Q55320 · ALPH_SYNE7
- ProteinAlkaline phosphatase PhoV
- GenephoV
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids550 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Alkaline phosphatase with broad substrate specificity.
Catalytic activity
- a phosphate monoester + H2O = an alcohol + phosphate
Cofactor
Note: Binds 2 Zn2+ ions.
Activity regulation
Subject to competitive inhibition by phosphate. Inhibited by manganese. Magnesium mildly increases enzyme activity when the zinc concentration is suboptimal. Optimal activity is dependent on the presence of 0.01-2% Triton X-100. Triton X-100 at a concentration of 0.05% increases the activity about fivefold relative to that in its absence. The enzyme is even active in Triton X-100 concentrations up to 80%. 50% inhibition by 4 mM EDTA and 50% inhibition by 48 mM sodium citrate.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.1 mM | 4-nitrophenyl phosphate | |||||
1 mM | ATP | |||||
0.5 mM | ADP | |||||
1.5 mM | AMP | |||||
1.9 mM | D-glucose 6-phosphate | |||||
1.4 mM | fructose 1,6-phosphate | |||||
2.3 mM | fructose 6-phosphate | |||||
3.8 mM | fructose 1-phosphate | |||||
1.9 mM | 3-phosphoglycerate | |||||
2.4 mM | 3-phosphocreatine |
pH Dependence
Optimum pH is 7-10. Activity on 4-nitrophenyl phosphate is observed between pH 6 and pH 11.
Temperature Dependence
Heat-labile. Activity increases with temperature between 15 and 35 degrees Celsius and decreases with further heating. No activity at 65 degrees Celsius. Preincubation for 10 minutes at 50 or 60 degrees Celsius causes 50% or 100% inactivation, respectively. Heat-inactivated enzyme cannot be renaturated.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 48 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 89 | Phosphothreonine intermediate | ||||
Sequence: T | ||||||
Binding site | 89 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 110 | substrate | ||||
Sequence: N | ||||||
Binding site | 171-173 | substrate | ||||
Sequence: KDR | ||||||
Binding site | 313 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 317 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 360 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 361 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 491 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Gram-negative-bacterium-type cell wall | |
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
Molecular Function | alkaline phosphatase activity | |
Molecular Function | glucose-6-phosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | phosphoglycerate phosphatase activity | |
Molecular Function | sugar-phosphatase activity | |
Molecular Function | zinc ion binding | |
Biological Process | fructose 6-phosphate metabolic process | |
Biological Process | phosphocreatine metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlkaline phosphatase PhoV
- EC number
- Short namesAPase PhoV
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Synechococcales > Synechococcaceae > Synechococcus
Accessions
- Primary accessionQ55320
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Lipid-anchor
Cell inner membrane ; Peripheral membrane protein
Note: Associated with the periplasmic side of the inner membrane.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MKIKLLCISLAVLFCSSANA | ||||||
Chain | PRO_0000425537 | 21-550 | Alkaline phosphatase PhoV | |||
Sequence: QKKQAKVQPSVFPQTVARPKLVVGMVIDQMRWDYLYRFYARYGNGGFKRLINEGFSAENTLIPYTPTLTACGHSSIYTGSVPAINGIIGNNWFDPQLGRDVYCVEDKSVKTVGSSSNEGLMSPKNLLVTTVTDELRMATNFRSKVISVSIKDRGAILPGGHTANGAYWYDDMTGSFISSTHYMQQLPTWVNDFNAQRLPNKYFEQDWNTLYPIETYTESTADAKPYERTFKGAKTSSFPHLFKQYANKNYSMMASMPQGNSFTLEFAKAAIPAEKLGQTGNTDFLAVSLSSTDYVGHQFGPNSIELEDTYLRLDKDLEDFFNYLDKTIGKGNYLLFLTADHGATHVPGFLRNKMPGGRLLLKVQTDLDSLIFNEFKVRCNFTIINNQVIFDTDAIKEAKADYAKIKQSTIDYLVKQDGVLNAVDIKNMGAVTIPQEIKNKIINGYNARRSGDVYIILDAGWYPTLTPGTGHAAWNPYDSHIPALFMGWGVKPGKTNKEYYMSDIAPTVSALLHIQQPSGSIGKVITDLLK |
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length550
- Mass (Da)61,325
- Last updated1996-11-01 v1
- ChecksumB3D58CF18FCFD483