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P52904

- ODPB_PEA

UniProt

P52904 - ODPB_PEA

Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821Thiamine pyrophosphateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: InterPro
    2. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Pyruvate, Thiamine pyrophosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (EC:1.2.4.1)
    Short name:
    PDHE1-B
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    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 – 1919MitochondrionBy similarityAdd
    BLAST
    Chaini20 – 359340Pyruvate dehydrogenase E1 component subunit beta, mitochondrialPRO_0000020463Add
    BLAST

    Proteomic databases

    PRIDEiP52904.
    ProMEXiP52904.

    Interactioni

    Subunit structurei

    Tetramer of 2 alpha and 2 beta subunits.By similarity

    Protein-protein interaction databases

    IntActiP52904. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP52904.
    SMRiP52904. Positions 25-347.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di3.40.50.920. 1 hit.
    3.40.50.970. 1 hit.
    InterProiIPR027110. PDHB.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005475. Transketolase-like_Pyr-bd.
    IPR005476. Transketolase_C.
    [Graphical view]
    PANTHERiPTHR11624:SF56. PTHR11624:SF56. 1 hit.
    PfamiPF02779. Transket_pyr. 1 hit.
    PF02780. Transketolase_C. 1 hit.
    [Graphical view]
    SMARTiSM00861. Transket_pyr. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 1 hit.
    SSF52922. SSF52922. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P52904-1 [UniParc]FASTAAdd to Basket

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    MLGVIRNKTI RPSFSAFRFF SSAKQMTVRD ALNSALDVEM SADSKVFLMG    50
    EEVGEYQGAY KVTKGLLEKY GPERVLDTPI TEAGFTGIGV GAAYYGLKPV 100
    VEFMTFNFSM QAIDHIINSA AKSNYMSAGQ ISVPIVFRGL NGDAAGVGAQ 150
    HSHCYASWYG SCPGLKVLVP HSAEDARGLL KAAIRDPDPV VFLENELLYG 200
    ESFPVSAEVL DSSFWLPIGK AKIEREGKDV TITAFSKMVG FALKAAEILE 250
    KEGISAEVIN LRSIRPLDRP TINASVRKTN RLVTVEEGFP QHGVGAEICT 300
    SVIEESFGYL DATVERIGGA DVPMPYAGNL ERLVVPHVED IVRAAKRACH 350
    RSVPLAAAA 359
    Length:359
    Mass (Da):38,793
    Last modified:October 1, 1996 - v1
    Checksum:i5AFE49F165C13C83
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U56697 mRNA. Translation: AAB01223.1.
    PIRiT06532.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U56697 mRNA. Translation: AAB01223.1 .
    PIRi T06532.

    3D structure databases

    ProteinModelPortali P52904.
    SMRi P52904. Positions 25-347.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P52904. 1 interaction.

    Proteomic databases

    PRIDEi P52904.
    ProMEXi P52904.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.920. 1 hit.
    3.40.50.970. 1 hit.
    InterProi IPR027110. PDHB.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005475. Transketolase-like_Pyr-bd.
    IPR005476. Transketolase_C.
    [Graphical view ]
    PANTHERi PTHR11624:SF56. PTHR11624:SF56. 1 hit.
    Pfami PF02779. Transket_pyr. 1 hit.
    PF02780. Transketolase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00861. Transket_pyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 1 hit.
    SSF52922. SSF52922. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Luethy M.H., Miernyk J.A., Randall D.D.
      Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiODPB_PEA
    AccessioniPrimary (citable) accession number: P52904
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program