Q88CC1 · HGLS_PSEPK
- Protein2-oxoadipate dioxygenase/decarboxylase
- GenehglS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids464 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the decarboxylation and hydroxylation of 2-oxoadipate (2OA) to form D-2-hydroxyglutarate (D-2-HGA) (PubMed:31064836, PubMed:32523014).
Is specific for 2-oxoadipate (PubMed:32523014).
Is involved in a D-lysine catabolic pathway (PubMed:31064836).
Is specific for 2-oxoadipate (PubMed:32523014).
Is involved in a D-lysine catabolic pathway (PubMed:31064836).
Catalytic activity
- 2-oxoadipate + O2 = (R)-2-hydroxyglutarate + CO2This reaction proceeds in the forward direction.
Cofactor
Activity regulation
Inhibited by EDTA.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.06 mM | 2-oxoadipate | |||||
0.01 mM | 2-oxoadipate |
kcat is 330 min-1.
Pathway
Amino-acid degradation.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 70 | 2-oxoadipate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 70 | Fe2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 74 | 2-oxoadipate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 74 | Important for substrate specificity | ||||
Sequence: R | ||||||
Binding site | 226 | 2-oxoadipate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 226 | Fe2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 294 | Fe2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 402 | 2-oxoadipate (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | dioxygenase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Community annotation
Catalyzes the intramolecular decarboxylation/hydroxylation of 2-oxoadipate to D-2-hydroxyglutarate.
Source | Submission date | Contributor |
---|---|---|
PubMed:31064836 | 0000-0002-1490-8074 |
Names & Taxonomy
Protein names
- Recommended name2-oxoadipate dioxygenase/decarboxylase
- EC number
- Alternative names
Gene names
Community suggested name: Hydroxyglutarate synthase.
Source | Submission date | Contributor |
---|---|---|
PubMed:31064836 | 0000-0002-1490-8074 |
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ88CC1
Proteomes
Phenotypes & Variants
Disruption phenotype
Deletion mutant is unable to grow on either isomer of lysine.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 74 | Loss of activity. | ||||
Sequence: R → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000457782 | 1-464 | 2-oxoadipate dioxygenase/decarboxylase | |||
Sequence: MPANDFVSPDSIRAQFSAAMSLMYKQEVPLYGTLLELVSEINQQVMAQQPEVAEALRWTGEIERLDQERHGAIRVGTAEELATIARLFAVMGMQPVGYYDLSSAGVPVHSTAFRAVHEQSLHVSPFRVFTSLLRLELIDNPQLRELAQSILAKRQIFTSRALELIAQCEREGGLDAADAETFVQEALHTFRWHQDATVTAEQYQQLHDQHRLIADVVAFKGPHINHLTPRTLDIDAIQLGMPAKGIPPKAVVEGPPTRRHPILLRQTSFKALQETVAFRDQQGREGSHTARFGEIEQRGAALTPKGRQLYDKLLDATRVALGGAPAEANAERYMALLQANFAEFPDDLAQMREQGLAYFRYFATEKGLAARDQEGRPTTLQGLIDAGHVHFEALVYEDFLPVSAAGIFQSNLGDDAQAEYGSNANREAFEAALGLQVQDELALYAQSERRSLQACAQALNLGSM |
Proteomic databases
Expression
Induction
Up-regulated when grown on L-lysine, D-lysine or 2-aminoadipate.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length464
- Mass (Da)51,372
- Last updated2003-06-01 v1
- Checksum59A237FBD2E79FDC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE015451 EMBL· GenBank· DDBJ | AAN70825.1 EMBL· GenBank· DDBJ | Genomic DNA |