Overview
| Uniprot ID | P11177 |
|---|
| Protein Name | Pyruvate dehydrogenase E1 component subunit beta, mitochondrial |
|---|
| Gene Name | PDHB |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 227 |
DFLIPIGKAKIERQG |
| 258 |
EAAAVLSKEGVECEV |
| 354 |
KDIIFAIKKTLNI** |
Function
Together with PDHA1 forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex (PubMed:17474719, PubMed:19081061). The PDH complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (Probable). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) (Probable). The E1 subunit catalyzes both the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvate and the reductive acetylation of a lipoyl group covalently linked to the lipoyl-bearing domains of E2 (PubMed:19081061)
Protein Sequence
10
MAAVSGLVRR
20
PLREVSGLLK
30
RRFHWTAPAA
40
LQVTVRDAIN
50
QGMDEELERD
60
EKVFLLGEEV
70
AQYDGAYKVS
80
RGLWKKYGDK
90
RIIDTPISEM
100
GFAGIAVGAA
110
MAGLRPICEF
120
MTFNFSMQAI
130
DQVINSAAKT
140
YYMSGGLQPV
150
PIVFRGPNGA
160
SAGVAAQHSQ
170
CFAAWYGHCP
180
GLKVVSPWNS
190
EDAKGLIKSA
200
IRDNNPVVVL
210
ENELMYGVPF
220
EFPPEAQSKD
230
FLIPIGKAKI
240
ERQGTHITVV
250
SHSRPVGHCL
260
EAAAVLSKEG
270
VECEVINMRT
280
IRPMDMETIE
290
ASVMKTNHLV
300
TVEGGWPQFG
310
VGAEICARIM
320
EGPAFNFLDA
330
PAVRVTGADV
340
PMPYAKILED
350
NSIPQVKDII
FAIKKTLNI
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005759 |
mitochondrial matrix |
| Cellular Component |
GO:0005739 |
mitochondrion |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0045254 |
pyruvate dehydrogenase complex |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Molecular Function |
GO:0004739 |
pyruvate dehydrogenase (acetyl-transferring) activity |
| Biological Process |
GO:0006006 |
glucose metabolic process |
| Biological Process |
GO:0006086 |
pyruvate decarboxylation to acetyl-CoA |
| Biological Process |
GO:0006099 |
tricarboxylic acid cycle |
Reference
[1] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.