B2HHR2 (B2HHR2_MYCMM) 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 marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 216594 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 929 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 ACC41760.1 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] | "Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis." Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. Cole S.T.Genome Res. 18:729-741(2008) [PubMed: 18403782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000854 Genomic DNA. Translation: ACC41760.1. |
| RefSeq | YP_001851615.1. NC_010612.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B2HHR2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000032896; EBMYCP00000031336; EBMYCG00000032891. |
| GeneID | 6227604. |
| GenomeReviews | Gene locus MMAR_3334 in contig CP000854_GR. |
| KEGG | mmi:MMAR_3334. |
| PATRIC | 18067783. VBIMycMar75906_3570. |
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. |
| 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 | B2HHR2_MYCMM | ||||||||
| Accession | Primary (citable) accession number: B2HHR2 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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