CDC19 pyruvate kinase CDC19 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: CDC19
Gene description: pyruvate kinase CDC19
Primary source: FungiDB:YAL038W
Locus tag: YAL038W
See related: SGD:S000000036; AllianceGenome:SGD:S000000036
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: PYK1
Summary: Enables pyruvate kinase activity. Involved in glycolytic process. Located in cytoplasm. Human ortholog(s) of this gene implicated in Gaucher's disease; congenital nonspherocytic hemolytic anemia; malaria; pyruvate kinase deficiency of red cells; and type 2 diabetes mellitus. Orthologous to human PKLR (pyruvate kinase L/R) and PKM (pyruvate kinase M1/2). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:: chromosome: I

Exon count:: 1

Sequence:: Chromosome: I; NC_001133.9 (71786..73288)

Chromosome I - NC_001133.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001133.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Protein aggregation and the evolution of stress resistance in clinical yeast.
Title: Protein aggregation and the evolution of stress resistance in clinical yeast.
Cdc19 aggregation in vitro is governed by protein quaternary structure. Cdc19 aggregates share several structural features with pathological amyloids formed by human insulin and the Alzheimer's disease-associated ABETA42 peptide.
Title: A hydrophobic low-complexity region regulates aggregation of the yeast pyruvate kinase Cdc19 into amyloid-like aggregates in vitro.
Reversible aggregation protects Cdc19 from stress-induced degradation, thereby allowing cell cycle restart after stress.
Title: Reversible protein aggregation is a protective mechanism to ensure cell cycle restart after stress.
Data show that the pyruvate-forming enzyme Pyk1 was tethered to heterologous pyruvate-converting enzymes, lactate dehydrogenase and alpha-acetolactate synthase, to producelactic acid and 2,3-butanediol, respectively.
Title: Redirection of pyruvate flux toward desired metabolic pathways through substrate channeling between pyruvate kinase and pyruvate-converting enzymes in Saccharomyces cerevisiae.
CDC19 allele from the Htg(+)Saccharomyces cereviseae strain had 7 base changes resulting in silent mutations in its coding region. The base changes increased pyruvate kinase activity and activation of energy metabolism to maintain cellular homeostasis.
Title: CDC19 encoding pyruvate kinase is important for high-temperature tolerance in Saccharomyces cerevisiae.
In yeast the major PKA phosphorylation site of Pyk1 is Ser22. Phosphorylation of Ser22 leads to a Pyk1 enzyme that is more active in the absence of fructose 1,6-bisphosphate
Title: Characterization of yeast pyruvate kinase 1 as a protein kinase A substrate, and specificity of the phosphorylation site sequence in the whole protein.

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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 ATP binding	IEA Inferred from Electronic Annotation more info
enables kinase activity	IEA Inferred from Electronic Annotation more info
enables magnesium ion binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables potassium ion binding	IEA Inferred from Electronic Annotation more info
enables pyruvate kinase activity	IBA Inferred from Biological aspect of Ancestor more info
enables pyruvate kinase activity	IDA Inferred from Direct Assay more info	PubMed
enables pyruvate kinase activity	IEA Inferred from Electronic Annotation more info
enables pyruvate kinase activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
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
involved_in monocarboxylic acid metabolic process	IEA Inferred from Electronic Annotation more info
involved_in pyruvate metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed

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

General protein information

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Preferred Names: pyruvate kinase CDC19

NP_009362.1

EC 2.7.1.40

Pyruvate kinase; functions as a homotetramer in glycolysis to convert phosphoenolpyruvate to pyruvate, the input for aerobic (TCA cycle) or anaerobic (glucose fermentation) respiration; regulated via allosteric activation by fructose bisphosphate; CDC19 has a paralog, PYK2, that arose from the whole genome duplication

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_001133.9 Reference assembly

Range

71786..73288

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178183.1 → NP_009362.1 TPA: pyruvate kinase CDC19 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009362.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VPH8, P00549, Q2VQG5

UniProtKB/TrEMBL

A0A6A5PVI5, A7A0C8, B3LUX4, B5VDI0, C7GU44, C8Z3F1, G2W8J2, N1P8V5

Conserved Domains (1) summary

cd00288
Location:18 → 500

Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...