Reviewed,
UniProtKB/Swiss-Prot Q72GU1 (ODBA_THET2)
Last modified
November 4, 2008.
Version 28.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 2-oxoisovalerate dehydrogenase subunit alpha EC=1.2.4.4 Alternative name(s): Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain Short name=BCKDH E1-alpha | ||
| Gene names |
| ||
| Organism | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 262724 [NCBI] | ||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
Protein attributes
| Sequence length | 367 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. |
| Catalytic activity | 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO(2). |
| Cofactor | Thiamine pyrophosphate By similarity. |
| Subunit structure | Heterotetramer of two alpha and two beta chains. Directly associated with ODBB in the E1 complex By similarity. |
| Sequence similarities | Belongs to the BCKDHA family. |
Ontologies
Keywords | |
|---|---|
| Ligand | Magnesium Metal-binding Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 367 | 367 | 2-oxoisovalerate dehydrogenase subunit alpha | PRO_0000294974 | |||||
Regions | |||||||||
| Region | 94 – 96 | 3 | Thiamine pyrophosphate binding By similarity | ||||||
| Region | 128 – 131 | 4 | Substrate binding By similarity | ||||||
| Region | 144 – 146 | 3 | Thiamine pyrophosphate binding By similarity | ||||||
| Region | 174 – 180 | 7 | Thiamine pyrophosphate binding By similarity | ||||||
| Region | 204 – 208 | 5 | Thiamine pyrophosphate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 175 | 1 | Magnesium By similarity | ||||||
| Metal binding | 204 | 1 | Magnesium By similarity | ||||||
| Metal binding | 206 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Binding site | 66 | 1 | Substrate By similarity | ||||||
| Binding site | 95 | 1 | Substrate By similarity | ||||||
| Binding site | 144 | 1 | Substrate By similarity | ||||||
| Binding site | 273 | 1 | Thiamine pyrophosphate By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of the extreme thermophile Thermus thermophilus." Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J. Nat. Biotechnol. 22:547-553(2004) [PubMed: 15064768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AE017221 Genomic DNA. Translation: AAS82099.1. | |
| RefSeq | YP_005726.1. |
3D structure databases | |
| SMR | Q72GU1. Positions 6-367. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2776443. |
| GenomeReviews | Gene locus TT_C1757 in contig AE017221_GR. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q72GU1. |
Enzyme and pathway databases | |
| BioCyc | TTHE262724:TT_C1757-MON. |
Family and domain databases | |
| InterPro | IPR001017. DHase_E1. [Graphical view] |
| Pfam | PF00676. E1_dh. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ODBA_THET2 | ||||||||
| Accession | Primary (citable) accession number: Q72GU1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


