A0A0S3F1W7 · A0A0S3F1W7_9SPHN
- ProteinFumarate hydratase class II
- GenefumC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids461 (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 | 98-100 | substrate | ||||
Sequence: SGT | ||||||
Binding site | 129-132 | substrate; in site B | ||||
Sequence: HPND | ||||||
Binding site | 139-141 | substrate | ||||
Sequence: SSN | ||||||
Binding site | 187 | substrate | ||||
Sequence: T | ||||||
Active site | 188 | Proton donor/acceptor | ||||
Sequence: H | ||||||
Active site | 319 | |||||
Sequence: S | ||||||
Binding site | 320 | substrate | ||||
Sequence: S | ||||||
Binding site | 325-327 | substrate | ||||
Sequence: KVN | ||||||
Site | 332 | 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 | 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 > Sphingomonadales > Sphingomonadaceae > Sphingobium
Accessions
- Primary accessionA0A0S3F1W7
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-343 | Fumarate lyase N-terminal | ||||
Sequence: GAIEVPAAAYWGAQTQRSIENFPFGDSERMPIGIVHALAIVKQAAARVNRKHGLDAKLADAIEIAAAEVVEGKLDDQFPLVIWQTGSGTQSNMNVNEVIAGRANEILTGTRGGKAPVHPNDHVNMSQSSNDSFPTAMHIAAALAATRALLPALERLEGALLAKAKAWDRIVKIGRTHLQDATPLTLGQEFSGYVAQLRLARTRTMPLVEHGLTKLAQGGTAVGTGLNTPPGFAEDVAAEIAALTGLPFETAPNKFEALASHDTLVDFSGRLNSIAVAVTKIANDIRLLGSGPRSGLGELDLPANEPGSSIMPGKVNPTQCEMLTMVAAQVIG | ||||||
Domain | 409-461 | Fumarase C C-terminal | ||||
Sequence: LVTALAPEIGYDNAAKIAKHAHVEGLTLKQAGLALGLVDEATFDRLVRPENMV |
Sequence similarities
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length461
- Mass (Da)48,628
- Last updated2016-02-17 v1
- ChecksumEBD83A09CF7C3489
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP013264 EMBL· GenBank· DDBJ | ALR21642.1 EMBL· GenBank· DDBJ | Genomic DNA |