A0A3D9D6D9 · A0A3D9D6D9_9FLAO
- ProteinFumarate hydratase class II
- GenefumC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids464 (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 | 318 | |||||
Sequence: S | ||||||
Binding site | 319 | substrate | ||||
Sequence: S | ||||||
Binding site | 324-326 | substrate | ||||
Sequence: KVN | ||||||
Site | 331 | 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 > Bacteroidota > Flavobacteriia > Flavobacteriales > Weeksellaceae > Chryseobacterium group > Chryseobacterium
Accessions
- Primary accessionA0A3D9D6D9
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-342 | Fumarate lyase N-terminal | ||||
Sequence: GEVQVPADKFWGAQTERSRNNFKIGPEGSMPHEIIEAFAYLKKAAAYTNTDLGVLSAEKRDMIAKVCDEILEGKLNDQFPLVIWQTGSGTQSNMNINEVVSNRAHVNNGGTLGDKSEIHPNDDVNKSQSSNDTYPTAMHIAAYKKVVEVTIPAVEKLKNTLSAKAEAFKDIVKIGRTHLMDATPLTLGQEFSGYKAQLEFGLRALKNTLPHLSELALGGTAVGTGLNTPNGYDVKVAEYIAKFTNHPFVTAENKFEALAAHDAIVESHGALKQLAVSLFKIAQDIRLLASGPRSGIGEIHIPENEPGSSIMPGKVNPTQNEAMTMVCAQVLG | ||||||
Region | 118-141 | Disordered | ||||
Sequence: NGGTLGDKSEIHPNDDVNKSQSSN | ||||||
Domain | 408-460 | Fumarase C C-terminal | ||||
Sequence: LVTALNTHIGYENAAKIAKTAHKNGTTLKEEAVNLGFLTAEQFDEWVKPENMV |
Sequence similarities
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length464
- Mass (Da)50,574
- Last updated2019-01-16 v1
- Checksum7E4A9C93F4311F24