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Information on EC 5.4.2.12 - phosphoglycerate mutase (2,3-diphosphoglycerate-independent) and Organism(s) Bacillus anthracis and UniProt Accession Q81X77

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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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Bacillus anthracis
UNIPROT: Q81X77
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Word Map
The taxonomic range for the selected organisms is: Bacillus anthracis
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
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-phospho-D-glycerate = 3-phospho-D-glycerate
show the reaction diagram
in the phospho-D-glycerate-free state the enzyme assumes an open conformation. Upon substrate binding the enzyme closes to the catalytically functional conformation, in the closed form the enzyme catalyzes 2/3-phospho-D-glycerate isomerization resulting in product release. Product release causes opening of the enzyme and return to the open conformation
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
-
-
-
r
3-phospho-D-glycerate
2-phospho-D-glycerate
show the reaction diagram
-
-
-
r
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GPMI_BACAN
509
0
56281
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
protein is composed of two structural and functiional domains, the phosphatase and the transferase. Comparison with the structurally similar domains of in Bacillus stearothermophilus
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nukui, M.; Mello, L.V.; Littlejohn, J.E.; Setlow, B.; Setlow, P.; Kim, K.; Leighton, T.; Jedrzejas, M.J.
Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species
Biophys. J.
92
977-988
2007
Bacillus anthracis (Q81X77), Bacillus anthracis
Manually annotated by BRENDA team