Literature summary for 3.1.3.8 extracted from

Suleimanova, A.D.; Beinhauer, A.; Valeeva, L.R.; Chastukhina, I.B.; Balaban, N.P.; Shakirov, E.V.; Greiner, R.; Sharipova, M.R.
Novel glucose-1-phosphatase with high phytase activity and unusual metal ion activation from soil bacterium Pantoea sp. strain 3.5.1 (2015), Appl. Environ. Microbiol., 81, 6790-6799 .

Search for more literature for 3.1.3.8

Cloned(Commentary)

Cloned (Comment)	Organism
gene agpP, DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme lacking the signal peptide in Escherichia coli	Pantoea sp. 3.5.1

Inhibitors

Inhibitors	Comment	Organism	Structure
Cu2+	16% inhibition at 1 mM	Pantoea sp. 3.5.1
Fe2+	10% inhibition at 1 mM	Pantoea sp. 3.5.1
additional information	no effect by Co2+ at 1 mM	Pantoea sp. 3.5.1
Zn2+	42% inhibition at 1 mM	Pantoea sp. 3.5.1

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	enzyme kinetics, also with other substrates, such as AMP, NADP, pNPP, 1-naphthyl phosphate, glucose phosphates, beta-glycerol phosphate, and diphosphate, overview	Pantoea sp. 3.5.1
0.28	-	myo-inositol hexakisphosphate	recombinant His-tagged enzyme, pH and temperature not specified in the publication	Pantoea sp. 3.5.1

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	-	Pantoea sp. 3.5.1	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	2fold activation at 1 mM	Pantoea sp. 3.5.1
Mg2+	2fold activation at 1 mM	Pantoea sp. 3.5.1
Mn2+	2fold activation at 1 mM	Pantoea sp. 3.5.1
additional information	no effect by Co2+ at 1 mM	Pantoea sp. 3.5.1

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
55000	57000	native enzyme, gel filtration	Pantoea sp. 3.5.1

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Pantoea sp. 3.5.1	the bifunctional enzyme also exhibits glucose-1-phosphatase, cf. EC 3.1.3.10	?	-	?
myo-inositol hexakisphosphate + H2O	Pantoea sp. 3.5.1	-	1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Pantoea sp. 3.5.1	A0A075FFV0	isolated from soil collected from four different ecological and geographical habitats of the Republic of Tatarstan, Russia, forest near the village Agerze, Aznakaevo District	-

Purification (Commentary)

Purification (Comment)	Organism
native enzyme by dialysis, anion exchange chromatography, and gel filtration, recombinant His6-tagged enzyme lacking the signal peptide from Escherichia coli by nickel affinity chromatography. Native extracellular enzyme 528fold by dialysis, anion and cation exchange chromatography, and gel filtration	Pantoea sp. 3.5.1

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	ability of the Pantoea sp. 3.5.1 isolate to grow with insoluble Ca-phytate as the sole source of phosphorus, not due to the secretion of an extracellular phytase. Growth dynamics and extracellular and intracellular phytate-hydrolyzing activities of Pantoea sp. 3.5.1 culture, overview	Pantoea sp. 3.5.1	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
5.92	-	purified recombinant His-tagged enzyme, pH and temperature not specified in the publication, substrate alpha-D-glucose 1-phosphate	Pantoea sp. 3.5.1

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the bifunctional enzyme also exhibits glucose-1-phosphatase, cf. EC 3.1.3.10	Pantoea sp. 3.5.1	?	-	?
additional information	glucose-1-phosphatase enzymes and, specifically, Agp phytases are known to have a broad substrate specificity. The bifunctional enzyme from Pantoea sp. 3.5.1 exhibits 3-phytase activity, and also glucose-1-phosphatase, cf. EC 3.1.3.10. Broad substrate specificity, substrates are phytate and many other phosphate-containing substrates, such as AMP, NADP, pNPP, 1-naphthyl phosphate, glucose phosphates, beta-glycerol phosphate, and diphosphate, overview	Pantoea sp. 3.5.1	?	-	?
myo-inositol hexakisphosphate + H2O	-	Pantoea sp. 3.5.1	1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate	-	?

Subunits

Subunits	Comment	Organism
monomer	1 * 48000, native enzyme, SDS-PAGE	Pantoea sp. 3.5.1

Synonyms

Synonyms	Comment	Organism
agpP	-	Pantoea sp. 3.5.1
AgpP phytase	-	Pantoea sp. 3.5.1
More	cf. EC 3.1.3.10	Pantoea sp. 3.5.1

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	-	Pantoea sp. 3.5.1

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
10	65	activity range, profile overview	Pantoea sp. 3.5.1

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
10	65	purified AgpP phytase remains stable for 1 h at a temperature interval of 10-45°C losing only up to 20% of activity at 45°C, only 40% and 12% of its maximum activity are retained at 55°C and 65°C, respectively	Pantoea sp. 3.5.1
70	-	purified enzyme, 1 h, inactivation	Pantoea sp. 3.5.1

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4.5	-	-	Pantoea sp. 3.5.1

pH Range

pH Minimum	pH Maximum	Comment	Organism
2.5	8	activity range, profile overview, narrow optimum, over 50% activity only at pH 4.0-5.0	Pantoea sp. 3.5.1

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
4	9	1 h, 4°C, the purified native phytase does not show any significant decline in activity at pH 4.0-5.5, almost 80% of the activity is lost at pH 9.0. At the optimum pH 4.5, the enzyme retains over 90% of its initial activity even after 10 days of incubation	Pantoea sp. 3.5.1

General Information

General Information	Comment	Organism
evolution	the enzyme AgpP from Pantoea sp. 3.5.1. belongs to the Agp subfamily of histidine acid phosphatases with 3-phytase specificity. The amino acid sequence of the Pantoea sp. 3.5.1 AgpP phytase harbors an N-terminal RHNLRAP motif (where the italicized residues are variable) and a C-terminal HD motif, which are the structural hallmarks of the highly conserved catalytic core of histidine acid phosphatases (HAPs) [consensus sequence RH(G/N)XRXP/HD, where the slash separates the N- and C-terminal sequences]	Pantoea sp. 3.5.1
physiological function	AgpP phytase and its unusual regulation by metal ions highlight the remarkable diversity of phosphorus metabolism regulation in soil bacteria	Pantoea sp. 3.5.1

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Release 2023.1 (January 2023)