Q9FLQ4 · ODO2A_ARATH

  • Protein
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

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) (By similarity).

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.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site435
Active site439

GO annotations

AspectTerm
Cellular Componentcytosolic ribosome
Cellular Componentmitochondrion
Cellular Componentoxoglutarate dehydrogenase complex
Cellular Componentplastid
Molecular Functiondihydrolipoyllysine-residue succinyltransferase activity
Molecular Functionsalicylic acid binding
Molecular Functionzinc ion binding
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 1, mitochondrial
  • EC number
  • Alternative names
    • 2-oxoglutarate dehydrogenase complex component E2-1 (OGDC-E2-1)
    • Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1
    • E2K-1

Gene names

    • ORF names
      MCO15.2
    • Ordered locus names
      At5g55070

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9FLQ4
  • Secondary accessions
    • Q9ZRQ1

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

PTM/Processing

Features

Showing features for transit peptide, chain, modified residue.

TypeIDPosition(s)Description
Transit peptide1-86Mitochondrion
ChainPRO_000039951287-464Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
Modified residue134N6-lipoyllysine

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain93-168Lipoyl-binding
Region168-242Disordered
Compositional bias209-225Pro residues
Compositional bias227-242Basic and acidic residues

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    464
  • Mass (Da)
    50,134
  • Last updated
    2001-03-01 v1
  • Checksum
    D5BD3083ACA39879
MMLRAVFRRASIRGSSSASGLGKSLQSSRVAVSAQFHSVSATETLVPRGNHAHSFHHRSCPGCPDCSRTIINGYQGTALQRWVRPFSSDSGDVVEAVVPHMGESITDGTLAAFLKKPGDRVEADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGNKVARISTSADAVSHVAPSEKAPEKPAPKPSPPAEKPKVESTKVAEKPKAPSPPPPPPSKQSAKEPQLPPKDRERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFLEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRDADKMNFADIEKTINGLAKKATEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVQRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRIKDVVEDPQRLLLDI

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict30-34in Ref. 1; CAA11553
Sequence conflict70in Ref. 1; CAA11553
Sequence conflict74in Ref. 1; CAA11553
Compositional bias209-225Pro residues
Sequence conflict218-219in Ref. 1; CAA11553
Compositional bias227-242Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ223803
EMBL· GenBank· DDBJ
CAA11553.1
EMBL· GenBank· DDBJ
mRNA
AB010071
EMBL· GenBank· DDBJ
BAB08576.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED96577.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
ANM68999.1
EMBL· GenBank· DDBJ
Genomic DNA
AY042897
EMBL· GenBank· DDBJ
AAK68837.1
EMBL· GenBank· DDBJ
mRNA
AY128726
EMBL· GenBank· DDBJ
AAM91126.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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