Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial precursor

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A5A6L0 (ODPA_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 45. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
EC=1.2.4.1

Alternative name(s):
PDHE1-A type I

Gene names

Name:

PDHA1

Organism

Pan troglodytes (Chimpanzee) [Reference proteome]

Taxonomic identifier

9598 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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 activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO₂.
Cofactor	Thiamine pyrophosphate By similarity.
Enzyme regulation	Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation By similarity.
Subunit structure	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.
Subcellular location	Mitochondrion matrix By similarity.
Post-translational modification	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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from sequence or structural similarity. Source: UniProtKB glycolysis Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell pyruvate dehydrogenase complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC pyruvate dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 29

Mitochondrion By similarity

Chain

30 – 390

361

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

PRO_0000297491

Amino acid modifications

Modified residue

232

Phosphoserine; by PDK1 By similarity

Modified residue

289

Phosphotyrosine By similarity

Modified residue

293

Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity

Modified residue

295

Phosphoserine By similarity

Modified residue

300

Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity

Modified residue

301

Phosphotyrosine By similarity

Modified residue

321

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A5A6L0 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 4F95746CBB792E78
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FASTA

390

43,238

        10         20         30         40         50         60 
MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 

        70         80         90        100        110        120 
GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 

       130        140        150        160        170        180 
HGFTFTRGLS VREILAELTG RKGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 

       190        200        210        220        230        240 
CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 

       250        260        270        280        290        300 
DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSGPGVS 

       310        320        330        340        350        360 
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP 

       370        380        390 
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS

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References

[1]

"Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome."
Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M.
Gene 399:1-10(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB222138 mRNA. Translation: BAF62383.1.
RefSeq	NP_001104283.1. NM_001110813.1.
UniGene	Ptr.3278.
3D structure databases
ProteinModelPortal	A5A6L0.
SMR	A5A6L0. Positions 29-390.
ModBase	Search...
Proteomic databases
PRIDE	A5A6L0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	465525.
KEGG	ptr:465525.
Organism-specific databases
CTD	5160.
Phylogenomic databases
eggNOG	COG1071.
HOGENOM	HOG000281336.
HOVERGEN	HBG001863.
InParanoid	A5A6L0.
KO	K00161.
OrthoDB	EOG4W0XD6.
Family and domain databases
InterPro	IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNet	Search...
Other
NextBio	20843882.

Entry information

Entry name

ODPA_PANTR

Accession

Primary (citable) accession number: A5A6L0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	June 12, 2007
Last modified:	April 3, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information