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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)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
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 lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

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

  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 – 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

        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...

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: January 7, 2015
This is version 50 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 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.