Q658P7 · Q658P7_HUMAN
- Protein2-oxoisovalerate dehydrogenase subunit alpha
- GeneDKFZp313C0640
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids403 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
Function
function
Together with BCKDHB forms the heterotetrameric E1 subunit of the mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD) complex. The BCKD complex catalyzes the multi-step oxidative decarboxylation of alpha-ketoacids derived from the branched-chain amino-acids valine, leucine and isoleucine producing CO2 and acyl-CoA which is subsequently utilized to produce energy. The E1 subunit catalyzes the first step with the decarboxylation of the alpha-ketoacid forming an enzyme-product intermediate. A reductive acylation mediated by the lipoylamide cofactor of E2 extracts the acyl group from the E1 active site for the next step of the reaction.
Catalytic activity
- 3-methyl-2-oxobutanoate + H+ + N6-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 + N6-[(R)-S8-2-methylpropanoyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]This reaction proceeds in the forward direction.
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity | |
Biological Process | branched-chain amino acid catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2-oxoisovalerate dehydrogenase subunit alpha
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ658P7
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Proteomic databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 33-52 | Disordered | ||||
Sequence: LARSHPPRQQQQFSSLDDKP | ||||||
Compositional bias | 37-51 | Polar residues | ||||
Sequence: HPPRQQQQFSSLDDK | ||||||
Domain | 106-319 | Dehydrogenase E1 component | ||||
Sequence: YKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATGGPKARASV |
Sequence similarities
Belongs to the BCKDHA family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length403
- Mass (Da)44,353
- Last updated2004-10-25 v1
- ChecksumA8CEB2C9C6741D2E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 37-51 | Polar residues | ||||
Sequence: HPPRQQQQFSSLDDK |