O00330 · ODPX_HUMAN
- ProteinPyruvate dehydrogenase protein X component, mitochondrial
- GenePDHX
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids501 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Cellular Component | pyruvate dehydrogenase complex | |
Molecular Function | acyltransferase activity | |
Biological Process | acetyl-CoA biosynthetic process from pyruvate |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate dehydrogenase protein X component, mitochondrial
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00330
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Pyruvate dehydrogenase E3-binding protein deficiency (PDHXD)
- Note
- DescriptionA metabolic disorder characterized by decreased activity of the pyruvate dehydrogenase complex without observable reduction in the activities of enzymes E1, E2, or E3. Clinical features include hypotonia and psychomotor retardation.
- See alsoMIM:245349
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_046619 | 23 | in dbSNP:rs1049306 | |||
Sequence: R → C | ||||||
Natural variant | VAR_046620 | 101 | in dbSNP:rs11539202 | |||
Sequence: T → A | ||||||
Mutagenesis | 183 | Strongly decreased DLD binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 185 | Strongly decreased DLD binding. | ||||
Sequence: S → A | ||||||
Mutagenesis | 186 | Strongly decreased DLD binding. | ||||
Sequence: P → A | ||||||
Mutagenesis | 187 | Strongly decreased DLD binding. | ||||
Sequence: A → M | ||||||
Mutagenesis | 189 | Strongly decreased DLD binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 190 | Decreased DLD binding. | ||||
Sequence: N → A | ||||||
Mutagenesis | 190 | Moderately decreased interaction with DLD. | ||||
Sequence: N → K | ||||||
Mutagenesis | 193 | Strongly decreased DLD binding. | ||||
Sequence: E → A | ||||||
Mutagenesis | 208 | Strongly decreased DLD binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 208 | Decreased interaction with DLD. | ||||
Sequence: R → D | ||||||
Mutagenesis | 210 | Strongly decreased DLD binding. | ||||
Sequence: I → A | ||||||
Mutagenesis | 210 | Decreased interaction with DLD. | ||||
Sequence: I → R | ||||||
Mutagenesis | 210 | Decreased interaction with DLD. | ||||
Sequence: I → S | ||||||
Mutagenesis | 213 | Strongly decreased DLD binding. | ||||
Sequence: K → A | ||||||
Mutagenesis | 214 | Strongly decreased DLD binding. | ||||
Sequence: E → A | ||||||
Natural variant | VAR_046621 | 370 | in dbSNP:rs17850649 | |||
Sequence: D → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 630 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-53 | UniProt | Mitochondrion | ||||
Sequence: MAASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLR | |||||||
Chain | PRO_0000020484 | 54-501 | UniProt | Pyruvate dehydrogenase protein X component, mitochondrial | |||
Sequence: GDPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGEDWKHVEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKITESRPTPAPTATPTAPSPLQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEEGNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRLA | |||||||
Modified residue (large scale data) | 67 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 97 | UniProt | N6-lipoyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 168 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 194 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 196 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 196 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 394 | UniProt | N6-succinyllysine | ||||
Sequence: K |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
This core binds multiple copies of pyruvate dehydrogenase (subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) (PubMed:14638692).
Interacts with SIRT4 (PubMed:25525879).
Interacts with DLD (PubMed:16263718, PubMed:16442803, PubMed:20160912, PubMed:20361979, PubMed:20385101).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00330 | AGTRAP Q6RW13 | 5 | EBI-751566, EBI-741181 | |
BINARY | O00330 | CIDEB Q9UHD4 | 3 | EBI-751566, EBI-7062247 | |
BINARY | O00330 | DLD P09622 | 8 | EBI-751566, EBI-353366 | |
BINARY | O00330 | SIRT4 Q9Y6E7 | 4 | EBI-751566, EBI-2606540 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 56-132 | Lipoyl-binding | ||||
Sequence: PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIV | ||||||
Region | 142-175 | Disordered | ||||
Sequence: EIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEH | ||||||
Compositional bias | 145-166 | Pro residues | ||||
Sequence: KDVGPPPPVSKPSEPRPSPEPQ | ||||||
Domain | 183-220 | Peripheral subunit-binding (PSBD) | ||||
Sequence: RLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLV | ||||||
Region | 225-268 | Disordered | ||||
Sequence: TGKITESRPTPAPTATPTAPSPLQATAGPSYPRPVIPPVSTPGQ |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 3 isoforms produced by Alternative splicing.
O00330-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length501
- Mass (Da)54,122
- Last updated2001-01-24 v3
- Checksum9CF0C1DAE9E12EF9
O00330-2
- Name2
- Differences from canonical
- 115-341: Missing
O00330-3
- Name3
- Differences from canonical
- 2-53: AASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLR → QSGGAEGSPGAGRTGRGPGSGKAPPAEISSGAPDFPG
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YD97 | H0YD97_HUMAN | PDHX | 189 | ||
E9PRI6 | E9PRI6_HUMAN | PDHX | 182 | ||
E9PLU0 | E9PLU0_HUMAN | PDHX | 151 | ||
A0A8C8MSB2 | A0A8C8MSB2_HUMAN | PDHX | 441 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_053817 | 2-53 | in isoform 3 | |||
Sequence: AASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLR → QSGGAEGSPGAGRTGRGPGSGKAPPAEISSGAPDFPG | ||||||
Sequence conflict | 41 | in Ref. 3; AAC39661 | ||||
Sequence: A → R | ||||||
Alternative sequence | VSP_045271 | 115-341 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 145-166 | Pro residues | ||||
Sequence: KDVGPPPPVSKPSEPRPSPEPQ | ||||||
Sequence conflict | 251 | in Ref. 1; AAB66315 and 2; CAA73606 | ||||
Sequence: A → S | ||||||
Sequence conflict | 344 | in Ref. 5; BAG62924 | ||||
Sequence: P → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF001437 EMBL· GenBank· DDBJ | AAB66315.1 EMBL· GenBank· DDBJ | mRNA | ||
Y13145 EMBL· GenBank· DDBJ | CAA73606.1 EMBL· GenBank· DDBJ | mRNA | ||
U82328 EMBL· GenBank· DDBJ | AAC39661.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ298105 EMBL· GenBank· DDBJ | CAC18649.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK301384 EMBL· GenBank· DDBJ | BAG62924.1 EMBL· GenBank· DDBJ | mRNA | ||
AC107928 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL138810 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL356215 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471064 EMBL· GenBank· DDBJ | EAW68158.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW68160.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC010389 EMBL· GenBank· DDBJ | AAH10389.1 EMBL· GenBank· DDBJ | mRNA | ||
U79296 EMBL· GenBank· DDBJ | AAB50223.1 EMBL· GenBank· DDBJ | mRNA |