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P81896

- ODO2_SOLTU

UniProt

P81896 - ODO2_SOLTU

Protein

Dihydrolipoamide-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).1 Publication

    Catalytic activityi

    Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.1 Publication

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Pathwayi

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
    2. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    UniPathwayiUPA00868; UER00840.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoamide-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC:2.3.1.61)
    Alternative name(s):
    2-oxoglutarate dehydrogenase complex component E2
    Short name:
    OGDC-E2
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
    E2K
    OrganismiSolanum tuberosum (Potato)
    Taxonomic identifieri4113 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
    ProteomesiUP000011115: Unplaced

    Subcellular locationi

    Mitochondrion membrane 1 Publication

    GO - Cellular componenti

    1. mitochondrial membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›20›20Dihydrolipoamide-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexPRO_0000238929Add
    BLAST

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Sequence Analysis

    Keywords - Domaini

    Lipoyl

    Sequencei

    Sequence statusi: Fragment.

    P81896-1 [UniParc]FASTAAdd to Basket

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    XSNSGDLVDA VVPYMGESIS                                    20
    Length:20
    Mass (Da):2,051
    Last modified:June 1, 2000 - v1
    Checksum:i9256BE292E26A344
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei20 – 2011 Publication

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Plant mitochondrial 2-oxoglutarate dehydrogenase complex: purification and characterization in potato."
      Millar A.H., Hill S.A., Leaver C.J.
      Biochem. J. 343:327-334(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
      Strain: cv. Romano1 Publication.
      Tissue: Tuber1 Publication.

    Entry informationi

    Entry nameiODO2_SOLTU
    AccessioniPrimary (citable) accession number: P81896
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: June 1, 2000
    Last modified: October 1, 2014
    This is version 50 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3