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P26268 (ODPT_ASCSU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 71. 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 II, mitochondrial

Short name=PDHA2
Short name=PDHE1-A
EC=1.2.4.1
OrganismAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier6253 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

Protein attributes

Sequence length391 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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 PDHA2; it is reactivated by dephosphorylation.

Subunit structure

Heterotetramer of two PDHA2 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – 17›17Mitochondrion
Chain18 – 391374Pyruvate dehydrogenase E1 component subunit alpha type II, mitochondrial
PRO_0000020438

Amino acid modifications

Modified residue2841Phosphoserine Probable
Modified residue2911Phosphoserine Probable

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P26268 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: BA66E56C300FB8E7

FASTA39143,207
        10         20         30         40         50         60 
SNIFKGPTVG SSVVAMSARL ASTEATFQAK PFKLHKLDSG PDVNMHVTKE DALRYYTQMQ 

        70         80         90        100        110        120 
TIRRMETAAG NLYKEKKVRG FCHLYSGQEA CAVGMKAAME PGDAAITAYR CHGWTYLSGS 

       130        140        150        160        170        180 
PVAKVLCELT GRITGNVYGK GGSMHMYGEN FYGGNGIVGA QQPLGTGIAF AMKYKKQKNV 

       190        200        210        220        230        240 
CITLFGDGAT NQGQLYESMN MAKLWELPVL YVCENNGYGM GTSAARSSAS TDYYTRGDYV 

       250        260        270        280        290        300 
PGFWVDGMDV LAVRQAIRWG KEWCNAGKGP LMIEMATYRY GGHSMSDPGT SYRTREEIQE 

       310        320        330        340        350        360 
VRKTRDPITG FKDKIVTAGL VTEDELKEVD KEIRKEVDAA VKQAHTDKEA PVEMLLTDIY 

       370        380        390 
YNTPAQYVRC TTEDVLQQYV TSEEAFKALS K 

« 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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M76554 mRNA. Translation: AAA29377.1.

3D structure databases

ProteinModelPortalP26268.
SMRP26268. Positions 22-369.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP26268.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 nameODPT_ASCSU
AccessionPrimary (citable) accession number: P26268
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 11, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)