2005 - v1
Checksum:i6D3DA1537BCC1CB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ786362 mRNA. Translation: CAH05260.1.
RefSeqiNP_001234040.1. NM_001247111.1.
UniGeneiLes.5994.

Genome annotation databases

EnsemblPlantsiSolyc10g086500.1.1; Solyc10g086500.1.1; Solyc10g086500.1.
GeneIDi543801.
KEGGisly:543801.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ786362 mRNA. Translation: CAH05260.1.
RefSeqiNP_001234040.1. NM_001247111.1.
UniGeneiLes.5994.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4081.Solyc10g086500.1.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiSolyc10g086500.1.1; Solyc10g086500.1.1; Solyc10g086500.1.
GeneIDi543801.
KEGGisly:543801.

Phylogenomic databases

InParanoidiQ5K2N1.
KOiK09591.
OMAiRGWFFPL.

Enzyme and pathway databases

UniPathwayiUPA00381.
BRENDAi1.3.1.22. 3101.

Family and domain databases

InterProiIPR016636. 3-oxo-5-alpha-steroid_4-DH.
IPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015596. 5_alpha-SR2. 1 hit.
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "5alpha-Reductase activity in Lycopersicon esculentum: cloning and functional characterization of LeDET2 and evidence of the presence of two isoenzymes."
    Rosati F., Bardazzi I., De Blasi P., Simi L., Scarpi D., Guarna A., Serio M., Racchi M.L., Danza G.
    J. Steroid Biochem. Mol. Biol. 96:287-299(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: cv. Saint Pierre.
    Tissue: Leaf.

Entry informationi

Entry nameiDET2_SOLLC
AccessioniPrimary (citable) accession number: Q5K2N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: February 15, 2005
Last modified: July 22, 2015
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.