A0AAI8MBQ8 · A0AAI8MBQ8_9BRAD
- ProteinFumarate hydratase class II
- GenefumC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids482 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Miscellaneous
There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors.
Catalytic activity
- (S)-malate = fumarate + H2O
Pathway
Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 117-119 | substrate | ||||
Sequence: SGT | ||||||
Binding site | 148-151 | substrate; in site B | ||||
Sequence: HPND | ||||||
Binding site | 158-160 | substrate | ||||
Sequence: SSN | ||||||
Binding site | 206 | substrate | ||||
Sequence: T | ||||||
Active site | 207 | Proton donor/acceptor | ||||
Sequence: H | ||||||
Active site | 337 | |||||
Sequence: S | ||||||
Binding site | 338 | substrate | ||||
Sequence: S | ||||||
Binding site | 343-345 | substrate | ||||
Sequence: KVN | ||||||
Site | 350 | Important for catalytic activity | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | fumarate hydratase activity | |
Biological Process | fumarate metabolic process | |
Biological Process | malate metabolic process | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFumarate hydratase class II
- EC number
- Short namesFumarase C
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Bradyrhizobium
Accessions
- Primary accessionA0AAI8MBQ8
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MDVLMAKAARSKPTNSKTARP | ||||||
Domain | 31-361 | Fumarate lyase N-terminal | ||||
Sequence: GPIEVPADRYWGAQTERSRQNFRIGIDRMPISLVHALGIVKLAAAQSNLELGLLDQRRANAIIRAAREVIEGKLDDHFPLVVWQTGSGTQSNMNLNEVIANRANELLGGELGAKKPVHPNDHVNMSQSSNDSFPTAMHIAAANRINADLVPALGELLRALRKKEKEFAKIVKIGRTHTQDATPLTLGQEFSGYAAQVESGIARLKVAVKELYPLAQGGTAVGTGLNSSPRFAKLFAKHAAGITKLPFTSAANKFEALASNDAYVLAHGAINSVATGLFKIANDIRLLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVCCQVFG | ||||||
Domain | 427-480 | Fumarase C C-terminal | ||||
Sequence: LVTALAPKIGYDNAAKVAKTAHANGTTLKEEALRLGLVSAEEFDRLVQPEKMTR |
Sequence similarities
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length482
- Mass (Da)51,935
- Last updated2024-07-24 v1
- ChecksumF2101F2153273625
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP012279 EMBL· GenBank· DDBJ | BAL75033.1 EMBL· GenBank· DDBJ | Genomic DNA |