A0AA96UJY8 · A0AA96UJY8_9BACI

  • Protein
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
  • Gene
    odhB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO2.

Catalytic activity

Cofactor

(R)-lipoate (UniProtKB | Rhea| CHEBI:83088 )

Note: Binds 1 lipoyl cofactor covalently.

Pathway

Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.

GO annotations

AspectTerm
Cellular Componentoxoglutarate dehydrogenase complex
Molecular Functiondihydrolipoyllysine-residue succinyltransferase activity
Biological ProcessL-lysine catabolic process to acetyl-CoA via saccharopine
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
  • EC number
  • Alternative names
    • 2-oxoglutarate dehydrogenase complex component E2

Gene names

    • Name
      odhB
    • ORF names
      RUI02_10490

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • TSA-4
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus

Accessions

  • Primary accession
    A0AA96UJY8

Subcellular Location

Interaction

Subunit

Forms a 24-polypeptide structural core with octahedral symmetry. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the complex contains multiple copies of the three enzymatic components (E1, E2 and E3).

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain1-76Lipoyl-binding
Region75-191Disordered
Compositional bias91-107Basic and acidic residues
Domain123-160Peripheral subunit-binding (PSBD)
Compositional bias166-180Polar residues

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    417
  • Mass (Da)
    45,956
  • Last updated
    2024-03-27 v1
  • Checksum
    0700BC2CB580C816
MAEIKVPELAESISEGTIAQWLKQPGDYVEQGEYLLELETDKVNVELTAEESGVLQEVLKDSGDTVQVGEIIGTISEGAGESSAPAPTEKAESKESVKEEKQAEPAAQEVSEEAQSEAKSRTIASPSARKLAREKGIDLSQVPTGDPLGRVRKQDVEAYEKPASKPAPQQKQQPQAPKAQQSFDKPVEVQKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMTAVMNLRKRRKDQFFEQNEVKLGFMSFFTKAVVAALKKYPLLNAEIQGDELIVKKFYDIGIAVAADEGLVVPVVRDADRLTFAGIEKEIGELAKKARNNKLTLSELQGGSFTITNGGTFGSLMSTPILNSPQVGILGMHKIQLRPVAIDEERFENRPMMYIALSYDHRIVDGKEAVGFLVTIKKLLEDPEQLLLEG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias91-107Basic and acidic residues
Compositional bias166-180Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP136099
EMBL· GenBank· DDBJ
WNW98215.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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