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Information on EC 5.4.2.12 - phosphoglycerate mutase (2,3-diphosphoglycerate-independent) and Organism(s) Saccharolobus solfataricus and UniProt Accession Q980A0

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EC Tree
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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Saccharolobus solfataricus
UNIPROT: Q980A0
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Word Map
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
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, ph0037, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2,3-diphosphoglycerate-independent phosphoglycerate mutase
-
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
3-phospho-D-glycerate
2-phospho-D-glycerate
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
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
divalent cation required for activity
Co2+
divalent cation required for activity, 3times higher activity than with Mn2+
Mn2+
divalent cation required for activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 0.26
2-phospho-D-glycerate
0.04 - 0.11
3-phospho-D-glycerate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.04 - 4.01
2-phospho-D-glycerate
1.51 - 3.01
3-phospho-D-glycerate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.84 - 36.45
2-phospho-D-glycerate
19.81 - 35.95
3-phospho-D-glycerate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45179
x * 45179, deduced from nucleotide sequence
46000
x * 46000, SDS-PAGE
46800
x * 46000-48000, SDS-PAGE, x * 46800, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
autophosphorylation at Ser59
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Potters, M.B.; Solow, B.T.; Bischoff, K.M.; Graham, D.E.; Lower, B.H.; Helm, R.; Kennelly, P.J.
Phosphoprotein with phosphoglycerate mutase activity from the archaeon Sulfolobus solfataricus
J. Bacteriol.
185
2112-2121
2003
Saccharolobus solfataricus (Q980A0), Saccharolobus solfataricus
Manually annotated by BRENDA team
Haferkamp, P.
Biochemical studies of enzymes involved in glycolysis of the thermoacidophilic crenarchaeon Sulfolobus solfataricus
PH. D. Thesis Universitt Duisburg-Essen
2011
0000
2011
Saccharolobus solfataricus (Q980A0), Saccharolobus solfataricus DSM 1617 (Q980A0)
-
Manually annotated by BRENDA team