U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

PF3D7_1124500 pyruvate dehydrogenase E1 component subunit alpha [ Plasmodium falciparum 3D7 ]

Gene ID: 810803, updated on 16-Oct-2023

Summary

Go to the top of the page Help
Gene symbol
PF3D7_1124500
Gene description
pyruvate dehydrogenase E1 component subunit alpha
Locus tag
PF3D7_1124500
Gene type
protein coding
RNA name
pyruvate dehydrogenase E1 component subunit alpha
RefSeq status
PROVISIONAL
Organism
Plasmodium falciparum 3D7 (isolate: 3D7)
Lineage
Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; Plasmodiidae; Plasmodium; Plasmodium (Laverania)
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
Location:
chromosome: 11
Exon count:
1
Sequence:
Chromosome: 11; NC_037282.1 (966980..968806)

Chromosome 11 - NC_037282.1Genomic Context describing neighboring genes Neighboring gene conserved protein, unknown function Neighboring gene U6 snRNA-associated Sm-like protein LSm1, putative Neighboring gene ethanolamine kinase Neighboring gene GrpE protein homolog, mitochondrial, putative

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_037282.1

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Acquisition of exogenous fatty acids renders apicoplast-based biosynthesis dispensable in tachyzoites of Toxoplasma. Liang X, et al. J Biol Chem, 2020 May 29. PMID 32341123, Free PMC Article
  2. The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast. Foth BJ, et al. Mol Microbiol, 2005 Jan. PMID 15612915
  3. Integrative proteomics and bioinformatic prediction enable a high-confidence apicoplast proteome in malaria parasites. Boucher MJ, et al. PLoS Biol, 2018 Sep. PMID 30212465, Free PMC Article
  4. Genome sequence of the human malaria parasite Plasmodium falciparum. Gardner MJ, et al. Nature, 2002 Oct 3. PMID 12368864, Free PMC Article

GeneRIFs: Gene References Into Functions

General gene information

Go to the top of the page Help

Homology

Gene Ontology Provided by GeneDB

Process Evidence Code Pubs
acts_upstream_of_or_within acetyl-CoA biosynthetic process from pyruvate ISS
Inferred from Sequence or Structural Similarity
more info
  
acts_upstream_of_or_within fatty acid biosynthetic process ISO
Inferred from Sequence Orthology
more info
 PubMed 
Component Evidence Code Pubs
located_in apicoplast HDA PubMed 
located_in apicoplast IDA
Inferred from Direct Assay
more info
 PubMed 
part_of pyruvate dehydrogenase complex IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
pyruvate dehydrogenase E1 component subunit alpha
XP_001347927.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

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

Reference assembly

Genomic

  1. NC_037282.1 Reference assembly

    Range
    966980..968806
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_001347891.1 → XP_001347927.1  pyruvate dehydrogenase E1 component subunit alpha [Plasmodium falciparum 3D7]

    See identical proteins and their annotated locations for XP_001347927.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A024UYW7, A0A024VWN4, A0A024X5Z5, A0A0L1IEG7, A0A0L7KI54, A0A0L7M4D6, Q5VGY4, Q8IIB8, W4IG31, W4IU51, W7FD83, W7FG12, W7JAV1, W7K3Q0
    Conserved Domains (1) summary
    cl01629
    Location:190 → 526
    TPP_enzymes; Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and ...
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Molecular Biology Databases