Reviewed,
UniProtKB/Swiss-Prot Q9ZDR3 (ODPB_RICPR)
Last modified
November 4, 2008.
Version 49.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pyruvate dehydrogenase E1 component subunit beta EC=1.2.4.1 | ||||
| Gene names |
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| Organism | Rickettsia prowazekii [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 782 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group |
Protein attributes
| Sequence length | 326 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
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) By similarity. |
| Catalytic activity | Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). |
| Cofactor | Thiamine pyrophosphate By similarity. |
| Subunit structure | Heterodimer of an alpha and a beta chain. |
Ontologies
Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| 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 | pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The genome sequence of Rickettsia prowazekii and the origin of mitochondria." Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G. Nature 396:133-140(1998) [PubMed: 9823893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Madrid E. |
Cross-references
Sequence databases | |
|---|---|
| AJ235271 Genomic DNA. Translation: CAA14724.1. | |
| PIR | B71681. |
| RefSeq | NP_220647.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1IK6 based on UniProtKB Q8ZUR7. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 883167. |
| GenomeReviews | Gene locus RP262 in contig AJ235269_GR. |
| KEGG | rpr:RP262. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9ZDR3. |
Enzyme and pathway databases | |
| BioCyc | RPRO272947:RP262-MON. |
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] |
| BLOCKS | Search... |
| ProtoNet | Search... |
Entry information
| Entry name | ODPB_RICPR | ||||||||
| Accession | Primary (citable) accession number: Q9ZDR3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Rickettsia prowazekii Rickettsia prowazekii (strain Madrid E): entries and gene names |

Clusters with


