Reviewed,
UniProtKB/Swiss-Prot P0AFG9 (ODP1_ECO57)
Last modified
June 16, 2009.
Version 30.
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 EC=1.2.4.1 | ||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 887 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
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) By similarity. |
| Catalytic activity | Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. |
| Cofactor | Magnesium By similarity. Thiamine pyrophosphate By similarity. |
| Subunit structure | Homodimer By similarity. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Magnesium Metal-binding Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyruvate dehydrogenase (acetyl-transferring) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 887 | 886 | Pyruvate dehydrogenase E1 component | PRO_0000162244 | |||||
Sites | |||||||||
| Metal binding | 231 | 1 | Magnesium By similarity | ||||||
| Metal binding | 261 | 1 | Magnesium By similarity | ||||||
| Metal binding | 263 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 716 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG54418.1. BA000007 Genomic DNA. Translation: BAB33541.1. | |
| PIR | F85494. F90643. |
| RefSeq | NP_285810.1. NP_308145.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 913657. 956809. |
| GenomeReviews | Gene locus Z0124 in contig AE005174_GR. Gene locus ECs0118 in contig BA000007_GR. |
| KEGG | ece:Z0124. ecs:ECs0118. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0AFG9. |
| OMA | P0AFG9. REISTTQ. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS0118-MON. |
Family and domain databases | |
| InterPro | IPR004660. 2-oxoA_DH_E1. IPR005474. Transketo_N. IPR015941. Transketolase_C-like. [Graphical view] |
| Gene3D | G3DSA:3.40.50.920. Transketo_C_like. 1 hit. |
| Pfam | PF00456. Transketolase_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000156. Pyruvate_dh_E1. 1 hit. |
| TIGRFAMs | TIGR00759. aceE. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODP1_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0AFG9 Secondary accession number(s): P06958, P78049, Q53382 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


