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 27-MAR-2024, entry version 77. 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 ATCC 33912 / PCC 7942 / FACHB-805) OS (Anacystis nidulans R2). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae; OC 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=ATCC 33912 / 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 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. CC Heat-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z48801; CAA88739.1; -; Genomic_DNA. DR AlphaFoldDB; Q55320; -. DR SMR; 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: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:0006002; P:fructose 6-phosphate metabolic process; IDA:UniProtKB. DR GO; GO:0006603; P:phosphocreatine metabolic process; IDA:UniProtKB. DR CDD; cd16016; AP-SPAP; 1. DR Gene3D; 3.30.1360.150; -; 1. DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1. DR InterPro; IPR017850; Alkaline_phosphatase_core_sf. DR InterPro; IPR026263; Alkaline_phosphatase_prok. DR InterPro; IPR002591; Phosphodiest/P_Trfase. DR PANTHER; PTHR10151:SF120; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1. DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1. DR Pfam; PF01663; Phosphodiest; 1. DR PIRSF; PIRSF031924; Pi-irrepressible_AP; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 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 //