SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P26268

- ODPT_ASCSU

UniProt

P26268 - ODPT_ASCSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Pyruvate dehydrogenase E1 component subunit alpha type II, mitochondrial
Gene
N/A
Organism
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Thiamine pyrophosphate.

Enzyme regulationi

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA2; it is reactivated by dephosphorylation.

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

GO - Biological processi

  1. glucose metabolic process Source: UniProtKB-KW
  2. glycolytic process Source: InterPro
  3. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha type II, mitochondrial (EC:1.2.4.1)
Short name:
PDHA2
Short name:
PDHE1-A
OrganismiAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifieri6253 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei‹1 – 17›17Mitochondrion
Add
BLAST
Chaini18 – 391374Pyruvate dehydrogenase E1 component subunit alpha type II, mitochondrial
PRO_0000020438Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei284 – 2841Phosphoserine Inferred
Modified residuei291 – 2911Phosphoserine Inferred

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP26268.

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliP26268.
SMRiP26268. Positions 22-369.

Family & Domainsi

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26268-1 [UniParc]FASTAAdd to Basket

« Hide

SNIFKGPTVG SSVVAMSARL ASTEATFQAK PFKLHKLDSG PDVNMHVTKE    50
DALRYYTQMQ TIRRMETAAG NLYKEKKVRG FCHLYSGQEA CAVGMKAAME 100
PGDAAITAYR CHGWTYLSGS PVAKVLCELT GRITGNVYGK GGSMHMYGEN 150
FYGGNGIVGA QQPLGTGIAF AMKYKKQKNV CITLFGDGAT NQGQLYESMN 200
MAKLWELPVL YVCENNGYGM GTSAARSSAS TDYYTRGDYV PGFWVDGMDV 250
LAVRQAIRWG KEWCNAGKGP LMIEMATYRY GGHSMSDPGT SYRTREEIQE 300
VRKTRDPITG FKDKIVTAGL VTEDELKEVD KEIRKEVDAA VKQAHTDKEA 350
PVEMLLTDIY YNTPAQYVRC TTEDVLQQYV TSEEAFKALS K 391
Length:391
Mass (Da):43,207
Last modified:May 1, 1992 - v1
Checksum:iBA66E56C300FB8E7
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M76554 mRNA. Translation: AAA29377.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M76554 mRNA. Translation: AAA29377.1 .

3D structure databases

ProteinModelPortali P26268.
SMRi P26268. Positions 22-369.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P26268.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.970. 1 hit.
InterProi IPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view ]
Pfami PF00676. E1_dh. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
TIGRFAMsi TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiODPT_ASCSU
AccessioniPrimary (citable) accession number: P26268
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)

Similar proteinsi