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Alkaline phosphatase PhoV (APase PhoV) (EC 3.1.3.1)

 ALPH_SYNE7              Reviewed;         550 AA.
Q55320;
19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 59.
RecName: Full=Alkaline phosphatase PhoV {ECO:0000303|PubMed:8574398, ECO:0000312|EMBL:CAA88739.1};
Short=APase PhoV {ECO:0000303|PubMed:8574398};
EC=3.1.3.1 {ECO:0000269|PubMed:8574398};
Flags: Precursor;
Name=phoV {ECO:0000312|EMBL:CAA88739.1};
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2).
Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
Synechococcus.
NCBI_TaxID=1140;
[1] {ECO:0000305, ECO:0000312|EMBL:CAA88739.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, FUNCTION, CATALYTIC
ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
AND SUBCELLULAR LOCATION.
STRAIN=PCC 7942 {ECO:0000269|PubMed:8574398};
PubMed=8574398; DOI=10.1099/13500872-141-12-3049;
Wagner K.U., Masepohl B., Pistorius E.K.;
"The cyanobacterium Synechococcus sp. strain PCC7942 contains a second
alkaline phosphatase encoded by phoV.";
Microbiology 141:3049-3058(1995).
-!- FUNCTION: Alkaline phosphatase with broad substrate specificity.
{ECO:0000269|PubMed:8574398}.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000269|PubMed:8574398}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:A1YYW7,
ECO:0000269|PubMed:8574398};
Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:A1YYW7,
ECO:0000269|PubMed:8574398};
-!- 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.
{ECO:0000269|PubMed:8574398}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.1 mM for 4-nitrophenyl phosphate
{ECO:0000269|PubMed:8574398};
KM=1.0 mM for ATP {ECO:0000269|PubMed:8574398};
KM=0.5 mM for ADP {ECO:0000269|PubMed:8574398};
KM=1.5 mM for AMP {ECO:0000269|PubMed:8574398};
KM=1.9 mM for D-glucose 6-phosphate
{ECO:0000269|PubMed:8574398};
KM=1.4 mM for fructose 1,6-phosphate
{ECO:0000269|PubMed:8574398};
KM=2.3 mM for fructose 6-phosphate {ECO:0000269|PubMed:8574398};
KM=3.8 mM for fructose 1-phosphate {ECO:0000269|PubMed:8574398};
KM=1.9 mM for 3-phosphoglycerate {ECO:0000269|PubMed:8574398};
KM=2.4 mM for 3-phosphocreatine {ECO:0000269|PubMed:8574398};
pH dependence:
Optimum pH is 7-10. Activity on 4-nitrophenyl phosphate is
observed between pH 6 and pH 11. {ECO:0000269|PubMed:8574398};
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.
{ECO:0000269|PubMed:8574398};
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:8574398}; Lipid-anchor
{ECO:0000269|PubMed:8574398, ECO:0000305}; Periplasmic side
{ECO:0000269|PubMed:8574398}. Cell inner membrane
{ECO:0000269|PubMed:8574398}; Peripheral membrane protein
{ECO:0000269|PubMed:8574398}; Periplasmic side
{ECO:0000269|PubMed:8574398}. Note=Associated with the periplasmic
side of the inner membrane. {ECO:0000269|PubMed:8574398}.
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EMBL; Z48801; CAA88739.1; -; Genomic_DNA.
ProteinModelPortal; Q55320; -.
SMR; Q55320; -.
GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0098552; C:side of membrane; IDA:UniProtKB.
GO; GO:0004035; F:alkaline phosphatase activity; IDA:UniProtKB.
GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IDA:UniProtKB.
GO; GO:0050192; F:phosphoglycerate phosphatase activity; IDA:UniProtKB.
GO; GO:0050308; F:sugar-phosphatase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:UniProtKB.
GO; GO:0006603; P:phosphocreatine metabolic process; IDA:UniProtKB.
GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; IDA:UniProtKB.
CDD; cd16016; AP-SPAP; 1.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core.
InterPro; IPR026263; Alkaline_phosphatase_prok.
InterPro; IPR002591; Phosphodiest/P_Trfase.
Pfam; PF01663; Phosphodiest; 1.
PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
SUPFAM; SSF53649; SSF53649; 2.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Hydrolase; Lipoprotein; Membrane;
Metal-binding; Phosphoprotein; Signal; Zinc.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 550 Alkaline phosphatase PhoV. {ECO:0000255}.
/FTId=PRO_0000425537.
REGION 171 173 Substrate binding.
{ECO:0000250|UniProtKB:A1YYW7}.
ACT_SITE 89 89 Phosphothreonine intermediate.
{ECO:0000250|UniProtKB:A1YYW7}.
METAL 48 48 Zinc 1. {ECO:0000250|UniProtKB:A1YYW7}.
METAL 89 89 Zinc 1. {ECO:0000250|UniProtKB:A1YYW7}.
METAL 313 313 Zinc 2. {ECO:0000250|UniProtKB:A1YYW7}.
METAL 317 317 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:A1YYW7}.
METAL 360 360 Zinc 1. {ECO:0000250|UniProtKB:A1YYW7}.
METAL 361 361 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:A1YYW7}.
METAL 491 491 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:A1YYW7}.
BINDING 110 110 Substrate.
{ECO:0000250|UniProtKB:A1YYW7}.
SEQUENCE 550 AA; 61325 MW; B3D58CF18FCFD483 CRC64;
MKIKLLCISL AVLFCSSANA QKKQAKVQPS VFPQTVARPK LVVGMVIDQM RWDYLYRFYA
RYGNGGFKRL INEGFSAENT LIPYTPTLTA CGHSSIYTGS VPAINGIIGN NWFDPQLGRD
VYCVEDKSVK TVGSSSNEGL MSPKNLLVTT VTDELRMATN FRSKVISVSI KDRGAILPGG
HTANGAYWYD DMTGSFISST HYMQQLPTWV NDFNAQRLPN KYFEQDWNTL YPIETYTEST
ADAKPYERTF KGAKTSSFPH LFKQYANKNY SMMASMPQGN SFTLEFAKAA IPAEKLGQTG
NTDFLAVSLS STDYVGHQFG PNSIELEDTY LRLDKDLEDF FNYLDKTIGK GNYLLFLTAD
HGATHVPGFL RNKMPGGRLL LKVQTDLDSL IFNEFKVRCN FTIINNQVIF DTDAIKEAKA
DYAKIKQSTI DYLVKQDGVL NAVDIKNMGA VTIPQEIKNK IINGYNARRS GDVYIILDAG
WYPTLTPGTG HAAWNPYDSH IPALFMGWGV KPGKTNKEYY MSDIAPTVSA LLHIQQPSGS
IGKVITDLLK


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