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Q55320

- ALPH_SYNE7

UniProt

Q55320 - ALPH_SYNE7

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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

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.1 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 ATP
  3. KM=0.5 mM for ADP
  4. KM=1.5 mM for AMP
  5. KM=1.9 mM for D-glucose 6-phosphate
  6. KM=1.4 mM for fructose 1,6-phosphate
  7. KM=2.3 mM for fructose 6-phosphate
  8. KM=3.8 mM for fructose 1-phosphate
  9. KM=1.9 mM for 3-phosphoglycerate
  10. KM=2.4 mM for 3-phosphocreatine

pH dependencei

Optimum pH is 7-10. Activity on 4-nitrophenyl phosphate is observed between pH 6 and pH 11.

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi48 – 481Zinc 1 By similarity
Active sitei89 – 891Phosphothreonine intermediate By similarity
Metal bindingi89 – 891Zinc 1 By similarity
Binding sitei110 – 1101Substrate By similarity
Metal bindingi313 – 3131Zinc 2 By similarity
Metal bindingi317 – 3171Zinc 2; via tele nitrogen By similarity
Metal bindingi360 – 3601Zinc 1 By similarity
Metal bindingi361 – 3611Zinc 1; via tele nitrogen By similarity
Metal bindingi491 – 4911Zinc 2; via tele nitrogen By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alkaline phosphatase PhoV (EC:3.1.3.1)
Short name:
APase PhoV
Gene namesi
Name:phoV
OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifieri1140 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Subcellular locationi

Cell inner membrane; Lipid-anchor Reviewed prediction; Periplasmic side. Cell inner membrane; Peripheral membrane protein; Periplasmic side
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
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed prediction
Add
BLAST
Chaini21 – 550530Alkaline phosphatase PhoV
PRO_0000425537Add
BLAST

Keywords - PTMi

Lipoprotein, Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ55320.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni171 – 1733Substrate binding By 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

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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...

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 7942.

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: April 16, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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