Reviewed,
UniProtKB/Swiss-Prot Q9I1M2 (ODBA_PSEAE)
Last modified
November 3, 2009.
Version 48.
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 |
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| Organism | Pseudomonas aeruginosa [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 287 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 410 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 CO2. 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 + CO2. |
| Cofactor | Thiamine pyrophosphate By similarity. |
| Subunit structure | Heterodimer of an alpha and a beta chain By similarity. |
| Sequence similarities | Belongs to the BCKDHA family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | 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 |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 410 | 410 | 2-oxoisovalerate dehydrogenase subunit alpha | PRO_0000287782 | |||
Sequences
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References
| [1] | "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. Olson M.V.Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
Cross-references
Sequence databases | |
|---|---|
| AE004091 Genomic DNA. Translation: AAG05635.1. | |
| PIR | C83365. S05057. |
| RefSeq | NP_250937.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1QS0 based on UniProtKB P09060. |
| SMR | Q9I1M2. Positions 2-408. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 877901. |
| GenomeReviews | Gene locus PA2247 in contig AE004091_GR. |
| KEGG | pae:PA2247. |
Organism-specific databases | |
| PseudoCAP | PA2247. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9I1M2. |
| OMA | MQSLGEE. |
Enzyme and pathway databases | |
| BioCyc | PAER208964:PA2247-MON. |
| BRENDA | 1.2.4.4. 354. |
Family and domain databases | |
| InterPro | IPR001017. DH_E1. [Graphical view] |
| Pfam | PF00676. E1_dh. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ODBA_PSEAE | ||||||||
| Accession | Primary (citable) accession number: Q9I1M2 | ||||||||
| 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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