P16451 (ODPX_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 121.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Pyruvate dehydrogenase complex protein X component, mitochondrial Alternative name(s): Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex E3-binding protein Pyruvate dehydrogenase complex component E3BP | ||||||
| Gene names |
| ||||||
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome] | ||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › ![]() |
Protein attributes
| Sequence length | 410 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 (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds. |
| Subcellular location | |
| Miscellaneous | Present with 414 molecules/cell in log phase SD medium. |
| Sequence similarities | Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Lipoyl Transit peptide |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay PubMed 7947791. Source: SGD |
| Cellular_component | mitochondrial pyruvate dehydrogenase complex Inferred from direct assay Ref.6PubMed 7947791. Source: SGD |
| Molecular_function | structural molecule activity Inferred from direct assay Ref.6. Source: SGD transferase activity, transferring acyl groupsInferred 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 – 30 | 30 | Mitochondrion Ref.1 | ||||||
| Chain | 31 – 410 | 380 | Pyruvate dehydrogenase complex protein X component, mitochondrial | PRO_0000020487 | |||||
Regions | |||||||||
| Domain | 33 – 107 | 75 | Lipoyl-binding | ||||||
Amino acid modifications | |||||||||
| Modified residue | 73 | 1 | N6-lipoyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 378 | 1 | I → M in AAT93002. Ref.5 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae." Behal R.H., Browning K.S., Hall T.B., Reed L.J. Proc. Natl. Acad. Sci. U.S.A. 86:8732-8736(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-60 AND 192-206. |
| [2] | "The complete sequence of a 9037 bp DNA fragment of the right arm of Saccharomyces cerevisiae chromosome VII." Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., Nombela C. Yeast 11:587-591(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [3] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K.Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [4] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [5] | "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J.Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [6] | "Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene encoding the protein X component of the pyruvate dehydrogenase complex." Lawson J.E., Behal R.H., Reed L.J. Biochemistry 30:2834-2839(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS. |
| [7] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M28222 Genomic DNA. Translation: AAA34910.1. X82408 Genomic DNA. Translation: CAA57804.1. Z72978 Genomic DNA. Translation: CAA97219.1. AY692983 Genomic DNA. Translation: AAT93002.1. BK006941 Genomic DNA. Translation: DAA08286.1. |
| PIR | DEBYPX. A36183. |
| RefSeq | NP_011709.1. NM_001181322.1. |
3D structure databases | |
| ProteinModelPortal | P16451. |
| SMR | P16451. Positions 37-120, 169-211. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-5550N. |
| IntAct | P16451. 9 interactions. |
| MINT | MINT-508924. |
| STRING | 4932.YGR193C. |
Proteomic databases | |
| PaxDb | P16451. |
| PeptideAtlas | P16451. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | YGR193C; YGR193C; YGR193C. |
| GeneID | 853107. |
| KEGG | sce:YGR193C. |
Organism-specific databases | |
| CYGD | YGR193c. |
| SGD | S000003425. PDX1. |
Phylogenomic databases | |
| eggNOG | COG0508. |
| HOGENOM | HOG000246828. |
| OMA | EPIAYIA. |
| OrthoDB | EOG4QG0PK. |
Gene expression databases | |
| Genevestigator | P16451. |
| GermOnline | YGR193C. Saccharomyces cerevisiae. |
Family and domain databases | |
| Gene3D | 4.10.320.10. 1 hit. |
| InterPro | IPR003016. 2-oxoA_DH_lipoyl-BS. IPR000089. Biotin_lipoyl. IPR004167. E3-bd. IPR011053. Single_hybrid_motif. [Graphical view] |
| Pfam | PF00364. Biotin_lipoyl. 1 hit. [Graphical view] |
| SUPFAM | SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 1 hit. |
| PROSITE | PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 973115. |
Entry information
| Entry name | ODPX_YEAST | ||||||||
| Accession | Primary (citable) accession number: P16451 Secondary accession number(s): D6VUX5, E9P906 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome VII Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
