B8ZRY5 (B8ZRY5_MYCLB) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 25.
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 leprae (strain Br4923) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 561304 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 936 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 CAR71746.1 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] | "Comparative genomic and phylogeographic analysis of Mycobacterium leprae." Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A., Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C., Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H., Vera-Cabrera L. Cole S.T.Nat. Genet. 41:1282-1289(2009) [PubMed: 19881526] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FM211192 Genomic DNA. Translation: CAR71746.1. |
| RefSeq | YP_002503762.1. NC_011896.1. |
3D structure databases | |
| ProteinModelPortal | B8ZRY5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B8ZRY5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000085736; EBMYCP00000082766; EBMYCG00000086759. |
| GeneID | 7326772. |
| GenomeReviews | Gene locus MLBr01651 in contig FM211192_GR. |
| PATRIC | 18045826. VBIMycLep121698_3129. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| 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. |
| 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 | B8ZRY5_MYCLB | ||||||||
| Accession | Primary (citable) accession number: B8ZRY5 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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