Q59637 (ODP1_PSEAE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 92.
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 Short name=PDH E1 component EC=1.2.4.1 | ||||||
| Gene names |
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| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 208964 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › ![]() |
Protein attributes
| Sequence length | 882 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2 By similarity. |
| Catalytic activity | Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. |
| Cofactor | Thiamine pyrophosphate By similarity. |
| Subunit structure | Homodimer By similarity. Makes part of the PDH complex, consisting of multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 882 | 882 | Pyruvate dehydrogenase E1 component | PRO_0000162247 | |||||
Experimental info | |||||||||
| Sequence conflict | 76 – 78 | 3 | IRS → DPLP in AAC45353. Ref.1 | ||||||
| Sequence conflict | 149 – 156 | 8 | EGRISEEQ → GRPHQRRNK in AAC45353. Ref.1 | ||||||
| Sequence conflict | 167 – 174 | 8 | NGLSSYPH → TACPPIRT in AAC45353. Ref.1 | ||||||
| Sequence conflict | 377 | 1 | Q → H in AAC45353. Ref.1 | ||||||
| Sequence conflict | 388 | 1 | G → V in AAC45353. Ref.1 | ||||||
| Sequence conflict | 392 | 1 | G → A in AAC45353. Ref.1 | ||||||
| Sequence conflict | 408 – 409 | 2 | Missing in AAC45353. Ref.1 | ||||||
| Sequence conflict | 517 | 1 | A → G in AAC45353. Ref.1 | ||||||
| Sequence conflict | 671 | 1 | Missing in AAC45353. Ref.1 | ||||||
| Sequence conflict | 740 | 1 | R → H in AAC45353. Ref.1 | ||||||
| Sequence conflict | 744 – 746 | 3 | GIG → DIV in AAC45353. Ref.1 | ||||||
| Sequence conflict | 760 – 765 | 6 | RDGLAV → HDDLTL in AAC45353. Ref.1 | ||||||
| Sequence conflict | 788 – 791 | 4 | GRRG → APSR in AAC45353. Ref.1 | ||||||
| Sequence conflict | 821 | 1 | Missing in AAC45353. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequences and expression of pyruvate dehydrogenase genes from Pseudomonas aeruginosa." Rae J.L., Cutfield J.F., Lamont I.L. J. Bacteriol. 179:3561-3571(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PAO. |
| [2] | "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. Olson M.V.Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U47920 Genomic DNA. Translation: AAC45353.1. AE004091 Genomic DNA. Translation: AAG08400.1. |
| PIR | G83018. |
| RefSeq | NP_253702.1. NC_002516.2. |
3D structure databases | |
| ProteinModelPortal | Q59637. |
| SMR | Q59637. Positions 54-879. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 208964.PA5015. |
Proteomic databases | |
| PRIDE | Q59637. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 881326. |
| KEGG | pae:PA5015. |
| PATRIC | 19844853. VBIPseAer58763_5255. |
Organism-specific databases | |
| PseudoCAP | PA5015. |
Phylogenomic databases | |
| eggNOG | COG2609. |
| HOGENOM | HOG000115215. |
| KO | K00163. |
| OMA | NLIFTIS. |
| ProtClustDB | PRK09405. |
Family and domain databases | |
| Gene3D | 3.40.50.920. 1 hit. |
| InterPro | IPR004660. 2-oxoA_DH_E1. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005474. Transketolase_N. [Graphical view] |
| Pfam | PF00456. Transketolase_N. 2 hits. [Graphical view] |
| PIRSF | PIRSF000156. Pyruvate_dh_E1. 1 hit. |
| SUPFAM | SSF52922. Transketo_C_like. 1 hit. |
| TIGRFAMs | TIGR00759. aceE. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODP1_PSEAE | ||||||||
| Accession | Primary (citable) accession number: Q59637 Secondary accession number(s): Q9HUF3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||

Clusters with
