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Information on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and Organism(s) Mus musculus and UniProt Accession Q9DBJ1

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EC Tree
IUBMB Comments
The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase.
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This record set is specific for:
Mus musculus
UNIPROT: Q9DBJ1
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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[enzyme]-L-histidine
+
2,3-bisphospho-D-glycerate
=
[enzyme]-Ntau-phospho-L-histidine
+
3-phospho-D-glycerate
[enzyme]-L-histidine
+
=
[enzyme]-Ntau-phospho-L-histidine
+
2-phospho-D-glycerate
=
3-phospho-D-glycerate
=
Synonyms
phosphoglycerate mutase, pgam1, phosphoglycerate mutase 1, sts-1, pgam2, cofactor-dependent phosphoglycerate mutase, dpgm-b, bisphosphoglycerate phosphatase, 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, rv3214, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoglycerate mutase 1
-
alpha-PGAM
-
PGAM1
-
-
phosphoglycerate mutase 1
-
-
Sts-1
-
-
SYSTEMATIC NAME
IUBMB Comments
D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-dependent)
The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase.
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
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
additional information
?
-
Mdm2 is a direct binding partner and ubiquitin ligase for the enzyme in cultured cells and in vitro
-
-
?
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
phosphoglycerate mutase is upregulated in the cobalt-treated mouse cerebrum
additional information
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGAM1_MOUSE
254
0
28832
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28940
deduced from amino acid sequence
30500
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 30000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Pak1-mediated phosphorylation of phosphoglycerate mutase predisposes the enzyme to ubiquitin-mediated degradation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminal phosphoglycerate mutase domain of mouse Sts-1, crystallization in space group C2 with two different crystal forms. Data of native and selenomethionine protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminal phosphoglycerate mutase domain of mouse Sts-1, Sts-1PGM, comprised of residues 369-640 and an N-terminal His-tag
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kleinman, H.; Ford, B.; Keller, J.; Carpino, N.; Nassar, N.
Crystallization and initial crystal characterization of the C-terminal phosphoglycerate mutase homology domain of Sts-1
Acta Crystallogr. Sect. F
F62
218-220
2006
Mus musculus
Manually annotated by BRENDA team
Kajiwara, K.; Sunaga, K.; Tsuda, T.; Sugaya, A.; Sugaya, E.; Kimura, M.
Peony root extract upregulates transthyretin and phosphoglycerate mutase in mouse cobalt focus seizure
Biochem. Biophys. Res. Commun.
371
375-379
2008
Mus musculus (Q9DBJ1), Mus musculus
Manually annotated by BRENDA team
iao, Y.; Jin, X.; Yan, J.; Jiao, F.; Li, X.; Roe, B.A.; Jarrett, H.W.; Gu, W.
An insertion of intracisternal A-particle retrotransposon in a novel member of the phosphoglycerate mutase family in the lew allele of mutant mice
Genes Genet. Syst.
84
327-334
2009
Mus musculus
Manually annotated by BRENDA team
Mikawa, T.; Maruyama, T.; Okamoto, K.; Nakagama, H.; Lleonart, M.E.; Tsusaka, T.; Hori, K.; Murakami, I.; Izumi, T.; Takaori-Kondo, A.; Yokode, M.; Peters, G.; Beach, D.; Kondoh, H.
Senescence-inducing stress promotes proteolysis of phosphoglycerate mutase via ubiquitin ligase Mdm2
J. Cell Biol.
204
729-745
2014
Mus musculus (O70250), Homo sapiens (P15259)
Manually annotated by BRENDA team