A1KKT4 (A1KKT4_MYCBP) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 35.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Pyruvate dehydrogenase E1 component PIRNR PIRNR000156 EC=1.2.4.1 PIRNR PIRNR000156 | ||||
| Gene names |
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| Organism | Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 410289 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 901 AA. |
| Sequence status | Complete. |
| 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. PIRNR PIRNR000156 |
| Catalytic activity | Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. PIRNR PIRNR000156 |
| Cofactor | Thiamine pyrophosphate By similarity. PIRNR PIRNR000156 |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyruvate PIRNR PIRNR000156 EMBL CAL72246.1 Thiamine pyrophosphate PIRNR PIRNR000156 |
| Molecular function | Oxidoreductase PIRNR PIRNR000156 EMBL CAL72246.1 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Molecular function | pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequences
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References
| [1] | "Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed: 17372194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
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| EMBL GenBank DDBJ | AM408590 Genomic DNA. Translation: CAL72246.1. |
| RefSeq | YP_978347.1. NC_008769.1. |
3D structure databases | |
| ProteinModelPortal | A1KKT4. |
| SMR | A1KKT4. Positions 56-891. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A1KKT4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000018359; EBMYCP00000018109; EBMYCG00000018354. |
| GeneID | 4697781. |
| GenomeReviews | Gene locus BCG_2258 in contig AM408590_GR. |
| KEGG | mbb:BCG_2258. |
| PATRIC | 18015414. VBIMycBov80988_2466. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2609. |
| GeneTree | EBGT00050000016271. |
| HOGENOM | HBG289271. |
| OMA | FRQEKSH. |
| ProtClustDB | PRK09405. |
Family and domain databases | |
| InterPro | IPR004660. 2-oxoA_DH_E1. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005474. Transketolase_N. [Graphical view] |
| Gene3D | G3DSA:3.40.50.920. Transketo_C_like. 1 hit. |
| KO | K00163. |
| PANTHER | PTHR11624:SF37. PTHR11624:SF37. 1 hit. |
| Pfam | PF00456. Transketolase_N. 1 hit. [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 | A1KKT4_MYCBP | ||||||||
| Accession | Primary (citable) accession number: A1KKT4 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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