PDX1/YGR193C Summary Help

Standard Name PDX1 1
Systematic Name YGR193C
Feature Type ORF, Verified
Description E3-binding protein of the mitochondrial pyruvate dehydrogenase complex; plays a structural role in the complex by binding and positioning dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide acetyltransferase (E2) core (1, 2, 3 and see Summary Paragraph)
Name Description Pyruvate Dehydrogenase complex protein X 1
Chromosomal Location
ChrVII:885741 to 884509 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All PDX1 GO evidence and references
  View Computational GO annotations for PDX1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 3 genes
Resources
Large-scale survey
null
Resources
39 total interaction(s) for 31 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 14
  • Affinity Capture-RNA: 1
  • Co-crystal Structure: 1
  • Co-fractionation: 1

Genetic Interactions
  • Dosage Growth Defect: 1
  • Negative Genetic: 15
  • Positive Genetic: 1
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 2
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 410
Molecular Weight (Da) 45,361
Isoelectric Point (pI) 5.49
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVII:885741 to 884509 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1233 885741..884509 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003425
SUMMARY PARAGRAPH for PDX1

PDX1 encodes the Protein X (E3-binding) subunit of the mitochondrial pyruvate dehydrogenase multienzyme complex (2). The pyruvate dehydrogenase complex consists of an E2 (Lat1p) core that binds E1 (Pda1p and Pdb1p), E3 (Lpd1p) and Protein X (Pdx1p) subunits (4). E1, E2, and E3 have catalytic activity; Pdx1p appears to be required for binding of the E3 subunit to the central E2 core (1). Cells lacking PDX1 are viable, but the pyruvate dehydrogenase complex is inactive (1). Mutations in the human homolog of PDX1 appear to be responsible for some cases of neonatal lactic acidosis (5).

Last updated: 2000-03-01 Contact SGD

References cited on this page View Complete Literature Guide for PDX1
1) Lawson JE, et al.  (1991) Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene encoding the protein X component of the pyruvate dehydrogenase complex. Biochemistry 30(11):2834-9
2) Behal RH, et al.  (1989) Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 86(22):8732-6
3) Maeng CY, et al.  (1994) Expression, purification, and characterization of the dihydrolipoamide dehydrogenase-binding protein of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae. Biochemistry 33(46):13801-7
4) Pronk JT, et al.  (1996) Pyruvate metabolism in Saccharomyces cerevisiae. Yeast 12(16):1607-33
5) Aral B, et al.  (1997) Mutations in PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase-complex gene on chromosome 11p1, in congenital lactic acidosis. Am J Hum Genet 61(6):1318-26