Reviewed,
UniProtKB/Swiss-Prot A1UK81 (KGD_MYCSK)
Last modified
June 16, 2009.
Version 21.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 2-oxoglutarate decarboxylase EC=4.1.1.71 Alternative name(s): Alpha-ketoglutarate decarboxylase 2-oxoglutarate carboxy-lyase | ||||
| Gene names |
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| Organism | Mycobacterium sp. (strain KMS) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 189918 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 1269 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes an oxidative decarboxylation from five-carbon 2-oxoglutarate (alpha-ketoglutarate) to four-carbon succinate semialdehyde By similarity. |
| Catalytic activity | 2-oxoglutarate = succinate semialdehyde + CO2. |
| Cofactor | Magnesium By similarity. Thiamine pyrophosphate By similarity. |
| Sequence similarities | Belongs to the 2-oxoacid dehydrogenase family. Kgd subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Domain | Coiled coil |
| Ligand | Magnesium Thiamine pyrophosphate |
| Molecular function | Decarboxylase Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 2-oxoglutarate decarboxylase activity Inferred from electronic annotation. Source: EC acyltransferase activityInferred from electronic annotation. Source: InterPro magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW oxoglutarate dehydrogenase (succinyl-transferring) activityInferred from electronic annotation. Source: InterPro thiamin pyrophosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Complete sequence of chromosome of Mycobacterium sp. KMS." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. Richardson P.Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000518 Genomic DNA. Translation: ABL93239.1. | |
| RefSeq | YP_940029.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4611987. |
| GenomeReviews | Gene locus Mkms_4047 in contig CP000518_GR. |
| KEGG | mkm:Mkms_4047. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | A1UK81. EGDEPAF. |
Family and domain databases | |
| InterPro | IPR001078. 2-oxoacid_DH_actylTfrase. IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase_central-reg. [Graphical view] |
| PANTHER | PTHR23152. 2oxoglutarate_DH_E1. 1 hit. |
| Pfam | PF00198. 2-oxoacid_dh. 1 hit. PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view] |
| PIRSF | PIRSF000157. Oxoglu_dh_E1. 1 hit. |
| ProDom | PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00239. 2oxo_dh_E1. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | KGD_MYCSK | ||||||||
| Accession | Primary (citable) accession number: A1UK81 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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