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P21873

- ODPA_GEOSE

UniProt

P21873 - ODPA_GEOSE

Protein

Pyruvate dehydrogenase E1 component subunit alpha

Gene

pdhA

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

    Catalytic activityi

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

    Cofactori

    Thiamine pyrophosphate.

    GO - Molecular functioni

    1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC
    2. thiamine pyrophosphate binding Source: InterPro

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Pyruvate, Thiamine pyrophosphate

    Enzyme and pathway databases

    SABIO-RKP21873.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha (EC:1.2.4.1)
    Gene namesi
    Name:pdhA
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 369368Pyruvate dehydrogenase E1 component subunit alphaPRO_0000162198Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain.

    Protein-protein interaction databases

    DIPiDIP-29596N.
    IntActiP21873. 1 interaction.

    Structurei

    Secondary structure

    1
    369
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 1910
    Helixi36 – 383
    Helixi44 – 6926
    Helixi83 – 919
    Beta strandi98 – 1003
    Beta strandi102 – 1043
    Helixi106 – 1116
    Helixi116 – 1249
    Helixi127 – 1304
    Helixi147 – 16115
    Beta strandi168 – 1736
    Helixi175 – 1784
    Helixi180 – 19112
    Beta strandi196 – 2027
    Beta strandi204 – 2063
    Helixi211 – 2133
    Helixi221 – 2266
    Beta strandi231 – 2355
    Helixi239 – 25416
    Beta strandi260 – 2656
    Beta strandi274 – 2774
    Helixi278 – 2803
    Helixi285 – 2928
    Helixi296 – 30611
    Helixi312 – 33423
    Helixi341 – 3466
    Helixi354 – 36613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W85X-ray2.00A/C/E/G2-369[»]
    1W88X-ray2.30A/C/E/G2-369[»]
    3DUFX-ray2.50A/C/E/G1-369[»]
    3DV0X-ray2.50A/C/E/G1-369[»]
    3DVAX-ray2.35A/C/E/G1-369[»]
    ProteinModelPortaliP21873.
    SMRiP21873. Positions 5-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21873.

    Family & Domainsi

    Family and domain databases

    Gene3Di3.40.50.970. 1 hit.
    InterProiIPR001017. DH_E1.
    IPR017596. PdhA/BkdA.
    IPR029061. THDP-binding.
    [Graphical view]
    PfamiPF00676. E1_dh. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 1 hit.
    TIGRFAMsiTIGR03181. PDH_E1_alph_x. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P21873-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGVKTFQFPF AEQLEKVAEQ FPTFQILNEE GEVVNEEAMP ELSDEQLKEL    50
    MRRMVYTRIL DQRSISLNRQ GRLGFYAPTA GQEASQIASH FALEKEDFIL 100
    PGYRDVPQII WHGLPLYQAF LFSRGHFHGN QIPEGVNVLP PQIIIGAQYI 150
    QAAGVALGLK MRGKKAVAIT YTGDGGTSQG DFYEGINFAG AFKAPAIFVV 200
    QNNRFAISTP VEKQTVAKTL AQKAVAAGIP GIQVDGMDPL AVYAAVKAAR 250
    ERAINGEGPT LIETLCFRYG PHTMSGDDPT RYRSKELENE WAKKDPLVRF 300
    RKFLEAKGLW SEEEENNVIE QAKEEIKEAI KKADETPKQK VTDLISIMFE 350
    ELPFNLKEQY EIYKEKESK 369
    Length:369
    Mass (Da):41,469
    Last modified:January 23, 2007 - v2
    Checksum:iDBF43982C0E1926D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53560 Genomic DNA. Translation: CAA37628.1.
    PIRiS10798. DEBSPF.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53560 Genomic DNA. Translation: CAA37628.1 .
    PIRi S10798. DEBSPF.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W85 X-ray 2.00 A/C/E/G 2-369 [» ]
    1W88 X-ray 2.30 A/C/E/G 2-369 [» ]
    3DUF X-ray 2.50 A/C/E/G 1-369 [» ]
    3DV0 X-ray 2.50 A/C/E/G 1-369 [» ]
    3DVA X-ray 2.35 A/C/E/G 1-369 [» ]
    ProteinModelPortali P21873.
    SMRi P21873. Positions 5-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29596N.
    IntActi P21873. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P21873.

    Miscellaneous databases

    EvolutionaryTracei P21873.

    Family and domain databases

    Gene3Di 3.40.50.970. 1 hit.
    InterProi IPR001017. DH_E1.
    IPR017596. PdhA/BkdA.
    IPR029061. THDP-binding.
    [Graphical view ]
    Pfami PF00676. E1_dh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 1 hit.
    TIGRFAMsi TIGR03181. PDH_E1_alph_x. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of the genes encoding the alpha and beta subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
      Hawkins C.F., Borges A., Perham R.N.
      Eur. J. Biochem. 191:337-346(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-35; 54-111 AND 269-331.
      Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.

    Entry informationi

    Entry nameiODPA_GEOSE
    AccessioniPrimary (citable) accession number: P21873
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3