Q93WP4 · PEPP_ALLCE
- ProteinPhosphoenolpyruvate phosphatase
- GeneACPEPP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids481 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phosphoenolpyruvate phosphatase that probably operates in the vacuole to release phosphate from phosphoenolpyruvate (PEP) under phosphorus starvation.
Catalytic activity
- H2O + phosphoenolpyruvate = phosphate + pyruvate
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.44 mM | phosphoenolpyruvate | |||||
3.72 mM | fructose 6-phosphate | |||||
1.47 mM | glucose 6-phosphate | |||||
1.6 mM | p-nitrophenylphosphate | |||||
1.51 mM | ATP | |||||
2.69 mM | ADP | |||||
1.36 mM | phytic acid |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
240 μmol/min/mg | toward phosphoenolpyruvate | ||||
242 μmol/min/mg | toward fructose 6-phosphate | ||||
374 μmol/min/mg | toward glucose 6-phosphate | ||||
279 μmol/min/mg | toward p-nitrophenylphosphate | ||||
349 μmol/min/mg | toward ATP | ||||
510 μmol/min/mg | toward ADP | ||||
178 μmol/min/mg | toward phytic acid |
pH Dependence
Optimum pH is 7.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 168 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 195 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 195 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 198 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 232 | substrate | ||||
Sequence: N | ||||||
Binding site | 232 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 317 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 327 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 354 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 354-356 | substrate | ||||
Sequence: HVH | ||||||
Binding site | 356 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | vacuolar lumen | |
Molecular Function | acid phosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | phosphoenolpyruvate phosphatase activity | |
Molecular Function | phosphoprotein phosphatase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoenolpyruvate phosphatase
- EC number
- Short namesPEP phosphatase
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Asparagales > Amaryllidaceae > Allioideae > Allieae > Allium
Accessions
- Primary accessionQ93WP4
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-36 | |||||
Sequence: MPIYTSRSCFYLLLFHIILLCSVDKTLCRQTSSFVR | ||||||
Chain | PRO_5000049662 | 37-481 | Phosphoenolpyruvate phosphatase | |||
Sequence: SEFPAVDIPIDSKEFAVPKNQFSPQQVHITQGDYDGKAVIVSWVTFIDPGKSEVVYGTSPNSYDHSAQGKTTNYTYYDYTSGYIHHCLLDKLEYDTKYYYKIGKGDAAREFWFHTPPQIHPDASYTFGIIGDLGQTYNSLSTLEHYMKSKGQTVLFVGDLSYADRYSCNNGTRWDSWGRFVERSVAYQPWIWTVGNHEIEYRPDLGEVFPFRAYLNRYPTPHLASASSSPLWYSIRRASAHIIVLSSYSPFVKYTPQWLWLSEELTRVDREKTPWLIVLMHAPLYNSNEAHYMEGESMRVAFESWFVQYKVDLVFAGHVHAYERSYRISNIVYNITSGNRYPIPDKSAPVYITVGDGGNQEGLAERFSESQPDYSAFRESSYGHSTLELRNRTHAFYQWNRNDDGKHIPVDRIIFRNQYWASNTRRRRLKKTRPSQAVERLISSY | ||||||
Glycosylation | 109 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 206 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 370 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 427 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Structure
Family & Domains
Sequence similarities
Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length481
- Mass (Da)55,970
- Last updated2001-12-01 v1
- Checksum6DA72EB851D7C8FD