A5WPL2 (A5WPL2_MYCTF) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 23.
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 |
| ||
| Organism | Mycobacterium tuberculosis (strain F11) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 336982 [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 ABR06601.1 Thiamine pyrophosphate PIRNR PIRNR000156 |
| Molecular function | Oxidoreductase PIRNR PIRNR000156 |
| 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] | "The complete genome sequence of Mycobacterium tuberculosis F11." Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., Grabherr M., Mauceli E., Brockman W., Young S., LaButti K., Pushparaj V., Sykes S., Baldwin J., Fitzgerald M., Bloom T., Zimmer A., Settipalli S. Murray M.Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000717 Genomic DNA. Translation: ABR06601.1. |
| RefSeq | YP_001288203.1. NC_009565.1. |
3D structure databases | |
| ProteinModelPortal | A5WPL2. |
| SMR | A5WPL2. Positions 56-891. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A5WPL2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5222947. |
| GenomeReviews | Gene locus TBFG_12270 in contig CP000717_GR. |
| KEGG | mtf:TBFG_12270. |
| PATRIC | 18135720. VBIMycTub9078_2508. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| 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 | A5WPL2_MYCTF | ||||||||
| Accession | Primary (citable) accession number: A5WPL2 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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