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P26267

- ODPA_ASCSU

UniProt

P26267 - ODPA_ASCSU

Protein

Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrial

Gene
N/A
Organism
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (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 PDHA1; 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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18299.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrial (EC:1.2.4.1)
    Short name:
    PDHA1
    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 peptidei1 – 2525MitochondrionAdd
    BLAST
    Chaini26 – 396371Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrialPRO_0000020437Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei289 – 2891Phosphoserine1 Publication
    Modified residuei296 – 2961Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    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.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP26267.
    SMRiP26267. Positions 27-374.
    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: Complete.

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

    P26267-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIFVFANIFK VPTVSPSVMA ISVRLASTEA TFQTKPFKLH KLDSGPDINV    50
    HVTKEDAVHY YTQMLTIRRM ESAAGNLYKE KKVRGFCHLY SGQEACAVGT 100
    KAAMDAGDAA VTAYRCHGWT YLSGSSVAKV LCELTGRITG NVYGKGGSMH 150
    MYGENFYGGN GIVGAQQPLG TGIAFAMKYR KEKNVCITMF GDGATNQGQL 200
    FESMNMAKLW DLPVLYVCEN NGYGMGTAAA RSSASTDYYT RGDYVPGIWV 250
    DGMDVLAVRQ AVRWAKEWCN AGKGPLMIEM ATYRYSGHSM SDPGTSYRTR 300
    EEVQEVRKTR DPITGFKDKI VTAGLVTEDE IKEIDKQVRK EIDAAVKQAH 350
    TDKESPVELM LTDIYYNTPA QYVRCTTDEV LQKYLTSEEA VKALAK 396
    Length:396
    Mass (Da):43,771
    Last modified:May 1, 1992 - v1
    Checksum:i60A810BB5B48B836
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76555 mRNA. Translation: AAA29376.1.
    PIRiA31963.
    A45608.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76555 mRNA. Translation: AAA29376.1 .
    PIRi A31963.
    A45608.

    3D structure databases

    ProteinModelPortali P26267.
    SMRi P26267. Positions 27-374.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-18299.

    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].
    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.

    Entry informationi

    Entry nameiODPA_ASCSU
    AccessioniPrimary (citable) accession number: P26267
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    External Data

    Dasty 3