A0A9W8B6M0 · A0A9W8B6M0_9FUNG
- ProteinUrease
- GeneURE1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids880 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- 2 H+ + H2O + urea = CO2 + 2 NH4+
Cofactor
Note: Binds 2 nickel ions per subunit.
Pathway
Nitrogen metabolism; urea degradation; CO2 and NH3 from urea (urease route): step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 410 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 412 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 493 | Ni2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 493 | Ni2+ 2 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 495 | substrate | ||||
Sequence: H | ||||||
Binding site | 522 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 548 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 596 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 636 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | urease complex | |
Molecular Function | nickel cation binding | |
Molecular Function | urease activity | |
Biological Process | urea catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUrease
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Zoopagomycota > Kickxellomycotina > Dimargaritomycetes > Dimargaritales > Dimargaritaceae > Dimargaris
Accessions
- Primary accessionA0A9W8B6M0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 493 | N6-carboxylysine | ||||
Sequence: K |
Post-translational modification
Carbamylation allows a single lysine to coordinate two nickel ions.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 405-880 | Urease | ||||
Sequence: GGIDTHVHFIGLDICTEALANGLTTLIGGGAGPTTGSNATTCTAGQFHTQFMLEATDTIPLNLGFTGKGNTSAPEEIVVQIEAGAIGLKLHEDWGSTPQAIDNCLSVCEQYDVQVNIHTDTLNESGFVEETIAAFKGRTIHTYHSEGAGGGHAPDIITVCSLPNVLPSSTNPTRPYTLNTLDEHIDMLMVCHHLSKNIPEDVAFAESRIRAETIAAEDVLHDMGAISIISSDSQAMGRIGEVISRTWRTAHKMKVQRGHLAPGADDASTFPTAIPVQRSPEKLTQHQSTINSSEGAHPNFAHPSDNFRIRRYVAKYTINPAIAHGISHIVGSVEVGKLADLVMYRPQYFGSRPHIVLKGGTIAWSLLGDANGSIPTTEPMVLRKAFGGLPNAAKRNSLAFISQASIDRDIATNYRVSKRLVPVKRCRQVTKRDMKLNAAMPKLHVDPETYTVTADRQICSCEAVGELPLCQNYNLF |
Sequence similarities
In the C-terminal section; belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length880
- Mass (Da)95,022
- Last updated2023-11-08 v1
- Checksum201C3D37B06F34BE
Keywords
- Technical term