PGK1 phosphoglycerate kinase [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: PGK1
Official Full Name: phosphoglycerate kinase
Primary source: SGD:S000000605
Locus tag: YCR012W
See related: AllianceGenome:SGD:S000000605; FungiDB:YCR012W; VEuPathDB:YCR012W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables phosphoglycerate kinase activity. Involved in gluconeogenesis and glycolytic process. Located in mitochondrion. Used to study cancer. Human ortholog(s) of this gene implicated in hemolytic anemia and phosphoglycerate kinase 1 deficiency. Orthologous to several human genes including PGK2 (phosphoglycerate kinase 2). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See PGK1 in Genome Data Viewer

Location:: chromosome: III

Exon count:: 1

Sequence:: Chromosome: III; NC_001135.5 (137746..138996)

Chromosome III - NC_001135.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001135.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Global mapping of protein-metabolite interactions in Saccharomyces cerevisiae reveals that Ser-Leu dipeptide regulates phosphoglycerate kinase activity.
Title: Global mapping of protein-metabolite interactions in Saccharomyces cerevisiae reveals that Ser-Leu dipeptide regulates phosphoglycerate kinase activity.
Overexpression of PGK1 restored normal ageing and suppress apoptotic phenotypes of the mutant.
Title: PGK1, the gene encoding the glycolitic enzyme phosphoglycerate kinase, acts as a multicopy suppressor of apoptotic phenotypes in S. cerevisiae.
The stability curve reveals the existence of two stable, folded conformers with an abrupt conformational transition occurring at 24 degrees C.
Title: Thermodynamic analysis of the nondenaturational conformational change of baker's yeast phosphoglycerate kinase at 24 degrees C.
Misfolding of the domains within the complete protein is synchronized indicating that domain-domain interactions direct the misfolding and amyloid formation mechanism.
Title: Domain interactions direct misfolding and amyloid formation of yeast phosphoglycerate kinase.
A thermodynamic transition intermediate was observed in the pressure-denaturation; the C-terminal domain carrying all the Trp residues seemed to exert structural changes at relatively lower pressure
Title: Pressure-temperature-induced denaturation of yeast phosphoglycerate kinase, a double-domain protein.
Data suggest that proteolysis occurs from the globally unfolded state of E. coli phosphoglycerate kinase, but upon unfolding of only the C-domain in the Saccharomyces enzyme, with the N-domain remaining folded and consequently resistant to cleavage.
Title: Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables ADP binding	IBA Inferred from Biological aspect of Ancestor more info
enables ATP binding	IBA Inferred from Biological aspect of Ancestor more info
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables kinase activity	IEA Inferred from Electronic Annotation more info
enables phosphoglycerate kinase activity	IBA Inferred from Biological aspect of Ancestor more info
enables phosphoglycerate kinase activity	IDA Inferred from Direct Assay more info	PubMed
enables phosphoglycerate kinase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in gluconeogenesis	IBA Inferred from Biological aspect of Ancestor more info
involved_in gluconeogenesis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in glycolytic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in glycolytic process	IEA Inferred from Electronic Annotation more info
involved_in glycolytic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	HDA more info	PubMed

General protein information

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Preferred Names: phosphoglycerate kinase

NP_009938.2

EC 2.7.2.3

3-phosphoglycerate kinase; catalyzes transfer of high-energy phosphoryl groups from the acyl phosphate of 1,3-bisphosphoglycerate to ADP to produce ATP; key enzyme in glycolysis and gluconeogenesis

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001135.5 Reference assembly

Range

137746..138996

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178725.1 → NP_009938.2 TPA: phosphoglycerate kinase [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009938.2

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VR21, P00560

UniProtKB/TrEMBL

A6ZTJ3, B3LU83, C7GQM4, C8Z499, G2WA29, N1P832

Conserved Domains (1) summary

cl00198
Location:3 → 415

Phosphoglycerate_kinase; Phosphoglycerate kinase (PGK) is a monomeric enzyme which catalyzes the transfer of the high-energy phosphate group of 1,3-bisphosphoglycerate to ADP, forming ATP and 3-phosphoglycerate. This reaction represents the first of the two substrate-level ...