Search Results

Overview

Uniprot IDP08559
Protein NamePyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
Gene NamePDHA1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
244 AASTDYYKRGDFIPG
277 AAYCRSGKGPILMEL
313 EIQEVRSKSDPIMLL
321 SDPIMLLKDRMVNSN
336 LASVEELKEIDVEVR
344 EIDVEVRKEIEDAAQ
63 LTREDGLKYYRMMQT
83 LKADQLYKQKIIRGF

Function

Together with PDHB 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 (PubMed:19081061, PubMed:7782287). 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:17474719, PubMed:19081061, PubMed:7782287)

Protein Sequence

10 MRKMLAAVSR 20 VLSGASQKPA 30 SRVLVASRNF 40 ANDATFEIKK 50 CDLHRLEEGP 60 PVTTVLTRED 70 GLKYYRMMQT 80 VRRMELKADQ 90 LYKQKIIRGF 100 CHLCDGQEAC 110 CVGLEAGINP 120 TDHLITAYRA 130 HGFTFTRGLS 140 VREILAELTG 150 RKGGCAKGKG 160 GSMHMYAKNF 170 YGGNGIVGAQ 180 VPLGAGIALA 190 CKYNGKDEVC 200 LTLYGDGAAN 210 QGQIFEAYNM 220 AALWKLPCIF 230 ICENNRYGMG 240 TSVERAAAST 250 DYYKRGDFIP 260 GLRVDGMDIL 270 CVREATRFAA 280 AYCRSGKGPI 290 LMELQTYRYH 300 GHSMSDPGVS 310 YRTREEIQEV 320 RSKSDPIMLL 330 KDRMVNSNLA 340 SVEELKEIDV 350 EVRKEIEDAA 360 QFATADPEPP 370 LEELGYHIYS 380 SDPPFEVRGA 390 NQWIKFKSVS

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] 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.

[2] 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.

[3] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.