G8NTI5 · G8NTI5_GRAMM
- ProteinFormate dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids386 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Catalyzes the NAD+-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.
Catalytic activity
- formate + NAD+ = CO2 + NADH
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 123 | substrate | |||
Binding site | 147 | substrate | |||
Binding site | 148 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 148 | NADP+ 2 (UniProtKB | ChEBI) | |||
Binding site | 148 | NADP+ 1 (UniProtKB | ChEBI) | |||
Binding site | 202 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 202 | NADP+ 1 (UniProtKB | ChEBI) | |||
Binding site | 202 | NADP+ 2 (UniProtKB | ChEBI) | |||
Binding site | 202-203 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 203 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 203 | NADP+ 1 (UniProtKB | ChEBI) | |||
Binding site | 203 | NADP+ 2 (UniProtKB | ChEBI) | |||
Binding site | 222 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 224 | NADP+ 1 (UniProtKB | ChEBI) | |||
Binding site | 257-261 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 259 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 259 | NADP+ 1 (UniProtKB | ChEBI) | |||
Binding site | 261 | NADP+ 1 (UniProtKB | ChEBI) | |||
Binding site | 283 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 284 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 284 | NADP+ 1 (UniProtKB | ChEBI) | |||
Binding site | 284 | NADP+ 2 (UniProtKB | ChEBI) | |||
Site | 285 | Important for catalytic activity | |||
Binding site | 309 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 333 | NADP+ 1 (UniProtKB | ChEBI) | |||
Site | 333 | Important for catalytic activity | |||
Binding site | 333-336 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 335 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 335 | NADP+ 1 (UniProtKB | ChEBI) | |||
Binding site | 335 | NADP+ 2 (UniProtKB | ChEBI) | |||
Binding site | 381 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 381 | NADP+ 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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
- EC number
- Short namesFDH
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Acidobacteriota > Terriglobia > Terriglobales > Acidobacteriaceae > Granulicella
Accessions
- Primary accessionG8NTI5
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 72-359 | D-isomer specific 2-hydroxyacid dehydrogenase catalytic | |||
Domain | 156-335 | D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding | |||
Sequence similarities
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length386
- Mass (Da)42,536
- Last updated2012-02-22 v1
- MD5 ChecksumCD90EB5DC42D605FC638AF0F1793955D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003130 EMBL· GenBank· DDBJ | AEU35217.1 EMBL· GenBank· DDBJ | Genomic DNA |