PGAMPhosphoglycerate mutase family |
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| SMART accession number: | SM00855 |
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| Description: | Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate (PUBMED:2847721), (PUBMED:2831102), (PUBMED:10958932). Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein. |
| Family alignment: |
There are 6602 PGAM domains in 3261 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes - Cellular role (predicted cellular role)
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Cellular role: metabolism
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Tallaksen-Greene SJ, Kaatz KW, Romano C, Albin RL
- Localization of mGluR1a-like immunoreactivity and mGluR5-likeimmunoreactivity in identified populations of striatal neurons.
- Brain Res. 1998; 780: 210-7
- Display abstract
Metabotropic glutamate receptors are important mediators of excitatoryamino acid neurotransmission in the striatum. Two-color immunofluorescencehistochemistry and immunohistochemistry in combination with retrogradetract-tracing techniques were used to examine the distribution ofmetabotropic glutamate receptor subtypes 1a and 5 (mGluR1a and mGluR5)among identified subpopulations of striatal projection neurons andinterneurons. The majority of striatopallidal and striatonigral neuronswere double-labeled for both mGluR1a or mGluR5. Approximately 60% to 70%of either striatonigral or striatopallidal neurons expressed mGluR1a- ormGluR5-like immunoreactivity. The percentage of double-labeledstriatopallidal or striatonigral projection neurons did not differ amongstriatal quadrants. Striatal interneurons expressing parvalbumin orsomatostatin or choline acetyltransferase exhibited varying degrees ofexpression of mGluR1a or mGluR5. Virtually all (94%)parvalbumin-immunoreactive striatal neurons expressed mGluR1a-likeimmunoreactivity with a majority (79%) of these neurons expressingmGluR5-like immunoreactivity. A high percentage (89%) of striatal cholineacetyltransferase-immunoreactive neurons were double-labeled formGluR1a-like immunoreactivity. Approximately 65% of striatal cholineacetyltransferase-immunoreactive neurons expressed mGluR5-likeimmunoreactivity. A majority (65%) of somatostatin-immunoreactive striatalinterneurons expressed mGluR1a-like immunoreactivity with a slightly lowerpercentage (55%) expressing mGluR5-like immunoreactivity. These findingsindicate considerable heterogeneity among striatal projection andinterneurons with respect to mGluR1a and mGluR5 expression. There may besubpopulations of striatonigral and striatopallidal projection neurons.These results are consistent as well with prior data indicatingsubpopulations of the different classes of striatal interneurons.
- Metabolism (metabolic pathways involving proteins which contain this domain)
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Click the image to view the interactive version of the map in iPath% proteins involved KEGG pathway ID Description 74.65
map00010Glycolysis / Gluconeogenesis 9.43
map00051Fructose and mannose metabolism 3.89
map00860Porphyrin and chlorophyll metabolism 2.83
map00760Nicotinate and nicotinamide metabolism 2.83
map00740Riboflavin metabolism 2.83
map00530Aminosugars metabolism 2.83
map00730Thiamine metabolism 0.12
map00600Sphingolipid metabolism 0.12
map00603Glycosphingolipid biosynthesis - globoseries 0.12
map00561Glycerolipid metabolism 0.12
map00052Galactose metabolism 0.12
map00230Purine metabolism 0.12 map02010 ABC transporters - General This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with PGAM domain which could be assigned to a KEGG orthologous group, and not all proteins containing PGAM domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of PGAM domains in PDB
PDB code Main view Title 1bif 
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase bifunctional enzyme complexed with atp-g-s and phosphate 1bq3 
Saccharomyces cerevisiae phosphoglycerate mutase in complex with inositol hexakisphosphate 1bq4 
Saccharomyces cerevisiae phosphoglycerate mutase in complex with benzene hexacarboxylate 1c7z 
Regulatory complex of fructose-2,6-bisphosphatase 1c80 
Regulatory complex of fructose-2,6-bisphosphatase 1c81 
Michaelis complex of fructose-2,6-bisphosphatase 1e58 
E.coli cofactor-dependent phosphoglycerate mutase 1e59 
E.coli cofactor-dependent phosphoglycerate mutase complexed with vanadate 1ebb 
Bacillus stearothermophilus yhfr 1fbt 
The bisphosphatase domain of the bifunctional rat liver 6- phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1fzt 
Solution structure and dynamics of an open b-sheet, glycolytic enzyme-monomeric 23.7 kda phosphoglycerate mutase from schizosaccharomyces pombe 1h2e 
Bacillus stearothermophilus phoe (previously known as yhfr) in complex with phosphate 1h2f 
Bacillus stearothermophilus phoe (previously known as yhfr) in complex with trivanadate 1k6m 
Crystal structure of human liver 6-phosphofructo-2- kinase/fructose-2,6-bisphosphatase 1qhf 
Yeast phosphoglycerate mutase-3pg complex structure to 1.7 a 1rii 
Crystal structure of phosphoglycerate mutase from m. tuberculosis 1t8p 
Crystal structure of human erythrocyte 2,3- bisphosphoglycerate mutase 1tip 
The bisphosphatase domain of the bifunctional rat liver 6- phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1ujb 
Structure of the protein histidine phosphatase sixa 1ujc 
Structure of the protein histidine phosphatase sixa complexed with tungstate 1v37 
Crystal structure of phosphoglycerate mutase from thermus thermophilus hb8 1v7q 
Crystal structure of phosphoglycerate mutase from thermus thermophilus hb8 1xq9 
Structure of phosphoglycerate mutase from plasmodium falciparum at 2.6 resolution 1yfk 
Crystal structure of human b type phosphoglycerate mutase 1yjx 
Crystal structure of human b type phosphoglycerate mutase 2a6p 
Structure solution to 2.2 angstrom and functional characterisation of the open reading frame rv3214 from mycobacterium tuberculosis 2a9j 
Human bisphosphoglycerate mutase complexed with 3- phosphoglycerate (17 days) 2axn 
Crystal structure of the human inducible form 6- phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2bif 
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase h256a mutant with f6p in phosphatase active site 2dwo 
Pfkfb3 in complex with adp and pep 2dwp 
A pseudo substrate complex of 6-phosphofructo-2-kinase of pfkfb 2ekb 
Structural study of project id tthb049 from thermus thermophilus hb8 (l19m) 2ekz 
Structural study of project id tthb049 from thermus thermophilus hb8 (l52m) 2enu 
Mutant l121m structure of tthb049 from thermus thermophilus hb8 2enw 
Mutant y92h structure of tthb049 from thermus thermophilus hb8 2eoa 
Structural study of project id tthb049 from thermus thermophilus hb8 (w85h) 2f90 
Crystal structure of bisphosphoglycerate mutase in complex with 3-phosphoglycerate and alf4- 2h4x 
Human bisphosphoglycerate mutase complex with 3- phosphoglycerate with crystal growth 90 days 2h4z 
Human bisphosphoglycerate mutase complexed with 2,3- bisphosphoglycerate 2h52 
Crystal structure of human bisphosphoglycerate mutase complex with 3-phosphoglycerate (18 days) 2hhj 
Human bisphosphoglycerate mutase complexed with 2,3- bisphosphoglycerate (15 days) 2hia 
Crystal structure of tthb049 from thermus thermophilus hb8 2i1v 
Crystal structure of pfkfb3 in complex with adp and fructose-2,6-bisphosphate 2owd 
Crystal structure of tthb049 from thermus thermophilus hb8 2owe 
Crystal structure of tthb049 from thermus thermophilus hb8 2p2y 
Crystal structure of tthb049 from thermus thermophilus hb8 2p2z 
Crystal structure of tthb049 from thermus thermophilus hb8 2p30 
Crystal structure of tthb049 from thermus thermophilus hb8 2p6m 
Crystal structure of tthb049 from thermus thermophilus hb8 2p6o 
Crystal structure of tthb049 from thermus thermophilus hb8 2p75 
Crystal structure of tthb049 from thermus thermophilus hb8 2p77 
Crystal structure of tthb049 from thermus thermophilus hb8 2p78 
Crystal structure of tthb049 from thermus thermophilus hb8 2p79 
Crystal structure of tthb049 from thermus thermophilus hb8 2p9f 
Crystal structure of tthb049 from thermus thermophilus hb8 2p9y 
Crystal structure of tthb049 from thermus thermophilus hb8 2p9z 
Crystal structure of tthb049 from thermus thermophilus hb8 2pa0 
Crystal structure of tthb049 from thermus thermophilus hb8 2rfl 
Crystal structure of the putative phosphohistidine phosphatase sixa from agrobacterium tumefaciens 3bif 
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase empty 6-pf-2k active site 3d8h 
Crystal structure of phosphoglycerate mutase from cryptosporidium parvum, cgd7_4270 3dcy 
Crystal structure a tp53-induced glycolysis and apoptosis regulator protein from homo sapiens. 3e9c 
3e9d 
3e9e 
3eoz 
3ezn 
3f2i 
3f3k 
3fdz 
3fjy 
3gp3 
3gp5 
3gw8 
3hjg 
3kkk 
3pgm 
The structure of yeast phosphoglycerate mutase at 0.28 nm resolution 4pgm 
Saccharomyces cerevisiae phosphoglycerate mutase 5pgm 
Saccharomyces cerevisiae phosphoglycerate mutase - Links (links to other resources describing this domain)
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PFAM PGAM






