P10801 (ODP1_AZOVI) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 60.
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 EC=1.2.4.1 |
| Organism | Azotobacter vinelandii |
| Taxonomic identifier | 354 [NCBI] |
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter![]() |
Protein attributes
| Sequence length | 45 AA. |
| Sequence status | Fragment. |
| Protein existence | Predicted |
General annotation (Comments)
| Function | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. 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 + CO2. |
| Cofactor | Thiamine pyrophosphate. |
| Subunit structure | Homodimer. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis." Hanemaaijer R., Janssen A., de Kok A., Veeger C. Eur. J. Biochem. 174:593-599(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X12455 Genomic DNA. Translation: CAA30986.1. |
| PIR | S12208. |
3D structure databases | |
| ProteinModelPortal | P10801. |
| SMR | P10801. Positions 1-42. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.40.50.920. 1 hit. |
| InterPro | IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. [Graphical view] |
| SUPFAM | SSF52922. Transketo_C_like. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODP1_AZOVI | ||||||||
| Accession | Primary (citable) accession number: P10801 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||

Clusters with
