Q55320 · ALPH_SYNE7

Function

function

Alkaline phosphatase with broad substrate specificity.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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 mM4-nitrophenyl phosphate
1 mMATP
0.5 mMADP
1.5 mMAMP
1.9 mMD-glucose 6-phosphate
1.4 mMfructose 1,6-phosphate
2.3 mMfructose 6-phosphate
3.8 mMfructose 1-phosphate
1.9 mM3-phosphoglycerate
2.4 mM3-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.

TypeIDPosition(s)Description
Binding site48Zn2+ 1 (UniProtKB | ChEBI)
Active site89Phosphothreonine intermediate
Binding site89Zn2+ 1 (UniProtKB | ChEBI)
Binding site110substrate
Binding site171-173substrate
Binding site313Zn2+ 2 (UniProtKB | ChEBI)
Binding site317Zn2+ 2 (UniProtKB | ChEBI)
Binding site360Zn2+ 1 (UniProtKB | ChEBI)
Binding site361Zn2+ 1 (UniProtKB | ChEBI)
Binding site491Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular ComponentGram-negative-bacterium-type cell wall
Cellular Componentplasma membrane
Cellular Componentside of membrane
Molecular Functionalkaline phosphatase activity
Molecular Functionglucose-6-phosphatase activity
Molecular Functionmetal ion binding
Molecular Functionphosphoglycerate phosphatase activity
Molecular Functionsugar-phosphatase activity
Molecular Functionzinc ion binding
Biological Processfructose 6-phosphate metabolic process
Biological Processphosphocreatine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alkaline phosphatase PhoV
  • EC number
  • Short names
    APase PhoV

Gene names

    • Name
      phoV

Organism names

Accessions

  • Primary accession
    Q55320

Subcellular Location

Cell inner membrane
; Lipid-anchor
Cell inner membrane
; Peripheral membrane protein
Note: Associated with the periplasmic side of the inner membrane.

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_000042553721-550Alkaline phosphatase PhoV

Keywords

Structure

Family & Domains

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    550
  • Mass (Da)
    61,325
  • Last updated
    1996-11-01 v1
  • Checksum
    B3D58CF18FCFD483
MKIKLLCISLAVLFCSSANAQKKQAKVQPSVFPQTVARPKLVVGMVIDQMRWDYLYRFYARYGNGGFKRLINEGFSAENTLIPYTPTLTACGHSSIYTGSVPAINGIIGNNWFDPQLGRDVYCVEDKSVKTVGSSSNEGLMSPKNLLVTTVTDELRMATNFRSKVISVSIKDRGAILPGGHTANGAYWYDDMTGSFISSTHYMQQLPTWVNDFNAQRLPNKYFEQDWNTLYPIETYTESTADAKPYERTFKGAKTSSFPHLFKQYANKNYSMMASMPQGNSFTLEFAKAAIPAEKLGQTGNTDFLAVSLSSTDYVGHQFGPNSIELEDTYLRLDKDLEDFFNYLDKTIGKGNYLLFLTADHGATHVPGFLRNKMPGGRLLLKVQTDLDSLIFNEFKVRCNFTIINNQVIFDTDAIKEAKADYAKIKQSTIDYLVKQDGVLNAVDIKNMGAVTIPQEIKNKIINGYNARRSGDVYIILDAGWYPTLTPGTGHAAWNPYDSHIPALFMGWGVKPGKTNKEYYMSDIAPTVSALLHIQQPSGSIGKVITDLLK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z48801
EMBL· GenBank· DDBJ
CAA88739.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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