ALPH_SYNE7
ID ALPH_SYNE7 Reviewed; 550 AA.
AC Q55320;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Alkaline phosphatase PhoV {ECO:0000303|PubMed:8574398, ECO:0000312|EMBL:CAA88739.1};
DE Short=APase PhoV {ECO:0000303|PubMed:8574398};
DE EC=3.1.3.1 {ECO:0000269|PubMed:8574398};
DE Flags: Precursor;
GN Name=phoV {ECO:0000312|EMBL:CAA88739.1};
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA88739.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805 {ECO:0000269|PubMed:8574398};
RX PubMed=8574398; DOI=10.1099/13500872-141-12-3049;
RA Wagner K.U., Masepohl B., Pistorius E.K.;
RT "The cyanobacterium Synechococcus sp. strain PCC7942 contains a second
RT alkaline phosphatase encoded by phoV.";
RL Microbiology 141:3049-3058(1995).
CC -!- FUNCTION: Alkaline phosphatase with broad substrate specificity.
CC {ECO:0000269|PubMed:8574398}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC Evidence={ECO:0000269|PubMed:8574398};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:A1YYW7, ECO:0000269|PubMed:8574398};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:A1YYW7,
CC ECO:0000269|PubMed:8574398};
CC -!- ACTIVITY REGULATION: Subject to competitive inhibition by phosphate.
CC Inhibited by manganese. Magnesium mildly increases enzyme activity when
CC the zinc concentration is suboptimal. Optimal activity is dependent on
CC the presence of 0.01-2% Triton X-100. Triton X-100 at a concentration
CC of 0.05% increases the activity about fivefold relative to that in its
CC absence. The enzyme is even active in Triton X-100 concentrations up to
CC 80%. 50% inhibition by 4 mM EDTA and 50% inhibition by 48 mM sodium
CC citrate. {ECO:0000269|PubMed:8574398}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for 4-nitrophenyl phosphate {ECO:0000269|PubMed:8574398};
CC KM=1.0 mM for ATP {ECO:0000269|PubMed:8574398};
CC KM=0.5 mM for ADP {ECO:0000269|PubMed:8574398};
CC KM=1.5 mM for AMP {ECO:0000269|PubMed:8574398};
CC KM=1.9 mM for D-glucose 6-phosphate {ECO:0000269|PubMed:8574398};
CC KM=1.4 mM for fructose 1,6-phosphate {ECO:0000269|PubMed:8574398};
CC KM=2.3 mM for fructose 6-phosphate {ECO:0000269|PubMed:8574398};
CC KM=3.8 mM for fructose 1-phosphate {ECO:0000269|PubMed:8574398};
CC KM=1.9 mM for 3-phosphoglycerate {ECO:0000269|PubMed:8574398};
CC KM=2.4 mM for 3-phosphocreatine {ECO:0000269|PubMed:8574398};
CC pH dependence:
CC Optimum pH is 7-10. Activity on 4-nitrophenyl phosphate is observed
CC between pH 6 and pH 11. {ECO:0000269|PubMed:8574398};
CC Temperature dependence:
CC Heat-labile. Activity increases with temperature between 15 and 35
CC degrees Celsius and decreases with further heating. No activity at 65
CC degrees Celsius. Preincubation for 10 minutes at 50 or 60 degrees
CC Celsius causes 50% or 100% inactivation, respectively. Heat-
CC inactivated enzyme cannot be renaturated.
CC {ECO:0000269|PubMed:8574398};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8574398};
CC Lipid-anchor {ECO:0000269|PubMed:8574398, ECO:0000305}; Periplasmic
CC side {ECO:0000269|PubMed:8574398}. Cell inner membrane
CC {ECO:0000269|PubMed:8574398}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8574398}; Periplasmic side
CC {ECO:0000269|PubMed:8574398}. Note=Associated with the periplasmic side
CC of the inner membrane. {ECO:0000269|PubMed:8574398}.
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DR EMBL; Z48801; CAA88739.1; -; Genomic_DNA.
DR AlphaFoldDB; Q55320; -.
DR SMR; Q55320; -.
DR PRIDE; Q55320; -.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IDA:UniProtKB.
DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IDA:UniProtKB.
DR GO; GO:0050192; F:phosphoglycerate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0050308; F:sugar-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0006603; P:phosphocreatine metabolic process; IDA:UniProtKB.
DR GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; IDA:UniProtKB.
DR CDD; cd16016; AP-SPAP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR026263; Alkaline_phosphatase_prok.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR Pfam; PF01663; Phosphodiest; 1.
DR PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Hydrolase; Lipoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..550
FT /note="Alkaline phosphatase PhoV"
FT /evidence="ECO:0000255"
FT /id="PRO_0000425537"
FT ACT_SITE 89
FT /note="Phosphothreonine intermediate"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 171..173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
FT BINDING 491
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A1YYW7"
SQ 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
