Reviewed,
UniProtKB/Swiss-Prot O00330 (ODPX_HUMAN)
Last modified
June 16, 2009.
Version 94.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pyruvate dehydrogenase protein X component, mitochondrial Alternative name(s): Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex Lipoyl-containing pyruvate dehydrogenase complex component X E3-binding protein Short name=E3BP proX | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 501 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex. |
| Subunit structure | Eukaryotic pyruvate dehydrogenase complexes are organized about a core consisting of the oligomeric dihydrolipoamide acetyl-transferase, around which are arranged multiple copies of pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound by non-covalent bonds. |
| Subcellular location | |
| Involvement in disease | Defects in PDHX are a cause of lacticacidemia [MIM:245349]. |
| Sequence similarities | Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Coding sequence diversity | Polymorphism |
| Domain | Lipoyl Transit peptide |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acyltransferase activity Inferred from electronic annotation. Source: InterPro lipoic acid bindingInferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 53 | 53 | Mitochondrion By similarity | ||||||||||||||||||||||||||||||
| Chain | 54 – 501 | 448 | Pyruvate dehydrogenase protein X component, mitochondrial | PRO_0000020484 | |||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||
| Domain | 57 – 131 | 75 | Lipoyl-binding | ||||||||||||||||||||||||||||||
| Region | 183 – 214 | 32 | Interaction with DLD | ||||||||||||||||||||||||||||||
| Compositional bias | 149 – 170 | 22 | Pro-rich | ||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||
| Modified residue | 97 | 1 | N6-lipoyllysine By similarity | ||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||
| Natural variant | 23 | 1 | R → C: dbSNP rs1049306. Ref.1 | VAR_046619 | |||||||||||||||||||||||||||||
| Natural variant | 101 | 1 | T → A: dbSNP rs11539202. | VAR_046620 | |||||||||||||||||||||||||||||
| Natural variant | 370 | 1 | D → V: dbSNP rs17850649. Ref.5 | VAR_046621 | |||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||
| Mutagenesis | 183 | 1 | R → A: Strongly decreased DLD binding. Ref.9 | ||||||||||||||||||||||||||||||
| Mutagenesis | 185 | 1 | S → A: Strongly decreased DLD binding. Ref.9 | ||||||||||||||||||||||||||||||
| Mutagenesis | 186 | 1 | P → A: Strongly decreased DLD binding. Ref.9 | ||||||||||||||||||||||||||||||
| Mutagenesis | 187 | 1 | A → M: Strongly decreased DLD binding. Ref.9 | ||||||||||||||||||||||||||||||
| Mutagenesis | 189 | 1 | R → A: Strongly decreased DLD binding. Ref.9 | ||||||||||||||||||||||||||||||
| Mutagenesis | 190 | 1 | N → A: Strongly decreased DLD binding. Ref.9 | ||||||||||||||||||||||||||||||
| Mutagenesis | 193 | 1 | E → A: Strongly decreased DLD binding. Ref.9 | ||||||||||||||||||||||||||||||
| Mutagenesis | 208 | 1 | R → A: Strongly decreased DLD binding. Ref.9 | ||||||||||||||||||||||||||||||
| Mutagenesis | 210 | 1 | I → A: Strongly decreased DLD binding. Ref.9 | ||||||||||||||||||||||||||||||
| Mutagenesis | 213 | 1 | K → A: Strongly decreased DLD binding. Ref.9 | ||||||||||||||||||||||||||||||
| Mutagenesis | 214 | 1 | E → A: Strongly decreased DLD binding. Ref.9 | ||||||||||||||||||||||||||||||
| Sequence conflict | 41 | 1 | A → R in AAC39661. Ref.3 | ||||||||||||||||||||||||||||||
| Sequence conflict | 251 | 1 | A → S in AAB66315. Ref.1 | ||||||||||||||||||||||||||||||
| Sequence conflict | 251 | 1 | A → S in CAA73606. Ref.2 | ||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||
| Beta strand | 57 – 60 | 4 | |||||||||||||||||||||||||||||||
| Beta strand | 69 – 71 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 73 – 78 | 6 | |||||||||||||||||||||||||||||||
| Beta strand | 88 – 94 | 7 | |||||||||||||||||||||||||||||||
| Beta strand | 99 – 103 | 5 | |||||||||||||||||||||||||||||||
| Beta strand | 108 – 112 | 5 | |||||||||||||||||||||||||||||||
| Beta strand | 122 – 125 | 4 | |||||||||||||||||||||||||||||||
| Beta strand | 127 – 132 | 6 | |||||||||||||||||||||||||||||||
| Helix | 188 – 194 | 7 | |||||||||||||||||||||||||||||||
| Helix | 199 – 201 | 3 | |||||||||||||||||||||||||||||||
| Helix | 207 – 209 | 3 | |||||||||||||||||||||||||||||||
| Helix | 213 – 224 | 12 | |||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex." Harris R.A., Bowker-Kinley M.M., Wu P., Jeng J., Popov K.M. J. Biol. Chem. 272:19746-19751(1997) [PubMed: 9242632] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-23. |
| [2] | "Mutations in PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase-complex gene on chromosome 11p1, in congenital lactic acidosis." Aral B., Benelli C., Ait-Ghezala G., Amessou M., Fouque F., Maunoury C., Creau N., Kamoun P., Marsac C. Am. J. Hum. Genet. 61:1318-1326(1997) [PubMed: 9399911] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [3] | "Detection of a homozygous four base pair deletion in the protein X gene in a case of pyruvate dehydrogenase complex deficiency." Ling M., McEachern G., Seyda A., Mackay N., Scherer S.W., Bratinova S., Beatty B., Giovannucci-Uzielli M.L., Robinson B.H. Hum. Mol. Genet. 7:501-505(1998) [PubMed: 9467010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [4] | "Human gene sequence for PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase complex." Aral B., Dey R., Marsac C. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [5] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-370. Tissue: Brain. |
| [6] | "Large-scale concatenation cDNA sequencing." Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A. Genome Res. 7:353-358(1997) [PubMed: 9110174] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-501. Tissue: Brain. |
| [7] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [8] | "How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex." Ciszak E.M., Makal A., Hong Y.S., Vettaikkorumakankauv A.K., Korotchkina L.G., Patel M.S. J. Biol. Chem. 281:648-655(2006) [PubMed: 16263718] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 54-274 IN COMPLEX WITH DLD. |
| [9] | "Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex." Brautigam C.A., Wynn R.M., Chuang J.L., Machius M., Tomchick D.R., Chuang D.T. Structure 14:611-621(2006) [PubMed: 16442803] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 174-230 IN COMPLEX WITH DLD, MUTAGENESIS OF ARG-183; SER-185; PRO-186; ALA-187; ARG-189; ASN-190; GLU-193; ARG-208; ILE-210; LYS-213 AND GLU-214. |
| [10] | "Solution structure of RSGI RUH-054, a lipoyl domain from human 2-oxoacid dehydrogenase." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 57-141. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF001437 mRNA. Translation: AAB66315.1. Y13145 mRNA. Translation: CAA73606.1. U82328 mRNA. Translation: AAC39661.1. AJ298105 Genomic DNA. Translation: CAC18649.1. BC010389 mRNA. Translation: AAH10389.1. U79296 mRNA. Translation: AAB50223.1. | |||||||||||||||||||||||||||||||
| IPI | IPI00298423. | ||||||||||||||||||||||||||||||
| RefSeq | NP_001128496.1. NP_003468.2. | ||||||||||||||||||||||||||||||
| UniGene | Hs.502315 | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| DIP | DIP:29026N. | ||||||||||||||||||||||||||||||
| IntAct | O00330. 2 interactions. | ||||||||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||||||||
| PhosphoSite | O00330. | ||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||
| PeptideAtlas | O00330. | ||||||||||||||||||||||||||||||
| PRIDE | O00330. | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| Ensembl | ENSG00000110435. Homo sapiens. [Contig view] | ||||||||||||||||||||||||||||||
| GeneID | 8050. | ||||||||||||||||||||||||||||||
| NMPDR | fig|9606.3.peg.5459. | ||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||
| GeneCards | GC11P034894. | ||||||||||||||||||||||||||||||
| H-InvDB | HIX0009554. | ||||||||||||||||||||||||||||||
| HGNC | HGNC:21350. PDHX. | ||||||||||||||||||||||||||||||
| MIM | 245349. phenotype. 608769. gene. | ||||||||||||||||||||||||||||||
| Orphanet | 765. Pyruvate dehydrogenase deficiency. | ||||||||||||||||||||||||||||||
| PharmGKB | PA134976445. | ||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| HOGENOM | O00330. | ||||||||||||||||||||||||||||||
| HOVERGEN | O00330. | ||||||||||||||||||||||||||||||
| OMA | O00330. ADPIKIL. | ||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||
| Reactome | REACT_1505. Integration of energy metabolism. | ||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||
| ArrayExpress | O00330. | ||||||||||||||||||||||||||||||
| Bgee | O00330. | ||||||||||||||||||||||||||||||
| CleanEx | HS_PDHX. HS_PDX1. | ||||||||||||||||||||||||||||||
| GermOnline | ENSG00000110435. Homo sapiens. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| InterPro | IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. [Graphical view] | ||||||||||||||||||||||||||||||
| Pfam | PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| ProDom | PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||||||||||||||
| PROSITE | PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||||||||
| NextBio | 30644. | ||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | ODPX_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O00330 Secondary accession number(s): O60221, Q96FV8, Q99783 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 11 Human chromosome 11: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


