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P52900

- ODPA_SMIMA

UniProt

P52900 - ODPA_SMIMA

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Protein

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

Gene
PDHA
Organism
Sminthopsis macroura (Stripe-faced dunnart)
Status
Reviewed - Annotation score: 3 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

Thiamine pyrophosphate By similarity.

Enzyme regulationi

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

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC
  2. pyruvate dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
  2. glucose metabolic process Source: UniProtKB-KW
  3. glycolytic process Source: InterPro
  4. tricarboxylic acid cycle Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial (EC:1.2.4.1)
Short name:
PDHE1-A
Gene namesi
Name:PDHA
OrganismiSminthopsis macroura (Stripe-faced dunnart)
Taxonomic identifieri9302 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMetatheriaDasyuromorphiaDasyuridaeSminthopsis

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. pyruvate dehydrogenase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei‹1 – 2›2Mitochondrion By similarity
Chaini3 – 363361Pyruvate dehydrogenase E1 component subunit alpha, mitochondrialPRO_0000020446Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6-acetyllysine; alternate By similarity
Modified residuei36 – 361N6-succinyllysine; alternate By similarity
Modified residuei205 – 2051Phosphoserine; by PDK1 By similarity
Modified residuei217 – 2171N6-acetyllysine; alternate By similarity
Modified residuei217 – 2171N6-succinyllysine; alternate By similarity
Modified residuei240 – 2401N6-acetyllysine By similarity
Modified residuei250 – 2501N6-succinyllysine By similarity
Modified residuei266 – 2661Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity
Modified residuei268 – 2681Phosphoserine By similarity
Modified residuei273 – 2731Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity
Modified residuei274 – 2741Phosphotyrosine By similarity
Modified residuei286 – 2861N6-acetyllysine; alternate By similarity
Modified residuei286 – 2861N6-succinyllysine; alternate By similarity
Modified residuei294 – 2941N6-acetyllysine By similarity
Modified residuei309 – 3091N6-acetyllysine By similarity
Modified residuei358 – 3581N6-succinyllysine By similarity

Post-translational modificationi

Phosphorylation at Ser-205, Ser-266 and Ser-273 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-266 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-205, Ser-266 and Ser-273, is required for reactivation By similarity.
Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP52900.

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.

Structurei

3D structure databases

ProteinModelPortaliP52900.
SMRiP52900. Positions 2-363.

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG001863.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

Sequencei

Sequence statusi: Fragment.

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

P52900-1 [UniParc]FASTAAdd to Basket

« Hide

RNFANDATFD IKKCDVHRLE EGPPTTAVLT REEGLKYYKI MQTVRRMELK    50
ADQLYKQKII RGFCHLYDGQ EACCMGLEAG INPTDHVITA YRAHGFTYTR 100
GLPVREILAE LTGRRGGCAK GKGGSMHMYA KNFYGGNGIV GAQVPLGVGI 150
ALACKYNEKD EICLTLYGDG AANQGQIFEA YNMAALWKLP CIFICENNRY 200
GMGTSVERAA ASTDYYKRGD FIPGIMVDGM DVLCVREATK FAAAYCRSGK 250
GPMLMELQTY RYHGHSMSDP GVSYRTREEI QEVRSKSDPI MLLKDRMVNN 300
NLASIEELKE IDVEVRKEIE DAAQFATADP EPPLEELGYH IYSRDPPFEV 350
RGANQWIKYK SVS 363
Length:363
Mass (Da):40,735
Last modified:October 1, 1996 - v1
Checksum:i4884E0A17D7A15A8
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L20774 mRNA. Translation: AAA31589.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L20774 mRNA. Translation: AAA31589.1 .

3D structure databases

ProteinModelPortali P52900.
SMRi P52900. Positions 2-363.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P52900.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG001863.

Family and domain databases

Gene3Di 3.40.50.970. 1 hit.
InterProi IPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view ]
Pfami PF00676. E1_dh. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
TIGRFAMsi TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "A eutherian X-linked gene, PDHA1, is autosomal in marsupials: a model for the evolution of a second, testis-specific variant in eutherian mammals."
    Fitzgerald J., Wilcox S.A., Graves J.A., Dahl H.-H.M.
    Genomics 18:636-642(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiODPA_SMIMA
AccessioniPrimary (citable) accession number: P52900
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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