Overview
| Uniprot ID | P21953 |
|---|
| Protein Name | 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial |
|---|
| Gene Name | BCKDHB |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 294 |
VASMAKEKLGVSCEV |
Function
Together with BCKDHA 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
Protein Sequence
10
MAVVAAAAGW
20
LLRLRAAGAE
30
GHWRRLPGAG
40
LARGFLHPAA
50
TVEDAAQRRQ
60
VAHFTFQPDP
70
EPREYGQTQK
80
MNLFQSVTSA
90
LDNSLAKDPT
100
AVIFGEDVAF
110
GGVFRCTVGL
120
RDKYGKDRVF
130
NTPLCEQGIV
140
GFGIGIAVTG
150
ATAIAEIQFA
160
DYIFPAFDQI
170
VNEAAKYRYR
180
SGDLFNCGSL
190
TIRSPWGCVG
200
HGALYHSQSP
210
EAFFAHCPGI
220
KVVIPRSPFQ
230
AKGLLLSCIE
240
DKNPCIFFEP
250
KILYRAAAEE
260
VPIEPYNIPL
270
SQAEVIQEGS
280
DVTLVAWGTQ
290
VHVIREVASM
300
AKEKLGVSCE
310
VIDLRTIIPW
320
DVDTICKSVI
330
KTGRLLISHE
340
APLTGGFASE
350
ISSTVQEECF
360
LNLEAPISRV
370
CGYDTPFPHI
380
FEPFYIPDKW
390
KCYDALRKMI
NY
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0160157 |
branched-chain alpha-ketoacid dehydrogenase complex |
| Cellular Component |
GO:0005759 |
mitochondrial matrix |
| Cellular Component |
GO:0005739 |
mitochondrion |
| Molecular Function |
GO:0003863 |
branched-chain 2-oxo acid dehydrogenase activity |
| Biological Process |
GO:0120552 |
branched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA |
| Biological Process |
GO:0009083 |
branched-chain amino acid catabolic process |
| Biological Process |
GO:0007584 |
response to nutrient |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.