GPM1/YKL152C Summary Help

Standard Name GPM1 1
Systematic Name YKL152C
Feature Type ORF, Verified
Description Tetrameric phosphoglycerate mutase; mediates the conversion of 3-phosphoglycerate to 2-phosphoglycerate during glycolysis and the reverse reaction during gluconeogenesis (2, 3 and see Summary Paragraph)
Name Description Glycerate PhosphoMutase 1
Chromosomal Location
ChrXI:164385 to 163642 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All GPM1 GO evidence and references
  View Computational GO annotations for GPM1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 18 genes
Classical genetics
reduction of function
Large-scale survey
65 total interaction(s) for 52 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 43
  • Affinity Capture-RNA: 5
  • Affinity Capture-Western: 1
  • Biochemical Activity: 1
  • Co-crystal Structure: 1
  • Co-purification: 2
  • PCA: 3
  • Protein-peptide: 1
  • Reconstituted Complex: 1
  • Two-hybrid: 3

Genetic Interactions
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 2

Expression Summary
Length (a.a.) 247
Molecular Weight (Da) 27,608
Isoelectric Point (pI) 9.65
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXI:164385 to 163642 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..744 164385..163642 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001635

GPM1 encodes phosphoglycerate mutase (4), which is a tetrameric enzyme responsible for the conversion of 3-phospholycerate to 2-phosphoglycerate during glycolysis (5,6), and the reverse reaction during gluconeogenesis (7,3). As such, Gpm1p is required for growth on glucose, glycerol, or ethanol as a sole carbon source (4). Homozygous diploid gpm1 mutant cells fail to sporulate, an observation indicating that gluconeogenesis is required for sporulation (8).

Gluconeogenesis is the process whereby glucose is synthesized from non-carbohydrate precursors, which enables yeast cells to grow on non-sugar carbon sources like ethanol, glycerol, or peptone. The reactions of gluconeogenesis, shown here, mediate conversion of pyruvate to glucose, which is the opposite of glycolysis, the formation of pyruvate from glucose. While these two pathways have several reactions in common, they are not the exact reverse of each other. As the glycolytic enzymes phosphofructokinase (Pfk1p, Pfk2p) and pyruvate kinase (Cdc19p) only function in the forward direction, the gluconeogenesis pathway replaces those steps with the enzymes pyruvate carboxylase (Pyc1p, Pyc2p) and phosphoenolpyruvate carboxykinase (Pck1p)-generating oxaloacetate as an intermediate from pyruvate to phosphoenolpyruvate-and also the enzyme fructose-1,6-bisphosphatase (Fbp1p) (reviewed in 9). Overall, the gluconeogenic reactions convert two molecules of pyruvate to a molecule of glucose, with the expenditure of six high-energy phosphate bonds, four from ATP and two from GTP.

The GPM1 promoter has been extensively characterized (2). It contains separate regulatory elements for transcriptional activation and repression: two upstream repressing (URS) sites and one UAS (upstream activating) site are found upstream of the translational start codon. This region also contains binding sites for the transcriptional activator of glycolysis Gcr1p and the activator Rap1p.

The active-site residues of Gpm1p (His8, Arg59, and His181) have also been identified (10, 11). Two yeast sequences homologous to GPM1, designated GPM2 and GPM3, contain these active site residues. However, neither gene complements a gpm1 deletion mutant and it has been demonstrated that glycolysis is not affected in either the gpm2 or gpm3 single or double deletion mutants. In fact, neither mutation confers an obvious phenotype, suggesting that both GPM2 and GPM3 likely evolved from duplication events and appear to constitute non-functional homologs of GPM1 in yeast (12).

Last updated: 2005-07-22 Contact SGD

References cited on this page View Complete Literature Guide for GPM1
1) Heinisch J, et al.  (1991) Sequence and localization of the gene encoding yeast phosphoglycerate mutase. Curr Genet 20(1-2):167-71
2) Rodicio R, et al.  (1993) Transcriptional control of yeast phosphoglycerate mutase-encoding gene. Gene 125(2):125-33
3) Lam KB and Marmur J  (1977) Isolation and characterization of Saccharomyces cerevisiae glycolytic pathway mutants. J Bacteriol 130(2):746-9
4) Rodicio R and Heinisch J  (1987) Isolation of the yeast phosphoglyceromutase gene and construction of deletion mutants. Mol Gen Genet 206(1):133-40
5) Peter Smits H, et al.  (2000) Simultaneous overexpression of enzymes of the lower part of glycolysis can enhance the fermentative capacity of Saccharomyces cerevisiae. Yeast 16(14):1325-34
6) Price NC and Jaenicke R  (1982) The quaternary structure of phosphoglycerate mutase from yeast: evidence against dissociation of the tetrameric enzyme at low concentrations. FEBS Lett 143(2):283-6
7) Sasaki R, et al.  (1976) Subunit structure and multifunctional properties of yeast phosphoglyceromutase. Eur J Biochem 66(3):523-33
8) Dickinson JR and Williams AS  (1986) A genetic and biochemical analysis of the role of gluconeogenesis in sporulation of Saccharomyces cerevisiae. J Gen Microbiol 132(9):2605-10
9) Klein CJ, et al.  (1998) Glucose control in Saccharomyces cerevisiae: the role of Mig1 in metabolic functions. Microbiology 144 ( Pt 1)():13-24
10) White MF and Fothergill-Gilmore LA  (1992) Development of a mutagenesis, expression and purification system for yeast phosphoglycerate mutase. Investigation of the role of active-site His181. Eur J Biochem 207(2):709-14
11) White MF and Fothergill-Gilmore LA  (1990) Mutase versus synthase: the phosphoglycerate mutase family studied by protein engineering. Biochem Soc Trans 18(2):257
12) Heinisch JJ, et al.  (1998) Investigation of two yeast genes encoding putative isoenzymes of phosphoglycerate mutase. Yeast 14(3):203-13