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Q4MTG0

- ODPA_BACCE

UniProt

Q4MTG0 - ODPA_BACCE

Protein

Pyruvate dehydrogenase E1 component subunit alpha

Gene

pdhA

Organism
Bacillus cereus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 3 (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) By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Thiamine pyrophosphate.By similarity

    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
    2. response to stress Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis, Stress response

    Keywords - Ligandi

    Pyruvate, Thiamine pyrophosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha (EC:1.2.4.1)
    Gene namesi
    Name:pdhAImported
    ORF Names:BCE_G9241_3962
    OrganismiBacillus cereus
    Taxonomic identifieri1396 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 371370Pyruvate dehydrogenase E1 component subunit alphaPRO_0000271255Add
    BLAST

    Expressioni

    Inductioni

    By acid stress. Under acid-stress, this protein is expressed at a higher level in wild-type B.cereus than in the acid-sensitive mutant strain NB1.1 Publication

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain.Curated

    Structurei

    3D structure databases

    ProteinModelPortaliQ4MTG0.
    SMRiQ4MTG0. Positions 10-371.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    Q4MTG0-1 [UniParc]FASTAAdd to Basket

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    MGTKTKKTLF NVDEQMKAIA AQFETLQILN EKGEVVNEAA MPELSDDQLK    50
    ELMRRMVYTR VLDQRSISLN RQGRLGFYAP TAGQEASQLA SHFALEAEDF 100
    ILPGYRDVPQ LVWHGLPLYQ AFLFSRGHFM GNQMPENVNA LAPQIIIGAQ 150
    IIQTAGVALG MKLRGKKSVA ITYTGDGGAS QGDFYEGMNF AGAFKAPAIF 200
    VVQNNRYAIS TPVEKQSAAK TVAQKAVAAG IYGIQVDGMD PLAVYAATAF 250
    ARERAVNGEG PTLIETLTFR YGPHTMAGDD PTRYRTKDIE NEWEQKDPIV 300
    RFRAFLENKG LWSQEVEEKV IEEAKEDIKQ AIAKADQAPK QKVTDLMEIM 350
    YEKMPYNLAE QYEIYKEKES K 371
    Length:371
    Mass (Da):41,441
    Last modified:January 23, 2007 - v3
    Checksum:i884A8A94D6084451
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAEK01000007 Genomic DNA. Translation: EAL15457.1.

    Genome annotation databases

    EnsemblBacteriaiEAL15457; EAL15457; BCE_G9241_3962.
    PATRICi24955467. VBIBacCer116370_1693.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAEK01000007 Genomic DNA. Translation: EAL15457.1 .

    3D structure databases

    ProteinModelPortali Q4MTG0.
    SMRi Q4MTG0. Positions 10-371.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai EAL15457 ; EAL15457 ; BCE_G9241_3962 .
    PATRICi 24955467. VBIBacCer116370_1693.

    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: G9241Imported.
    2. "Acid stress in the food pathogen Bacillus cereus."
      Browne N., Dowds B.C.A.
      J. Appl. Microbiol. 92:404-414(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21, INDUCTION.
      Strain: NCIMB 11796 / DSM 6261 Publication.

    Entry informationi

    Entry nameiODPA_BACCE
    AccessioniPrimary (citable) accession number: Q4MTG0
    Secondary accession number(s): P83068, P83070
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 38 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    External Data

    Dasty 3