A0A7J9KLN1 · A0A7J9KLN1_GOSSC
- ProteinFormate dehydrogenase, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids382 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the NAD+-dependent oxidation of formate to carbon dioxide. Involved in the cell stress response.
Catalytic activity
- formate + NAD+ = CO2 + NADH
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 126 | substrate | ||||
Sequence: I | ||||||
Binding site | 150 | substrate | ||||
Sequence: N | ||||||
Binding site | 205-206 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: RI | ||||||
Binding site | 225 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 260-264 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: PLTEK | ||||||
Binding site | 286 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 288 | Important for catalytic activity | ||||
Sequence: R | ||||||
Binding site | 312 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 336 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 336-339 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: HISG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | mitochondrion | |
Molecular Function | formate dehydrogenase (NAD+) activity | |
Molecular Function | NAD binding | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | |
Biological Process | formate catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFormate dehydrogenase, mitochondrial
- EC number
- Short namesFDH
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Malvales > Malvaceae > Malvoideae > Gossypium
Accessions
- Primary accessionA0A7J9KLN1
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 67-364 | D-isomer specific 2-hydroxyacid dehydrogenase catalytic | ||||
Sequence: LESQGHQYIVTDDKEGPGCELEKHIPDLHVLISTPFHPAYVTAERIKKAKNLQLLLTAGIGSDHVDLKAAAEAGLTVAEVTGSNVVSVAEDELMRILILVRNFVPGYHQVITGDWNVAGIAYRAYDLEGKTVGTIGAGRIGKLLLQRLKPFNCNLLYHDRVKIDPELEKQTGAKFEEDLDAMLPKCDIIVINMPLTEKTRGMFDKDRIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIAGYSGDVWYPQPAPKDHPWRYMPNQAMTPHISGTTIDAQLRYAAGVKDMLERYFKGED | ||||||
Domain | 160-338 | D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding | ||||
Sequence: MRILILVRNFVPGYHQVITGDWNVAGIAYRAYDLEGKTVGTIGAGRIGKLLLQRLKPFNCNLLYHDRVKIDPELEKQTGAKFEEDLDAMLPKCDIIVINMPLTEKTRGMFDKDRIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIAGYSGDVWYPQPAPKDHPWRYMPNQAMTPHIS |
Sequence similarities
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length382
- Mass (Da)42,053
- Last updated2021-04-07 v1
- ChecksumEBA4DB55FED0D8BA
Keywords
- Technical term