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Protein

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Gene

PDHA1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.By similarity

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Enzyme regulationi

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processCarbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle
LigandPyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

ReactomeiR-BTA-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-BTA-389661. Glyoxylate metabolism and glycine degradation.
R-BTA-5362517. Signaling by Retinoic Acid.
R-BTA-70268. Pyruvate metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC:1.2.4.1)
Alternative name(s):
PDHE1-A type I
Gene namesi
Name:PDHA1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome X

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 29MitochondrionBy similarityAdd BLAST29
ChainiPRO_000032931230 – 390Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrialAdd BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei63N6-acetyllysine; alternateBy similarity1
Modified residuei63N6-succinyllysine; alternateBy similarity1
Modified residuei231PhosphothreonineBy similarity1
Modified residuei232Phosphoserine; by PDK1By similarity1
Modified residuei244N6-acetyllysine; alternateBy similarity1
Modified residuei244N6-succinyllysine; alternateBy similarity1
Modified residuei267N6-acetyllysineBy similarity1
Modified residuei277N6-succinyllysineBy similarity1
Modified residuei293Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity1
Modified residuei295PhosphoserineBy similarity1
Modified residuei300Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity1
Modified residuei301PhosphotyrosineBy similarity1
Modified residuei313N6-acetyllysine; alternateBy similarity1
Modified residuei313N6-succinyllysine; alternateBy similarity1
Modified residuei321N6-acetyllysineBy similarity1
Modified residuei336N6-acetyllysineBy similarity1
Modified residuei385N6-succinyllysineBy similarity1

Post-translational modificationi

Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-293 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation (By similarity).By similarity
Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiA7MB35.
PeptideAtlasiA7MB35.
PRIDEiA7MB35.

Expressioni

Gene expression databases

BgeeiENSBTAG00000019852.

Interactioni

Subunit structurei

Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000052439.

Structurei

3D structure databases

ProteinModelPortaliA7MB35.
SMRiA7MB35.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0225. Eukaryota.
COG1071. LUCA.
GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281336.
HOVERGENiHBG001863.
InParanoidiA7MB35.
KOiK00161.
OMAiRRFEDKC.
OrthoDBiEOG091G0966.
TreeFamiTF300742.

Family and domain databases

InterProiView protein in InterPro
IPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
PfamiView protein in Pfam
PF00676. E1_dh. 1 hit.
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A7MB35-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKMLAAVSR VLSGVAQKPA SRVLVASRHF ANDATFEIKK CDLHRLEEGP
60 70 80 90 100
PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC
110 120 130 140 150
CVGLEAGINP TDHLITAYRA HGFTFTRGLS VREILAELTG RRGGCAKGKG
160 170 180 190 200
GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAN
210 220 230 240 250
QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP
260 270 280 290 300
GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS
310 320 330 340 350
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA
360 370 380 390
QFATADPEPP LEELGYHIYC NDPPFEVRGA NQWIKFKSIS
Length:390
Mass (Da):43,388
Last modified:October 2, 2007 - v1
Checksum:i1297C2B1960BBEDF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC151313 mRNA. Translation: AAI51314.1.
RefSeqiNP_001094516.1. NM_001101046.2.
UniGeneiBt.19415.

Genome annotation databases

EnsembliENSBTAT00000057115; ENSBTAP00000052439; ENSBTAG00000019852.
GeneIDi407109.
KEGGibta:407109.

Similar proteinsi

Entry informationi

Entry nameiODPA_BOVIN
AccessioniPrimary (citable) accession number: A7MB35
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: October 2, 2007
Last modified: August 30, 2017
This is version 74 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome