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Protein

Alkaline phosphatase PhoV

Gene

phoV

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Alkaline phosphatase with broad substrate specificity.1 Publication

Catalytic activityi

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

Cofactori

Zn2+By similarity1 PublicationNote: Binds 2 Zn2+ ions.By similarity1 Publication

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=0.1 mM for 4-nitrophenyl phosphate1 Publication
  2. KM=1.0 mM for ATP1 Publication
  3. KM=0.5 mM for ADP1 Publication
  4. KM=1.5 mM for AMP1 Publication
  5. KM=1.9 mM for D-glucose 6-phosphate1 Publication
  6. KM=1.4 mM for fructose 1,6-phosphate1 Publication
  7. KM=2.3 mM for fructose 6-phosphate1 Publication
  8. KM=3.8 mM for fructose 1-phosphate1 Publication
  9. KM=1.9 mM for 3-phosphoglycerate1 Publication
  10. KM=2.4 mM for 3-phosphocreatine1 Publication

    pH dependencei

    Optimum pH is 7-10. Activity on 4-nitrophenyl phosphate is observed between pH 6 and pH 11.1 Publication

    Temperature dependencei

    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.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi48Zinc 1By similarity1
    Active sitei89Phosphothreonine intermediateBy similarity1
    Metal bindingi89Zinc 1By similarity1
    Binding sitei110SubstrateBy similarity1
    Metal bindingi313Zinc 2By similarity1
    Metal bindingi317Zinc 2; via tele nitrogenBy similarity1
    Metal bindingi360Zinc 1By similarity1
    Metal bindingi361Zinc 1; via tele nitrogenBy similarity1
    Metal bindingi491Zinc 2; via tele nitrogenBy similarity1

    GO - Molecular functioni

    • alkaline phosphatase activity Source: UniProtKB
    • glucose-6-phosphatase activity Source: UniProtKB
    • metal ion binding Source: UniProtKB
    • nucleotide phosphatase activity, acting on free nucleotides Source: UniProtKB
    • phosphoglycerate phosphatase activity Source: UniProtKB
    • sugar-phosphatase activity Source: UniProtKB
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • dephosphorylation Source: UniProtKB
    • fructose 6-phosphate metabolic process Source: UniProtKB
    • phosphocreatine metabolic process Source: UniProtKB
    • phosphorylated carbohydrate dephosphorylation Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alkaline phosphatase PhoV1 PublicationImported (EC:3.1.3.11 Publication)
    Short name:
    APase PhoV1 Publication
    Gene namesi
    Name:phoVImported
    OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
    Taxonomic identifieri1140 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus

    Subcellular locationi

    • Cell inner membrane 1 Publication; Lipid-anchor Curated1 Publication; Periplasmic side 1 Publication
    • Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication; Periplasmic side 1 Publication

    • Note: Associated with the periplasmic side of the inner membrane.1 Publication

    GO - Cellular componenti

    • Gram-negative-bacterium-type cell wall Source: UniProtKB
    • plasma membrane Source: UniProtKB-SubCell
    • side of membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 20Sequence analysisAdd BLAST20
    ChainiPRO_000042553721 – 550Alkaline phosphatase PhoVSequence analysisAdd BLAST530

    Keywords - PTMi

    Lipoprotein, Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ55320.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni171 – 173Substrate bindingBy similarity3

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.720.10. 2 hits.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR026263. Alkaline_phosphatase_prok.
    IPR002591. Phosphodiest/P_Trfase.
    [Graphical view]
    PfamiPF01663. Phosphodiest. 1 hit.
    [Graphical view]
    PIRSFiPIRSF031924. Pi-irrepressible_AP. 1 hit.
    SUPFAMiSSF53649. SSF53649. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q55320-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKIKLLCISL AVLFCSSANA QKKQAKVQPS VFPQTVARPK LVVGMVIDQM
    60 70 80 90 100
    RWDYLYRFYA RYGNGGFKRL INEGFSAENT LIPYTPTLTA CGHSSIYTGS
    110 120 130 140 150
    VPAINGIIGN NWFDPQLGRD VYCVEDKSVK TVGSSSNEGL MSPKNLLVTT
    160 170 180 190 200
    VTDELRMATN FRSKVISVSI KDRGAILPGG HTANGAYWYD DMTGSFISST
    210 220 230 240 250
    HYMQQLPTWV NDFNAQRLPN KYFEQDWNTL YPIETYTEST ADAKPYERTF
    260 270 280 290 300
    KGAKTSSFPH LFKQYANKNY SMMASMPQGN SFTLEFAKAA IPAEKLGQTG
    310 320 330 340 350
    NTDFLAVSLS STDYVGHQFG PNSIELEDTY LRLDKDLEDF FNYLDKTIGK
    360 370 380 390 400
    GNYLLFLTAD HGATHVPGFL RNKMPGGRLL LKVQTDLDSL IFNEFKVRCN
    410 420 430 440 450
    FTIINNQVIF DTDAIKEAKA DYAKIKQSTI DYLVKQDGVL NAVDIKNMGA
    460 470 480 490 500
    VTIPQEIKNK IINGYNARRS GDVYIILDAG WYPTLTPGTG HAAWNPYDSH
    510 520 530 540 550
    IPALFMGWGV KPGKTNKEYY MSDIAPTVSA LLHIQQPSGS IGKVITDLLK
    Length:550
    Mass (Da):61,325
    Last modified:November 1, 1996 - v1
    Checksum:iB3D58CF18FCFD483
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z48801 Genomic DNA. Translation: CAA88739.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z48801 Genomic DNA. Translation: CAA88739.1.

    3D structure databases

    ProteinModelPortaliQ55320.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    Gene3Di3.40.720.10. 2 hits.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR026263. Alkaline_phosphatase_prok.
    IPR002591. Phosphodiest/P_Trfase.
    [Graphical view]
    PfamiPF01663. Phosphodiest. 1 hit.
    [Graphical view]
    PIRSFiPIRSF031924. Pi-irrepressible_AP. 1 hit.
    SUPFAMiSSF53649. SSF53649. 2 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiALPH_SYNE7
    AccessioniPrimary (citable) accession number: Q55320
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 19, 2014
    Last sequence update: November 1, 1996
    Last modified: November 2, 2016
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.