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CDC19 pyruvate kinase CDC19 [ Saccharomyces cerevisiae S288C ]

Gene ID: 851193, updated on 9-Dec-2024

Summary

Official Symbol
CDC19
Official Full Name
pyruvate kinase CDC19
Primary source
SGD:S000000036
Locus tag
YAL038W
See related
AllianceGenome:SGD:S000000036; FungiDB:YAL038W; VEuPathDB:YAL038W
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. Orthologous to human PKM (pyruvate kinase M1/2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

See CDC19 in Genome Data Viewer
Location:
chromosome: I
Exon count:
1
Sequence:
Chromosome: I; NC_001133.9 (71786..73288)

Chromosome I - NC_001133.9Genomic Context describing neighboring genes Neighboring gene cyclin CLN3 Neighboring gene holocytochrome c synthase CYC3 Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein

Bibliography

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

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 PubMed 

General protein information

Preferred Names
pyruvate kinase CDC19
NP_009362.1
  • 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

  1. NC_001133.9 Reference assembly

    Range
    71786..73288
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001178183.1NP_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
    A7A0C8, B3LUX4, B5VDI0, C7GU44, C8Z3F1, G2W8J2, N1P8V5
    Conserved Domains (1) summary
    cd00288
    Location:18500
    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 ...