P26269 (ODPB_ASCSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 72.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial Short name=PDHE1-B EC=1.2.4.1 |
| Organism | Ascaris suum (Pig roundworm) (Ascaris lumbricoides) |
| Taxonomic identifier | 6253 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Ascaridida › Ascaridoidea › Ascarididae › Ascaris![]() |
Protein attributes
| Sequence length | 361 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 CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle. |
| Catalytic activity | Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. |
| Cofactor | Thiamine pyrophosphate. |
| Subunit structure | Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) By similarity. |
| Subcellular location |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | acetyl-CoA biosynthetic process from pyruvate Inferred from electronic annotation. Source: InterPro glucose metabolic processInferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycleInferred 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)
Sequences
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References
| [1] | "Characterization of cDNA clones for the beta subunit of pyruvate dehydrogenase from Ascaris suum." Wheelock M.J., Komuniecki R., Duran E., Johnson K.R. Mol. Biochem. Parasitol. 45:9-17(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-42. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M38017 mRNA. Translation: AAA29379.1. |
3D structure databases | |
| ProteinModelPortal | P26269. |
| SMR | P26269. Positions 31-360. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P26269. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.40.50.920. 1 hit. |
| InterPro | IPR027110. PDHB. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [Graphical view] |
| PANTHER | PTHR11624:SF11. PTHR11624:SF11. 1 hit. |
| Pfam | PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view] |
| SMART | SM00861. Transket_pyr. 1 hit. [Graphical view] |
| SUPFAM | SSF52922. Transketo_C_like. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODPB_ASCSU | ||||||||
| Accession | Primary (citable) accession number: P26269 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with
