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Information on EC 5.4.2.2 - phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) and Organism(s) Arabidopsis thaliana and UniProt Accession O49299

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IUBMB Comments
Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. The enzyme also catalyses (more slowly) the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. cf. EC 5.4.2.5, phosphoglucomutase (glucose-cofactor).
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Arabidopsis thaliana
UNIPROT: O49299
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphoglucomutase, phosphoglucomutase 1, phosphomannomutase/phosphoglucomutase, pmm/pgm, alpha-phosphoglucomutase, pgm/pmm, alpha-pgm, phosphoglucose mutase, phosphoglucomutase1, plastidic phosphoglucomutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho-glucomutase
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cytosolic phosphoglucomutase
-
-
Glucose phosphomutase
-
-
-
-
phospho-glucomutase
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phosphoglucomutase
-
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Phosphoglucose mutase
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-
-
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Phosphomutase, glucose
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucose 1,6-phosphomutase
Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. The enzyme also catalyses (more slowly) the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. cf. EC 5.4.2.5, phosphoglucomutase (glucose-cofactor).
CAS REGISTRY NUMBER
COMMENTARY hide
9001-81-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
r
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isoform PGM1
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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cytosolic PGM activity is not limiting for carbon metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGMC1_ARATH
583
0
63171
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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recombinant expression of plastidial phosphoglucomutase in Nicotiana tabacum cv. Xanthi stimulates photosynthetic carbon flow into starch synthesis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Agrobacterium tumefaciens
expression in Agrobacterium tumefaciens
expression of cytosolic and plastidial isozymes in Nicotiana tabacum cv. Xanthi using the cauliflower mosaic virus 35S promoter. The transgenic plants expressing Arabidopsis plastidial PGM show 3.5-8.2fold higher enzyme activity compared to the wild-type, and leaf starch and sucrose contents increase 2.3-3.2fold and 1.3-1.4fold, respectively over wild-type levels, while transgenic plants expressing Arabidopsis cytosolic PGM show a 2.1-3.4fold increase in PGM activity over wild-type and a decrease of leaf starch content, but no change in sucrose content
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (O49299), Arabidopsis thaliana (Q9SCY0), Arabidopsis thaliana (Q9SGC1)
Manually annotated by BRENDA team
Egli, B.; Koelling, K.; Koehler, C.; Zeeman, S.C.; Streb, S.
Loss of cytosolic phosphoglucomutase compromises gametophyte development in Arabidopsis
Plant Physiol.
154
1659-1671
2010
Arabidopsis thaliana, Arabidopsis thaliana ecotypes Columbia, Landsberg erecta, and Cvi
Manually annotated by BRENDA team
Uematsu, K.; Suzuki, N.; Iwamae, T.; Inui, M.; Yukawa, H.
Expression of Arabidopsis plastidial phosphoglucomutase in tobacco stimulates photosynthetic carbon flow into starch synthesis
J. Plant Physiol.
169
1454-1462
2012
Arabidopsis thaliana
Manually annotated by BRENDA team
Malinova, I.; Kunz, H.H.; Alseekh, S.; Herbst, K.; Fernie, A.R.; Gierth, M.; Fettke, J.
Reduction of the cytosolic phosphoglucomutase in Arabidopsis reveals impact on plant growth, seed and root development, and carbohydrate partitioning
PLoS ONE
9
e112468
2014
Arabidopsis thaliana
Manually annotated by BRENDA team