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P26267 (ODPA_ASCSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrial

Short name=PDHA1
Short name=PDHE1-A
EC=1.2.4.1
OrganismAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier6253 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Catalytic activity

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

Cofactor

Thiamine pyrophosphate.

Enzyme regulation

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

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) By similarity.

Subcellular location

Mitochondrion matrix.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion
Chain26 – 396371Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrial
PRO_0000020437

Amino acid modifications

Modified residue2891Phosphoserine Ref.2
Modified residue2961Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
P26267 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 60A810BB5B48B836

FASTA39643,771
        10         20         30         40         50         60 
MIFVFANIFK VPTVSPSVMA ISVRLASTEA TFQTKPFKLH KLDSGPDINV HVTKEDAVHY 

        70         80         90        100        110        120 
YTQMLTIRRM ESAAGNLYKE KKVRGFCHLY SGQEACAVGT KAAMDAGDAA VTAYRCHGWT 

       130        140        150        160        170        180 
YLSGSSVAKV LCELTGRITG NVYGKGGSMH MYGENFYGGN GIVGAQQPLG TGIAFAMKYR 

       190        200        210        220        230        240 
KEKNVCITMF GDGATNQGQL FESMNMAKLW DLPVLYVCEN NGYGMGTAAA RSSASTDYYT 

       250        260        270        280        290        300 
RGDYVPGIWV DGMDVLAVRQ AVRWAKEWCN AGKGPLMIEM ATYRYSGHSM SDPGTSYRTR 

       310        320        330        340        350        360 
EEVQEVRKTR DPITGFKDKI VTAGLVTEDE IKEIDKQVRK EIDAAVKQAH TDKESPVELM 

       370        380        390 
LTDIYYNTPA QYVRCTTDEV LQKYLTSEEA VKALAK 

« Hide

References

[1]"Characterization of cDNA clones for the alpha subunit of pyruvate dehydrogenase from Ascaris suum."
Johnson K.R., Komuniecki R., Sun Y., Wheelock M.J.
Mol. Biochem. Parasitol. 51:37-48(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Phosphorylation and inactivation of the pyruvate dehydrogenase from the anaerobic parasitic nematode, Ascaris suum. Stoichiometry and amino acid sequence around the phosphorylation sites."
Thissen J., Komuniecki R.
J. Biol. Chem. 263:19092-19097(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 285-298, PHOSPHORYLATION AT SER-289 AND SER-296.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M76555 mRNA. Translation: AAA29376.1.
PIRA31963.
A45608.

3D structure databases

ProteinModelPortalP26267.
SMRP26267. Positions 27-374.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-18299.

Family and domain databases

Gene3D3.40.50.970. 1 hit.
InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPA_ASCSU
AccessionPrimary (citable) accession number: P26267
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 9, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)