O82796 · SERC_ARATH
- ProteinPhosphoserine phosphatase, chloroplastic
- GenePSP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids295 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the last step in the plastidial phosphorylated pathway of serine biosynthesis (PPSB). The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. Required for embryo, pollen and root development. May be required preferentially for serine biosynthesis in non-photosynthetic tissues.
Catalytic activity
- H2O + O-phospho-L-serine = L-serine + phosphateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Activity regulation
Approximately 60% inhibition of PSP activity is observed in presence of 10 mM serine.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.5 mM | 3-phosphoserine | 7.5 | 30 |
Pathway
Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 89 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 89 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 91 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 91 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 98 | substrate | ||||
Sequence: E | ||||||
Binding site | 134 | substrate | ||||
Sequence: R | ||||||
Binding site | 178-179 | substrate | ||||
Sequence: SG | ||||||
Binding site | 227 | substrate | ||||
Sequence: K | ||||||
Binding site | 248 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | plastid | |
Molecular Function | L-phosphoserine phosphatase activity | |
Molecular Function | magnesium ion binding | |
Biological Process | embryo development ending in seed dormancy | |
Biological Process | L-serine biosynthetic process | |
Biological Process | L-serine metabolic process | |
Biological Process | pollen development | |
Biological Process | root development | |
Biological Process | sulfur amino acid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoserine phosphatase, chloroplastic
- EC number
- Short namesPSP; PSPase
- 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 accessionO82796
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Embryo lethal when homozygous.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-54 | Chloroplast | ||||
Sequence: MEALTTSRVVPVQVPCRKLSSLFANFSCLELRRYPCRGLVSIMNHPKLLRPVTA | ||||||
Chain | PRO_0000032375 | 55-295 | Phosphoserine phosphatase, chloroplastic | |||
Sequence: SVQPHELSTLGHEGNIVPSKEILDLWRSVEAVCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVEEYLDKRPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPRENIFANNLLFGNSGEFLGFDENEPTSRSGGKAKAVQQIRKGRLYKTMAMIGDGATDLEARKPGGADLFICYAGVQLREAVAANADWLIFKFESLINSLD |
Proteomic databases
Expression
Tissue specificity
Ubiquitous. Mainly expressed in shoot and root meristems, vasculature, pollen, anthers, carpels and seeds.
Induction
Up-regulated in aerial parts by 8 hours exposure to darkness, whereas longer exposure down-regulate expression in both roots and aerial parts.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length295
- Mass (Da)32,318
- Last updated2005-04-26 v2
- ChecksumF14C95E636F7745E
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8AMY1 | A0A1P8AMY1_ARATH | PSP | 279 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 266 | in Ref. 1; BAA33806/BAA33807 | ||||
Sequence: C → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB018408 EMBL· GenBank· DDBJ | BAA33806.1 EMBL· GenBank· DDBJ | mRNA | ||
AB018409 EMBL· GenBank· DDBJ | BAA33807.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC026238 EMBL· GenBank· DDBJ | AAF98410.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE29738.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY065351 EMBL· GenBank· DDBJ | AAL38792.1 EMBL· GenBank· DDBJ | mRNA | ||
AY096687 EMBL· GenBank· DDBJ | AAM20321.1 EMBL· GenBank· DDBJ | mRNA | ||
AY087385 EMBL· GenBank· DDBJ | AAM64935.1 EMBL· GenBank· DDBJ | mRNA |