Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q55320

- ALPH_SYNE7

UniProt

Q55320 - ALPH_SYNE7

Protein

Alkaline phosphatase PhoV

Gene

phoV

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Alkaline phosphatase with broad substrate specificity.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc 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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi48 – 481Zinc 1By similarity
    Active sitei89 – 891Phosphothreonine intermediateBy similarity
    Metal bindingi89 – 891Zinc 1By similarity
    Binding sitei110 – 1101SubstrateBy similarity
    Metal bindingi313 – 3131Zinc 2By similarity
    Metal bindingi317 – 3171Zinc 2; via tele nitrogenBy similarity
    Metal bindingi360 – 3601Zinc 1By similarity
    Metal bindingi361 – 3611Zinc 1; via tele nitrogenBy similarity
    Metal bindingi491 – 4911Zinc 2; via tele nitrogenBy similarity

    GO - Molecular functioni

    1. alkaline phosphatase activity Source: UniProtKB
    2. glucose-6-phosphatase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB
    4. nucleotide phosphatase activity, acting on free nucleotides Source: UniProtKB
    5. phosphoglycerate phosphatase activity Source: UniProtKB
    6. sugar-phosphatase activity Source: UniProtKB
    7. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. dephosphorylation Source: UniProtKB
    2. fructose 6-phosphate metabolic process Source: UniProtKB
    3. phosphocreatine metabolic process Source: UniProtKB
    4. phosphorylated carbohydrate dephosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alkaline phosphatase PhoVImported1 Publication (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 lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

    Subcellular locationi

    Cell inner membrane 1 Publication; Lipid-anchor 1 PublicationCurated; 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

    1. Gram-negative-bacterium-type cell wall Source: UniProtKB
    2. plasma membrane Source: UniProtKB-SubCell
    3. side of membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 550530Alkaline phosphatase PhoVSequence AnalysisPRO_0000425537Add
    BLAST

    Keywords - PTMi

    Lipoprotein, Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ55320.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni171 – 1733Substrate bindingBy similarity

    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

    MKIKLLCISL AVLFCSSANA QKKQAKVQPS VFPQTVARPK LVVGMVIDQM    50
    RWDYLYRFYA RYGNGGFKRL INEGFSAENT LIPYTPTLTA CGHSSIYTGS 100
    VPAINGIIGN NWFDPQLGRD VYCVEDKSVK TVGSSSNEGL MSPKNLLVTT 150
    VTDELRMATN FRSKVISVSI KDRGAILPGG HTANGAYWYD DMTGSFISST 200
    HYMQQLPTWV NDFNAQRLPN KYFEQDWNTL YPIETYTEST ADAKPYERTF 250
    KGAKTSSFPH LFKQYANKNY SMMASMPQGN SFTLEFAKAA IPAEKLGQTG 300
    NTDFLAVSLS STDYVGHQFG PNSIELEDTY LRLDKDLEDF FNYLDKTIGK 350
    GNYLLFLTAD HGATHVPGFL RNKMPGGRLL LKVQTDLDSL IFNEFKVRCN 400
    FTIINNQVIF DTDAIKEAKA DYAKIKQSTI DYLVKQDGVL NAVDIKNMGA 450
    VTIPQEIKNK IINGYNARRS GDVYIILDAG WYPTLTPGTG HAAWNPYDSH 500
    IPALFMGWGV KPGKTNKEYY MSDIAPTVSA LLHIQQPSGS IGKVITDLLK 550
    Length:550
    Mass (Da):61,325
    Last modified:November 1, 1996 - v1
    Checksum:iB3D58CF18FCFD483
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z48801 Genomic DNA. Translation: CAA88739.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z48801 Genomic DNA. Translation: CAA88739.1 .

    3D structure databases

    ProteinModelPortali Q55320.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.720.10. 2 hits.
    InterProi IPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR026263. Alkaline_phosphatase_prok.
    IPR002591. Phosphodiest/P_Trfase.
    [Graphical view ]
    Pfami PF01663. Phosphodiest. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF031924. Pi-irrepressible_AP. 1 hit.
    SUPFAMi SSF53649. SSF53649. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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 79421 Publication.

    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: October 1, 2014
    This is version 47 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program