A0A6L8P5M7 · A0A6L8P5M7_BACAN

  • 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
    • Ordered locus names
      GBAA_1269

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Ames ancestor
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group

Accessions

  • Primary accession
    A0A6L8P5M7
  • Secondary accessions
    • A0A0F7RM04
    • E9R4S5
    • E9R4S6
    • Q6I1T4
    • Q6KVM4
    • Q81TK2

Proteomes

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
Region84-124Disordered
Compositional bias108-122Polar residues
Domain124-161Peripheral subunit-binding (PSBD)
Region156-179Disordered

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    418
  • Mass (Da)
    45,260
  • Last updated
    2020-10-07 v1
  • Checksum
    2F80E2458C9EEC17
MIEIKVPELAESITEGTISQWLLNVGDKVEKGGSVVELETDKVNVEIIAEDSGIVSKLLGEPGDTVEVGATIAILDANGAPVAVSTPAPAEQSKQETAEAPKAAAPSAEQTATLQGLPNTNRPIASPAARKMARELGIDLNDVRSTDPLGRVRPHDVQAHAAAPKEAPAAPKSPAPAPVAKTEFEKPVERVKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMTAIMELRKERKDAFEKKHDVRLGFMSFFTKAVVAALKQFPLLNAEIQGDELIIKKFYDIGIAVAAPDGLVVPVVRDANQLNFAEIESEIRELGKKARDNKLSLKELQGGTFTITNGGVFGSLMSTPILNSPQVGILGMHKIQVRPVAIDNERMENRPMMYIALSYDHRIVDGKEAVSFLVAVKDMLEDPKSLLLEG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias108-122Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE017334
EMBL· GenBank· DDBJ
AAT30360.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp