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Information on EC 3.1.3.3 - phosphoserine phosphatase and Organism(s) Arabidopsis thaliana and UniProt Accession O82796

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.3 phosphoserine phosphatase
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: O82796 not found.
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
psp, serine/threonine protein phosphatase, phosphoserine phosphatase, pspase, ctd phosphatase fcp1, serb2, serb653, l-phosphoserine phosphatase, 3-phosphoserine phosphatase, ipsp1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-phosphoserine phosphatase
-
-
-
-
CTD phosphatase fcp1
-
-
-
-
O-phosphoserine phosphohydrolase
-
-
-
-
phosphatase, phosphoserine
-
-
-
-
PSPase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
O-phosphoserine phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-73-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
biosynthesis of serine, terminal enzyme in the plastidic pathway
-
-
?
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
?
3-phospho-D-serine + H2O
D-serine + phosphate
show the reaction diagram
-
-
-
-
?
3-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
biosynthesis of serine, terminal enzyme in the plastidic pathway
-
-
?
3-phospho-D-serine + H2O
D-serine + phosphate
show the reaction diagram
-
-
-
-
?
3-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycine
not inhibitory
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5
L-3-phosphoserine
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
enzyme plays a crucial role in embry, pollen and root development
Manually annotated by BRENDA team
-
enzyme plays a crucial role in embry, pollen and root development
Manually annotated by BRENDA team
-
enzyme plays a crucial role in embry, pollen and root development
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme knock-down disturbs nitrogen metabolism but does not disturb glycine and serine synthesis or sulfur assimilation and metabolism. Enzyme knock-down induces additional defense mechanisms against cadmium toxicity
physiological function
-
the embryo-lethal phenotype of isoform psp1 mutants can be complemented with PSP1 cDNA under the control of Pro35S. However, this construct is poorly expressed in the anther tapetum, and does not complement mutant fertility. Microspore development in psp1.1/psp1.1 mutants expressing Pro35S:PSP1 arrest at the polarized stage. The tapetum from these lines displays delayed and irregular development. In addition to embryo death and male sterility, conditional psp1 mutants display a short-root phenotype, which is reverted in the presence of serine
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SERC_ARATH
295
0
32318
Swiss-Prot
Chloroplast (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
x * 37000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37000, SDS-PAGE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ho, C.L.; Noji, M.; Saito, K.
Plastidic pathway of serine biosynthesis. Molecular cloning and expression of 3-phosphoserine phosphatase from Arabidopsis thaliana
J. Biol. Chem.
274
11007-11012
1999
Arabidopsis thaliana (O82796), Arabidopsis thaliana
Manually annotated by BRENDA team
Cascales-Minana, B.; Munoz-Bertomeu, J.; Flores-Tornero, M.; Anoman, A.D.; Pertusa, J.; Alaiz, M.; Osorio, S.; Fernie, A.R.; Segura, J.; Ros, R.
The phosphorylated pathway of serine biosynthesis is essential both for male gametophyte and embryo development and for root growth in Arabidopsis
Plant Cell
25
2084-2101
2013
Arabidopsis thaliana
Manually annotated by BRENDA team
Samuilov, S.; Rademacher, N.; Brilhaus, D.; Flachbart, S.; Arab, L.; Kopriva, S.; Weber, A.P.M.; Mettler-Altmann, T.; Rennenberg, H.
Knock-down of the phosphoserine phosphatase gene effects rather N- than S-metabolism in Arabidopsis thaliana
Front. Plant Sci.
9
1830
2018
Arabidopsis thaliana
Manually annotated by BRENDA team