A1L258 · D2HDH_DANRE
- ProteinD-2-hydroxyglutarate dehydrogenase, mitochondrial
- Gened2hgdh
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids533 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Catalyzes the oxidation of D-2-hydroxyglutarate (D-2-HG) to alpha-ketoglutarate (By similarity).
Also catalyzes the oxidation of other D-2-hydroxyacids, such as D-malate (D-MAL) and D-lactate (D-LAC) (By similarity).
Exhibits high activities towards D-2-HG and D-MAL but a very weak activity towards D-LAC (By similarity).
Also catalyzes the oxidation of other D-2-hydroxyacids, such as D-malate (D-MAL) and D-lactate (D-LAC) (By similarity).
Exhibits high activities towards D-2-HG and D-MAL but a very weak activity towards D-LAC (By similarity).
Catalytic activity
- (R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
- (R)-malate + A = AH2 + oxaloacetateThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 397 | (R)-2-hydroxyglutarate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 397 | (R)-lactate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 397 | (R)-malate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 401 | (R)-2-hydroxyglutarate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 401 | (R)-malate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 412 | (R)-2-hydroxyglutarate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 412 | (R)-malate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 445 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 452 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 454 | (R)-2-hydroxyglutarate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 486 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 487 | (R)-2-hydroxyglutarate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 487 | (R)-lactate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 487 | (R)-malate (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | (R)-2-hydroxyglutarate dehydrogenase activity | |
Molecular Function | FAD binding | |
Molecular Function | zinc ion binding | |
Biological Process | malate metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameD-2-hydroxyglutarate dehydrogenase, mitochondrial
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionA1L258
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-55 | Mitochondrion | ||||
Sequence: MGLFQKCSRLSLRSSYMWSVCPQYSIAVTARETPDRALIVHWTQHRDVHNSRRLG | ||||||
Chain | PRO_0000347235 | 56-533 | D-2-hydroxyglutarate dehydrogenase, mitochondrial | |||
Sequence: ANPANPSAAPPRLPFSRVTQEDLSFFRALLPGRTITDPDLLKSSNVDWLKTVQGSSDVLLRPKTTEGVSQILRYCNERNLAVCPQGGNTGLVGGSVPVFDEIILSTSLMNQVFAFDNISGILTCQAGCVLENLSHYLEERDFIMPLDLGAKGSCHIGGNVSTNAGGLRLLRYGSLRGTVLGLEVVLADGHVLNCLATLRKDNTGYDLKQLFIGSEGTLGVITAVSILCPRKPKAVNVAFLGCSSFQQLLETFQCCRGMLGEILSAFEFLDASCMNLLEKHLKLTNPITECPFYIVIETAGSNATHDEEKLHQFLEEVMTSSLVTDGTVATEATKIKALWSLRERVTEALTHEGYTYKYDISLPVEKIYDLVQDMRRHLGGMAKNVVGYGHVGDGNLHLNITSPSKDFDLLAAIEPYVYEWTSQWKGSISAEHGLGLKKRNYIYYSKPSEAVALMGSIKAMLDPKGILNPYKTLPDNIN |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 107-286 | FAD-binding PCMH-type | ||||
Sequence: VQGSSDVLLRPKTTEGVSQILRYCNERNLAVCPQGGNTGLVGGSVPVFDEIILSTSLMNQVFAFDNISGILTCQAGCVLENLSHYLEERDFIMPLDLGAKGSCHIGGNVSTNAGGLRLLRYGSLRGTVLGLEVVLADGHVLNCLATLRKDNTGYDLKQLFIGSEGTLGVITAVSILCPRK |
Sequence similarities
Belongs to the FAD-binding oxidoreductase/transferase type 4 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length533
- Mass (Da)58,714
- Last updated2007-02-06 v1
- ChecksumA6636E8DB7B1485A
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F1R1R3 | F1R1R3_DANRE | d2hgdh | 533 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC129361 EMBL· GenBank· DDBJ | AAI29362.1 EMBL· GenBank· DDBJ | mRNA |