Q9FLQ4 · ODO2A_ARATH
- ProteinDihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids464 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- N6-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N6-[(R)-S8-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2]
Cofactor
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 435 | |||||
Sequence: H | ||||||
Active site | 439 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosolic ribosome | |
Cellular Component | mitochondrion | |
Cellular Component | oxoglutarate dehydrogenase complex | |
Cellular Component | plastid | |
Molecular Function | dihydrolipoyllysine-residue succinyltransferase activity | |
Molecular Function | salicylic acid binding | |
Molecular Function | zinc ion binding | |
Biological Process | L-lysine catabolic process to acetyl-CoA via saccharopine | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9FLQ4
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-86 | Mitochondrion | ||||
Sequence: MMLRAVFRRASIRGSSSASGLGKSLQSSRVAVSAQFHSVSATETLVPRGNHAHSFHHRSCPGCPDCSRTIINGYQGTALQRWVRPF | ||||||
Chain | PRO_0000399512 | 87-464 | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial | |||
Sequence: SSDSGDVVEAVVPHMGESITDGTLAAFLKKPGDRVEADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGNKVARISTSADAVSHVAPSEKAPEKPAPKPSPPAEKPKVESTKVAEKPKAPSPPPPPPSKQSAKEPQLPPKDRERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFLEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRDADKMNFADIEKTINGLAKKATEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVQRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRIKDVVEDPQRLLLDI | ||||||
Modified residue | 134 | N6-lipoyllysine | ||||
Sequence: K |
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 93-168 | Lipoyl-binding | ||||
Sequence: VVEAVVPHMGESITDGTLAAFLKKPGDRVEADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGNKVARIS | ||||||
Region | 168-242 | Disordered | ||||
Sequence: STSADAVSHVAPSEKAPEKPAPKPSPPAEKPKVESTKVAEKPKAPSPPPPPPSKQSAKEPQLPPKDRERRVPMTR | ||||||
Compositional bias | 209-225 | Pro residues | ||||
Sequence: PKAPSPPPPPPSKQSAK | ||||||
Compositional bias | 227-242 | Basic and acidic residues | ||||
Sequence: PQLPPKDRERRVPMTR |
Sequence similarities
Belongs to the 2-oxoacid dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length464
- Mass (Da)50,134
- Last updated2001-03-01 v1
- ChecksumD5BD3083ACA39879
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 30-34 | in Ref. 1; CAA11553 | ||||
Sequence: VAVSA → LVASS | ||||||
Sequence conflict | 70 | in Ref. 1; CAA11553 | ||||
Sequence: I → V | ||||||
Sequence conflict | 74 | in Ref. 1; CAA11553 | ||||
Sequence: Y → F | ||||||
Compositional bias | 209-225 | Pro residues | ||||
Sequence: PKAPSPPPPPPSKQSAK | ||||||
Sequence conflict | 218-219 | in Ref. 1; CAA11553 | ||||
Sequence: Missing | ||||||
Compositional bias | 227-242 | Basic and acidic residues | ||||
Sequence: PQLPPKDRERRVPMTR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |