Q9STX2 · VEP1_ARATH
- Protein3-oxo-Delta(4,5)-steroid 5-beta-reductase
- GeneVEP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids388 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in vascular strand development. Catalyzes the stereospecific conversion of progesterone to 5-beta-pregnane-3,20-dione. Can use progesterone, testosterone, 21-acetyl cortexone, 2-cyclohexenone, but-1-en-3-one, ethyl acrylate, ethylmethacrylate, cortisone and canarigenone as substrates, lower activity with 3-methyl-2-cyclohexenone and 3,5,5-trimethyl-2-cyclohexenone as substrate, and no activity with canarigenin, canarigenin digitoxoside and pregnenolone. May be involved in the formation of 5-beta phytoecdysteroids.
Catalytic activity
- 5beta-cholestan-3-one + NADP+ = cholest-4-en-3-one + H+ + NADPH
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
268 μM | progesterone | |||||
755 μM | cortisol | |||||
1423 μM | 4-androstene-3,17-dione | |||||
764 μM | cortexone | |||||
5 μM | NADPH | |||||
116 μM | 2-cyclohexen-1-one |
kcat is 10.11 min-1 with progesterone as substrate. kcat is 66.85 min-1 with 2-cyclohexen-1-one as substrate.
pH Dependence
Optimum pH is 8.0.
Temperature Dependence
Optimum temperature is 45 degrees Celsius.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 35-37 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: TGI | ||||||
Binding site | 63-64 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: RR | ||||||
Binding site | 81-82 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: DV | ||||||
Binding site | 105 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 143 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 147 | |||||
Sequence: K | ||||||
Active site | 178 | |||||
Sequence: Y | ||||||
Binding site | 178 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 205 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 212-214 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SLM |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | Delta4-3-oxosteroid 5beta-reductase activity | |
Molecular Function | enone reductase activity | |
Molecular Function | protein dimerization activity | |
Biological Process | response to wounding | |
Biological Process | steroid metabolic process | |
Biological Process | xylem and phloem pattern formation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-oxo-Delta(4,5)-steroid 5-beta-reductase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9STX2
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000419904 | 2-388 | 3-oxo-Delta(4,5)-steroid 5-beta-reductase | |||
Sequence: SWWWAGAIGAAKKKLDEDEPSQSFESVALIIGVTGIVGNSLAEILPLSDTPGGPWKVYGVARRPRPTWNADHPIDYIQCDVSDAEDTRSKLSPLTDVTHVFYVTWTNRESESENCEANGSMLRNVLQAIIPYAPNLRHVCLQTGTKHYLGPFTNVDGPRHDPPFTEDMPRLQIQNFYYTQEDILFEEIKKIETVTWSIHRPNMIFGFSPYSLMNIVGTLCVYAAICKHEGSPLLFPGSKKAWEGFMTASDADLIAEQQIWAAVDPYAKNEAFNCNNADIFKWKHLWKILAEQFGIEEYGFEEGKNLGLVEMMKGKERVWEEMVKENQLQEKKLEEVGVWWFADVILGVEGMIDSMNKSKEYGFLGFRNSNNSFISWIDKYKAFKIVP |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in roots, stems, leaves, flowers, seeds and siliques. Expressed in the vascular bundles.
Induction
Up-regulated by wounding. Not induced by drought, high salt, low temperature or herbicide treatment.
Gene expression databases
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9STX2-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length388
- Mass (Da)44,230
- Last updated2000-05-01 v1
- Checksum5ED9D6C12330A161
Q9STX2-2
- Name2
- Differences from canonical
- 13-13: Missing
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 1; CAA68126 | ||||
Sequence: S → R | ||||||
Alternative sequence | VSP_044368 | 13 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 36 | in Ref. 1; CAA68126 | ||||
Sequence: G → A | ||||||
Sequence conflict | 192 | in Ref. 1; CAA68126 | ||||
Sequence: I → T | ||||||
Sequence conflict | 359 | in Ref. 1; CAA68126 | ||||
Sequence: S → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X99793 EMBL· GenBank· DDBJ | CAA68126.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
EF579963 EMBL· GenBank· DDBJ | ABU55811.1 EMBL· GenBank· DDBJ | mRNA | ||
AL078637 EMBL· GenBank· DDBJ | CAB45057.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL161561 EMBL· GenBank· DDBJ | CAB79332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE84868.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE84869.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY062451 EMBL· GenBank· DDBJ | AAL32529.1 EMBL· GenBank· DDBJ | mRNA | ||
BT008479 EMBL· GenBank· DDBJ | AAP37838.1 EMBL· GenBank· DDBJ | mRNA | ||
AY087323 EMBL· GenBank· DDBJ | AAM64873.1 EMBL· GenBank· DDBJ | mRNA |