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J9RNE3 · J9RNE3_9ACTN

  • Protein
    Pyruvate dehydrogenase E1 component
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Predicted
  • Annotation score
    2/5

Function

function

Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

thiamine diphosphate (UniProtKB | Rhea| CHEBI:58937 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site295Mg2+ (UniProtKB | ChEBI)
Binding site325Mg2+ (UniProtKB | ChEBI)
Binding site327Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionmagnesium ion binding
Molecular Functionpyruvate dehydrogenase (acetyl-transferring) activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyruvate dehydrogenase E1 component
  • EC number

Gene names

    • ORF names
      KTR9_3112

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KTR9
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Gordoniaceae > Gordonia

Accessions

  • Primary accession
    J9RNE3

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias28-49Polar residues
Region28-55Disordered
Domain197-366Transketolase N-terminal
Domain551-766Pyruvate dehydrogenase E1 component middle
Domain782-916Transketolase-like C-terminal

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    964
  • Mass (Da)
    106,278
  • Last updated
    2012-11-28 v1
  • MD5 Checksum
    DAE016EEC216797F0307394238A0BDD1
MPDAMQSDHHPESGLSEGVGITVTNQMDHATQDVSPSEPAGNTGPRSNGRAAGQRVRVIREGVASYLPDIDPDETDEWLDSFDALLDAAGPGRARYLMLRLLERAGEKRVSIPALTSTDYVNTIPTEAEPWFPGDEDVERRFRQMIRWNAAIMVHRAQRPGVGVGGHISTYASSASLYEVGFNHFFRGKDHSGGGDHIFIQGHASPGIYARAYLEGRIDEARMDGFRQEHSHAGEGGGLPSYPHPRLMPDFWEFPTVSMGLGPMNAVYQARFNHYLHDRGIKDTSDQHVWAFLGDGEMDEPESRGFASFAATEGLDNLTFVINCNLQRLDGPVRGNGKIIQELESFFRGAGWNVIKVIWGREWDSLLHADRDGALVNLMNTTPDGDFQTYKANDGAFVREHFFNRDPRTKELVKDLSDADIWNLKRGGHDYRKIHAAYASAMTHKGQPTVILAHTIKGYTLGKHFEGRNATHQMKKLTLDDLKAFRDSTRIPITDEQLEKDPYLPPYYNPGKDSPELQYMLDRRKTLGGFLPSRRTKSKVLKADMSSALKATAKGSGKQQVATTMALVRVFKDLLRDKEIGKRIVPIIPDEARTFGMDSWFPTLKIYNRNGQLYTSVDAELMLAYKESSEGQILHEGINEAGSAASFAAVGTSYSTHDEPMIPLYIFYSMFGFQRTGDSFWAAADQMARGFVIGATAGRTTLTGEGLQHADGHSPLLAATNPAVVAYDPAFAYELGHIVERGIERMYGDDPENVFYYLTVYNEPISQPAKPEGLDPAGIVKGAYRFQKAPEGKQHPANILVSGVTMPDALRAADMLAEEWNVGADVYSVTSWSELARDGIRADREAVRDPGAEPAPAYLTELLADAAGPFVGVSDYMRGVQEQIRAYLPGTYLTLGTDGFGFSDTRPAARRFFNVDAESIVVAVLVALARDGNIEMSVAKQAADKYRIDDVSAAPEQTSDPGVA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias28-49Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002907
EMBL· GenBank· DDBJ
AFR49747.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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