Information on EC 2.7.9.5 - phosphoglucan, water dikinase:
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The lowest common taxonomy group for this enzyme is: Arabidopsis

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EC NUMBERCOMMENTARY
2.7.9.5-

RECOMMENDED NAMEGeneOntology No.
phosphoglucan, water dikinaseGO:0051752

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + [phospho-alpha-glucan] + H2O = AMP + O-phospho-[phospho-alpha-glucan] + phosphate
show the reaction diagram		----
ATP + [phospho-alpha-glucan] + H2O = AMP + O-phospho-[phospho-alpha-glucan] + phosphate
show the reaction diagram		-Arabidopsis sp.-660254

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

PATHWAYKEGG LinkMetaCyc Link
starch degradation II-PWY-6724

SYSTEMATIC NAMEIUBMB Comments
ATP:phospho-alpha-glucan, water phosphotransferaseThe enzyme phosphorylates granular starch that has previously been phosphorylated by EC 2.7.9.4, alpha-glucan, water dikinase; there is no activity with unphosphorylated glucans. It transfers the beta-phosphate of ATP to the phosphoglucan, whereas the gamma-phosphate is transferred to water [1]. In contrast to EC 2.7.9.4, which phosphorylates glucose groups in glucans on O-6, this enzyme phosphorylates glucose groups in phosphorylated starch on O-3 [2]. The protein phosphorylates itself with the beta-phosphate of ATP, which is then transferred to the glucan [1].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
OK1Arabidopsis sp.--660254
phosphoglucan, water dikinaseArabidopsis thaliana--694680
PWDArabidopsis sp.--660254
PWDArabidopsis thaliana--694680

CAS REGISTRY NUMBERCOMMENTARY
664327-94-0-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Arabidopsis sp.-660254--Manually annotated by BRENDA team
Arabidopsis thaliana-673664, 694680--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + phospho-maltodextrin + H2OAMP + O-phospho-[phospho-maltodextrin] + phosphate
show the reaction diagram		Arabidopsis thaliana-only pre-phosphorylated, crystallised (insoluble) maltodextrin694680--?
ATP + [phospho-alpha-glucan]AMP + O-phospho-[phospho-alpha-glucan] + phosphate
show the reaction diagram		Arabidopsis sp.-the enzyme phosphorylates granular starch that has previously been phosphorylated by EC 2.7.9.4, alpha-glucan, water dikinase, the enzyme transfers the beta-phosphate of ATP to the phosphoglucan, whereas the gamma-phosphate is transferred to water. The protein phosphorylates itself with the beta-phosphate of ATP at a His residue of the enzyme, which is then transferred to the glucan660254--?
additional information?-Arabidopsis thaliana-solubilised maltodextrin is no substrate whether pre-phosphorylated by glucan, water dikinase (GWD) or not694680---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + [phospho-alpha-glucan]AMP + O-phospho-[phospho-alpha-glucan] + phosphate
show the reaction diagram		Arabidopsis sp.-the enzyme phosphorylates granular starch that has previously been phosphorylated by EC 2.7.9.4, alpha-glucan, water dikinase660254--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.002-Arabidopsis thaliana-pre-phosphorylated, crystalline maltodextrin694680
additional information-Arabidopsis thaliana-no activity detectable on pre-phosphorylated, soluble maltodextrin694680

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
leafArabidopsis sp.--660254Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
plastidArabidopsis sp.--9536660254Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Arabidopsis sp.-660254

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Arabidopsis sp.-660254

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
additional informationArabidopsis thaliana-in mutant plants lacking phosphoglucan, water dikinase EC 2.7.9.5, C3-bound phosphate is reduced to levels close to detection limit. In mutant plants lacking alpha-glucan, water dikinase EC 2.7.9.4, phosphorylation at both C6- and C3-positions of glucose moieties in starch is dramatically decreased673664

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
660254Kotting, O.; Pusch, K.; Tiessen, A.; Geigenberger, P.; Steup, M.; Ritte, G.Identification of a novel enzyme required for starch metabolism in Arabidopsis leaves. The phosphoglucan, water dikinasePlant Physiol.137242-2522005Arabidopsis sp. PubMed
673664Ritte, G.; Heydenreich, M.; Mahlow, S.; Haebel, S.; Koetting, O.; Steup, M.Phosphorylation of C6- and C3-positions of glucosyl residues in starch is catalysed by distinct dikinasesFEBS Lett.5804872-48762006Arabidopsis thaliana PubMed
694680Hejazi, M.; Fettke, J.; Haebel, S.; Edner, C.; Paris, O.; Frohberg, C.; Steup, M.; Ritte, G.Glucan, water dikinase phosphorylates crystalline maltodextrins and thereby initiates solubilizationPlant J.55323-3342008Arabidopsis thaliana PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.7.9.5)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)