Reviewed,
UniProtKB/Swiss-Prot P49432 (ODPB_RAT)
Last modified
November 4, 2008.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial Short name=PDHE1-B EC=1.2.4.1 | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 359 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 | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). |
| Catalytic activity | Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). |
| Cofactor | Thiamine pyrophosphate. |
| Subunit structure | Tetramer of 2 alpha and 2 beta subunits. |
| Subcellular location |
Ontologies
Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 30 | 30 | Mitochondrion | ||||||
| Chain | 31 – 359 | 329 | Pyruvate dehydrogenase E1 component subunit beta, mitochondrial | PRO_0000020459 | |||||
Sites | |||||||||
| Binding site | 89 | 1 | Thiamine pyrophosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 67 | 1 | Phosphotyrosine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 3 | 1 | A → G Ref.1 | ||||||
| Sequence conflict | 11 – 15 | 5 | PLRQA → LCGRL Ref.1 | ||||||
| Sequence conflict | 22 | 1 | R → L Ref.1 | ||||||
| Sequence conflict | 25 | 1 | R → C Ref.1 | ||||||
| Sequence conflict | 238 | 1 | T → N Ref.1 | ||||||
| Sequence conflict | 241 – 242 | 2 | AH → CY Ref.1 | ||||||
| Sequence conflict | 259 | 1 | E → G Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The alpha-ketoacid dehydrogenase complexes. Sequence similarity of rat pyruvate dehydrogenase with Escherichia coli and Azotobacter vinelandii alpha-ketoglutarate dehydrogenase." Matuda S., Nakano K., Ohta S., Saheki T., Kawanishi Y., Miyata T. Biochim. Biophys. Acta 1089:1-7(1991) [PubMed: 2025639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "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]. Tissue: Kidney. |
| [3] | Dunn M.J. Submitted (MAR-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 31-38. Tissue: Heart. |
| [4] | Lubec G., Afjehi-Sadat L., Diao W. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 286-324, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord. |
Cross-references
Sequence databases | |
|---|---|
| BC079137 mRNA. Translation: AAH79137.1. | |
| PIR | S15892. |
| RefSeq | NP_001007621.1. |
| UniGene | Rn.102424 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NI4 based on UniProtKB P11177. |
| SMR | P49432. Positions 30-359. |
| ModBase | Search... |
2-D gel databases | |
| HSC-2DPAGE | P49432. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000007895. Rattus norvegicus. [Contig view] |
| GeneID | 289950. |
| KEGG | rno:289950. |
| NMPDR | fig|10116.3.peg.11094. |
Organism-specific databases | |
| RGD | 1359146. Pdhb. |
Phylogenomic databases | |
| HOVERGEN | P49432. |
Gene expression databases | |
| ArrayExpress | P49432. |
| GermOnline | ENSRNOG00000007895. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR005476. Transketo_C. IPR005475. Transketo_Cen_R. IPR015941. Transketolase_C-like. [Graphical view] |
| Gene3D | G3DSA:3.40.50.920. Transketo_C_like. 1 hit. |
| Pfam | PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 630523. |
Entry information
| Entry name | ODPB_RAT | ||||||||
| Accession | Primary (citable) accession number: P49432 Secondary accession number(s): Q6AY95 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


