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Information on EC 5.4.2.12 - phosphoglycerate mutase (2,3-diphosphoglycerate-independent) and Organism(s) Arabidopsis thaliana and UniProt Accession Q9M9K1
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5.4.2.12 phosphoglycerate mutase (2,3-diphosphoglycerate-independent)IUBMB Comments
The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction.
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Word Map
- 5.4.2.12
- mutases
- 2-phosphoglycerate
-
ipgms
-
2,3-bisphosphoglycerate-independent
-
cofactor-dependent
- 2,3-bisphosphoglycerate
- mexicana
-
brugia
- malayi
- phosphoenzyme
- dikinase
-
flux-controlling
- filariasis
- medicine
- drug development
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
Synonyms
ipgam, cofactor-independent phosphoglycerate mutase, 3-phosphoglycerate mutase, independent pgm, independent pgam, sso0417, 2,3-biphosphoglycerate-independent phosphoglycerate mutase, co-factor-independent phosphoglycerate mutase, cofactor independent phosphoglycerate mutase, mj0010, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-independent)
The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction.
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
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
PMG1/PMG2 double mutants have no detectable iPGAM activity and show defects in blue light-, abscisic acid-, and low CO2-regulated stomatal movements. Vegetative plant growth is severely impaired in the double mutants and pollen is not produced, phenotypes, overview
physiological function
2,3-biphosphoglycerate-independent phosphoglycerate mutase is a key enzymatic activity in glycolysis and catalyses the reversible interconversion of 3-phosphoglycerate to 2-phosphoglycerate, functions of iPGAMs and glycolysis in stomatal function and plant growth, overview. Both isozymes PMG1 and PMG2 and glycolytic activity are critical for guard cell function and fertility
malfunction
PMG1/PMG2 double mutants have no detectable iPGAM activity and show defects in blue light-, abscisic acid-, and low CO2-regulated stomatal movements. Vegetative plant growth is severely impaired in the double mutants and pollen is not produced, phenotypes, overview
physiological function
2,3-biphosphoglycerate-independent phosphoglycerate mutase is a key enzymatic activity in glycolysis and catalyses the reversible interconversion of 3-phosphoglycerate to 2-phosphoglycerate, functions of iPGAMs and glycolysis in stomatal function and plant growth, overview. Both isozymes PMG1 and PMG2 and glycolytic activity are critical for guard cell function and fertility
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). PMG2_ARATH
560
0
60764
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
insertional mutants of PMG1 and duble mutants of PMG1 and PMG2 are generated. While single mutants are indistinguishable from wild-type in all plant phenotypes assayed, double mutants have no detectable iPGAM activity and show defects in blue light-, abscisic acid-, and low CO2-regulated stomatal movements
additional information
insertional mutants of PMG1 and duble mutants of PMG1 and PMG2 are generated. While single mutants are indistinguishable from wild-type in all plant phenotypes assayed, double mutants have no detectable iPGAM activity and show defects in blue light-, abscisic acid-, and low CO2-regulated stomatal movements
additional information
-
insertional mutants of PMG1 and duble mutants of PMG1 and PMG2 are generated. While single mutants are indistinguishable from wild-type in all plant phenotypes assayed, double mutants have no detectable iPGAM activity and show defects in blue light-, abscisic acid-, and low CO2-regulated stomatal movements
additional information
insertional mutants of PMG1 and duble mutants of PMG1 and PMG2 are generated. While single mutants are indistinguishable from wild-type in all plant phenotypes assayed, double mutants have no detectable iPGAM activity and show defects in blue light-, abscisic acid-, and low CO2-regulated stomatal movements
additional information
insertional mutants of PMG1 and duble mutants of PMG1 and PMG2 are generated. While single mutants are indistinguishable from wild-type in all plant phenotypes assayed, double mutants have no detectable iPGAM activity and show defects in blue light-, abscisic acid-, and low CO2-regulated stomatal movements
additional information
-
insertional mutants of PMG1 and duble mutants of PMG1 and PMG2 are generated. While single mutants are indistinguishable from wild-type in all plant phenotypes assayed, double mutants have no detectable iPGAM activity and show defects in blue light-, abscisic acid-, and low CO2-regulated stomatal movements
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhao, Z.; Assmann, S.M.
The glycolytic enzyme, phosphoglycerate mutase, has critical roles in stomatal movement, vegetative growth, and pollen production in Arabidopsis thaliana
J. Exp. Bot.
62
5179-5189
2011
Arabidopsis thaliana (O04499), Arabidopsis thaliana (Q9M9K1), Arabidopsis thaliana
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