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Reviewed, UniProtKB/Swiss-Prot Q5R490 (ODPA_PONAB)

Last modified October 13, 2009. Version 35. 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
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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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_0000020444

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
Q5R490-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 4C0A5ADD25CB2D49

FASTA39043,224
        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 QGQIFGAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 

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

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

       370        380        390 
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

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Cross-references

Sequence databases

CR861366 mRNA. Translation: CAH93426.1.
RefSeqNP_001127663.1.
UniGenePab.18473

3D structure databases

SMRQ5R490. Positions 29-390.
ModBaseSearch...

Genome annotation databases

GeneID100174745.

Organism-specific databases

CTD100174745.

Phylogenomic databases

HOVERGENQ5R490.

Enzyme and pathway databases

BRENDA1.2.4.1. 269192.

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_PONAB
AccessionPrimary (citable) accession number: Q5R490
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: December 21, 2004
Last modified: October 13, 2009
This is version 35 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