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P26268

- ODPT_ASCSU

UniProt

P26268 - ODPT_ASCSU

Protein

Pyruvate dehydrogenase E1 component subunit alpha type II, mitochondrial

Gene
N/A
Organism
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei‹1 – 17›17MitochondrionAdd
    BLAST
    Chaini18 – 391374Pyruvate dehydrogenase E1 component subunit alpha type II, mitochondrialPRO_0000020438Add
    BLAST

    Amino acid modifications

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

    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.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP26268.
    SMRiP26268. Positions 22-369.
    ModBaseiSearch...
    MobiDBiSearch...

    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

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    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

    Experimental Info

    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: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)