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Q55320 (ALPH_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Alkaline phosphatase PhoV

Short name=APase PhoV
EC=3.1.3.1
Gene names
Name:phoV
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alkaline phosphatase with broad substrate specificity. Ref.1

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.1

Cofactor

Binds 2 zinc ions. Ref.1

Enzyme 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. Ref.1

Subcellular location

Cell inner membrane; Lipid-anchor Potential; Periplasmic side. Cell inner membrane; Peripheral membrane protein; Periplasmic side. Note: Associated with the periplasmic side of the inner membrane. Ref.1

Biophysicochemical properties

Kinetic parameters:

KM=0.1 mM for 4-nitrophenyl phosphate Ref.1

KM=1.0 mM for ATP

KM=0.5 mM for ADP

KM=1.5 mM for AMP

KM=1.9 mM for D-glucose 6-phosphate

KM=1.4 mM for fructose 1,6-phosphate

KM=2.3 mM for fructose 6-phosphate

KM=3.8 mM for fructose 1-phosphate

KM=1.9 mM for 3-phosphoglycerate

KM=2.4 mM for 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 550530Alkaline phosphatase PhoV
PRO_0000425537

Regions

Region171 – 1733Substrate binding By similarity

Sites

Active site891Phosphothreonine intermediate By similarity
Metal binding481Zinc 1 By similarity
Metal binding891Zinc 1 By similarity
Metal binding3131Zinc 2 By similarity
Metal binding3171Zinc 2; via tele nitrogen By similarity
Metal binding3601Zinc 1 By similarity
Metal binding3611Zinc 1; via tele nitrogen By similarity
Metal binding4911Zinc 2; via tele nitrogen By similarity
Binding site1101Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q55320 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B3D58CF18FCFD483

FASTA55061,325
        10         20         30         40         50         60 
MKIKLLCISL AVLFCSSANA QKKQAKVQPS VFPQTVARPK LVVGMVIDQM RWDYLYRFYA 

        70         80         90        100        110        120 
RYGNGGFKRL INEGFSAENT LIPYTPTLTA CGHSSIYTGS VPAINGIIGN NWFDPQLGRD 

       130        140        150        160        170        180 
VYCVEDKSVK TVGSSSNEGL MSPKNLLVTT VTDELRMATN FRSKVISVSI KDRGAILPGG 

       190        200        210        220        230        240 
HTANGAYWYD DMTGSFISST HYMQQLPTWV NDFNAQRLPN KYFEQDWNTL YPIETYTEST 

       250        260        270        280        290        300 
ADAKPYERTF KGAKTSSFPH LFKQYANKNY SMMASMPQGN SFTLEFAKAA IPAEKLGQTG 

       310        320        330        340        350        360 
NTDFLAVSLS STDYVGHQFG PNSIELEDTY LRLDKDLEDF FNYLDKTIGK GNYLLFLTAD 

       370        380        390        400        410        420 
HGATHVPGFL RNKMPGGRLL LKVQTDLDSL IFNEFKVRCN FTIINNQVIF DTDAIKEAKA 

       430        440        450        460        470        480 
DYAKIKQSTI DYLVKQDGVL NAVDIKNMGA VTIPQEIKNK IINGYNARRS GDVYIILDAG 

       490        500        510        520        530        540 
WYPTLTPGTG HAAWNPYDSH IPALFMGWGV KPGKTNKEYY MSDIAPTVSA LLHIQQPSGS 

       550 
IGKVITDLLK 

« Hide

References

[1]"The cyanobacterium Synechococcus sp. strain PCC7942 contains a second alkaline phosphatase encoded by phoV."
Wagner K.U., Masepohl B., Pistorius E.K.
Microbiology 141:3049-3058(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
Strain: PCC 7942.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z48801 Genomic DNA. Translation: CAA88739.1.

3D structure databases

ProteinModelPortalQ55320.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.720.10. 2 hits.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR026263. Alkaline_phosphatase_prok.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
PfamPF01663. Phosphodiest. 1 hit.
[Graphical view]
PIRSFPIRSF031924. Pi-irrepressible_AP. 1 hit.
SUPFAMSSF53649. SSF53649. 2 hits.
ProtoNetSearch...

Entry information

Entry nameALPH_SYNE7
AccessionPrimary (citable) accession number: Q55320
Entry history
Integrated into UniProtKB/Swiss-Prot: February 19, 2014
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program