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Information on EC 2.7.9.5 - phosphoglucan, water dikinase and Organism(s) Arabidopsis thaliana and UniProt Accession Q6ZY51
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2.7.9.5 phosphoglucan, water dikinaseIUBMB Comments
The 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 . 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 . The protein phosphorylates itself with the beta-phosphate of ATP, which is then transferred to the glucan .
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pwd, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
At5g26570
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:phospho-alpha-glucan, water phosphotransferase
The 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].
CAS REGISTRY NUMBER
COMMENTARY
664327-94-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + crystalline maltodextrin + H2O
AMP + phospho-alpha-glucosyl-maltodextrin + phosphate
crystalline maltodextrin (MDcryst) is used as a model substrate for glucan phosphorylating enzyme activity that mimics features of native starches, such as allomorph and crystallinity but omitted branching. Significant phosphorylation of MDcryst by PWD requires the preceding action of GWD. GWD-dependent phosphorylation alters the granule surface structure, which favors the action of PWD
-
-
?
ATP + phospho-maltodextrin + H2O
AMP + O-phospho-[phospho-maltodextrin] + phosphate
-
only pre-phosphorylated, crystallised (insoluble) maltodextrin
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
dikinases use ATP as a dual phosphate donor and transfer the beta- and gamma-phosphate groups to two distinct acceptor molecules, a glucan and water. A conserved histidine residue within this domain is capable of accepting the beta-phosphate group of ATP following nucleotide binding and hydrolysis. The phosphoramidate bond is acid labile, but rather stable under alkaline conditions. The gamma-phosphate group is transferred to water
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
GWD phosphorylates the hydroxyl group at carbon atom 3, the gamma-phosphate group of ATP is transferred to water and the beta-phosphate group to an autocatalytical histidine residue via a phosphoramidate bond. GWD-dependent phosphorylation alters the granule surface structure, which favors the action of PWD. PWD phosphorylates also non pre-phosphorylated glucan chains
-
-
?
ATP + [phospho-alpha-glucan] + H2O
AMP + O-phospho-[phospho-alpha-glucan] + phosphate
-
-
-
?
ATP + [phospho-alpha-glucan] + H2O
AMP + O-phospho-[phospho-alpha-glucan] + phosphate
important enzymes of starch metabolism. Catalyzes the addition of phosphate groups to amylopectin chains at the surface of starch granules, changing its physicochemical properties
-
-
?
ATP + [phospho-alpha-glucan] + H2O
AMP + O-phospho-[phospho-alpha-glucan] + phosphate
the enzyme is involved in starch phosphorylation, a key step in starch degradation
-
-
?
additional information
?
-
no phosphorylation of the hydroxyl group at the C2 position
-
-
?
additional information
?
-
-
solubilised maltodextrin is no substrate whether pre-phosphorylated by glucan, water dikinase (GWD) or not
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
dikinases use ATP as a dual phosphate donor and transfer the beta- and gamma-phosphate groups to two distinct acceptor molecules, a glucan and water. A conserved histidine residue within this domain is capable of accepting the beta-phosphate group of ATP following nucleotide binding and hydrolysis. The phosphoramidate bond is acid labile, but rather stable under alkaline conditions. The gamma-phosphate group is transferred to water
-
-
?
ATP + [phospho-alpha-glucan] + H2O
AMP + O-phospho-[phospho-alpha-glucan] + phosphate
important enzymes of starch metabolism. Catalyzes the addition of phosphate groups to amylopectin chains at the surface of starch granules, changing its physicochemical properties
-
-
?
ATP + [phospho-alpha-glucan] + H2O
AMP + O-phospho-[phospho-alpha-glucan] + phosphate
the enzyme is involved in starch phosphorylation, a key step in starch degradation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EARLY STARVATION1
i.e. ESV1, a 50000 Da starch-binding protein. Increases action of phosphoglucan, water dikinase. ESV1 does not affect the autophosphorylation of the phosphoglucan, water dikinase
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no activity detectable on pre-phosphorylated, soluble maltodextrin
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme acts significantly on the surface of native starch granules
-
additional information
the GWD full-length protein binds to native starch granules in vivo and in vitro. Binding of GWD in vivo is dependent on the metabolic status of the cells. A significantly higher proportion of the dikinases is associated with native leaf starch granules isolated during the dark period than in the light phase of the photoperiod
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the largest differences in the amino acid sequence of GWD, EC 2.7.9.4, and PWD, EC 2.7.9.5, span the non-catalytic N-terminal region. In case of PWD, the N-terminus contains a single starch-binding domain (SBD) that belongs to the well-characterized carbohydrate-binding module (CBM) family CBM20. In contrast to PWD, the identity of the N-terminal starch-binding domain of GWD is less pronounced but might be assigned to the recently identified CBM45 family
malfunction
mutants lacking the enzyme reveal a starch excess phenotype as well as growth retardation. The lack of PWD causes a reduction of G3P alone
metabolism
physiological function
metabolism
during starch metabolism, the phosphorylation of glucosyl residues of amylopectin is a repeatedly observed process. The phosphorylation is mediated by dikinases, glucan, water dikinase (GWD, EC 2.7.9.4) and phosphoglucan, water dikinase (PWD, EC 2.7.9.5). By the collaborative action of both enzymes, the initiation of a transition of alpha-glucans from highly ordered, water-insoluble state to a less order state is realized and thus the initial process of starch degradation
metabolism
the enzyme is involved in starch phosphorylation, a key step in starch degradation
physiological function
the starch-related dikinase utilizes ATP as dual phosphate donor transferring the terminal gamma-phosphate group to water selectively to C3 position of a glucosyl residue within amylopectin. The action of the dikinase is restricted to the granule surface and glucan chains exposed at the surface account only for a minor proportion of the entire granule. Glucan chains that are phosphorylated by the dikinase remain covalently linked to the insoluble starch particle. In Arabidopsis leaf starch, about 0.1% of the glucosyl residues are phosphorylated, respectively. PWD is mainly responsible for C3 phosphorylation. A significant PWD-mediated C3 phosphorylation requires the preceding phosphorylation by GWD in Arabidopsis thaiana wild-type starch
physiological function
important enzyme of starch metabolism. Catalyzes the addition of phosphate groups to amylopectin chains at the surface of starch granules, changing its physicochemical properties
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PWD_ARATH
1196
0
131323
Swiss-Prot
Chloroplast (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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 decreased
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ritte, 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 dikinases
FEBS Lett.
580
4872-4876
2006
Arabidopsis thaliana
Hejazi, M.; Fettke, J.; Haebel, S.; Edner, C.; Paris, O.; Frohberg, C.; Steup, M.; Ritte, G.
Glucan, water dikinase phosphorylates crystalline maltodextrins and thereby initiates solubilization
Plant J.
55
323-334
2008
Arabidopsis thaliana
Mahlow, S.; Orzechowski, S.; Fettke, J.
Starch phosphorylation: insights and perspectives
Cell. Mol. Life Sci.
73
2753-2764
2016
Solanum tuberosum (D2JRZ6), Arabidopsis thaliana (Q6ZY51)
Pirone, C.; Gurrieri, L.; Gaiba, I.; Adamiano, A.; Valle, F.; Trost, P.; Sparla, F.
The analysis of the different functions of starch-phosphorylating enzymes during the development of Arabidopsis thaliana plants discloses an unexpected role for the cytosolic isoform GWD2
Physiol. Plant.
160
447-457
2017
Arabidopsis thaliana (Q6ZY51), Arabidopsis thaliana
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