A0A229Z3R7 · A0A229Z3R7_9EURO
- ProteinUrease
- GeneURE1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids836 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- urea + 2 H2O + H+ = hydrogencarbonate + 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 | 405 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 407 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 488 | Ni2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 488 | Ni2+ 2 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 490 | substrate | ||||
Sequence: H | ||||||
Binding site | 517 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 543 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 591 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 631 | 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
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionA0A229Z3R7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 488 | N6-carboxylysine | ||||
Sequence: K |
Post-translational modification
Carbamylation allows a single lysine to coordinate two nickel ions.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 400-836 | Urease | ||||
Sequence: GGFDTHIHFICPQQVDEALASGITTFLGGGTGPSTGTNATTCTPGPTHMRQMIQACDSLPINVGITGKGNDCGGKSIEEQIRAGAAGLKLHEDWGSTPAAIDTCLDMCDKFDVQCMIHTDTLNESGFVEQTVKSFKNRTIHTYHTEGAGGGHAPDIISVVEHPNVLPSSTNPTRPFTMNTLDEHLDMLMVCHHLSKNIPEDVAFAESRIRAETIAAEDVLHDLGAISMMSSDSQAMGRCGEVILRTWNTAHKNKAQRGPLQEDEGTGADNFRVKRYISKYTINPAIAQGMSHLIGSVEVGKLADLVIWHPSSFGTKPAQILKSGMIVASQMGDPNGSIPTIEPVIMRPMFGSFVPSTSIMWVSQASIDDGIVQSYGLKKRIEPVRNCRNVGKKDMKFNDTMPKMRVDPESYRVEADGVLCEAEPADSLPLTQDYFVY |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length836
- Mass (Da)91,013
- Last updated2017-10-25 v1
- Checksum30B9FCB7DD8F0095
Keywords
- Technical term