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Reviewed, UniProtKB/Swiss-Prot A7MB35 (ODPA_BOVIN)

Last modified November 3, 2009. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

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Names and origin

Protein namesRecommended 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Catalytic activity

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

Cofactor

Thiamine pyrophosphate By similarity.

Enzyme regulation

E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit By similarity.

Subunit structure

Tetramer of 2 alpha and 2 beta subunits By similarity.

Subcellular location

Mitochondrion matrix By similarity.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion By similarity
Chain30 – 390361Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
PRO_0000329312

Amino acid modifications

Modified residue771N6-acetyllysine By similarity
Modified residue831N6-acetyllysine By similarity
Modified residue2321Phosphoserine By similarity
Modified residue2891Phosphotyrosine By similarity
Modified residue2931Phosphoserine By similarity
Modified residue2951Phosphoserine By similarity
Modified residue3001Phosphoserine By similarity
Modified residue3011Phosphotyrosine By similarity
Modified residue3211N6-acetyllysine By similarity
Modified residue3361N6-acetyllysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
A7MB35-1 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 1297C2B1960BBEDF

FASTA39043,388
        10         20         30         40         50         60 
MRKMLAAVSR VLSGVAQKPA SRVLVASRHF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 

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

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

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

       250        260        270        280        290        300 
DYYKRGDFIP GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 

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

       370        380        390 
LEELGYHIYC NDPPFEVRGA NQWIKFKSIS

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References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Hypothalamus.

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Cross-references

Sequence databases

BC151313 mRNA. Translation: AAI51314.1.
IPIIPI00694488.
RefSeqNP_001094516.1.
UniGeneBt.19415

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7MB35.

Genome annotation databases

EnsemblENSBTAT00000057115; ENSBTAP00000052439; ENSBTAG00000019852; Bos taurus. [Genome view]
GeneID407109.
KEGGbta:407109.

Organism-specific databases

CTD407109.

Phylogenomic databases

OMAYAMGTST.

Enzyme and pathway databases

BRENDA1.2.4.1. 251.

Family and domain databases

InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameODPA_BOVIN
AccessionPrimary (citable) accession number: A7MB35
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: October 2, 2007
Last modified: November 3, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information