P0CS22 · UREA_CRYNJ
- ProteinUrease
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids833 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Plays a nutritional role via nitrogen acquisition in the environment (By similarity).
Contributes to the central nervous system invasion by enhancing yeast sequestration within microcapillary beds (such as within the brain) during hematogenous spread, thereby facilitating blood-to-brain invasion by C.neoformans (By similarity).
Affects fitness within the mammalian phagosome, promoting non-lytic exocytosis while delaying intracellular replication and thus reducing phagolysosomal membrane damage, events that could facilitate cryptococcal dissemination when transported inside macrophages (By similarity).
Urease activity is also associated with the regulation of key intracellular metabolic pathways, including melanin biosynthesis, polyamine biosynthesis, as well as intracellular levels of proline and reactive oxygen species (By similarity).
Contributes to the central nervous system invasion by enhancing yeast sequestration within microcapillary beds (such as within the brain) during hematogenous spread, thereby facilitating blood-to-brain invasion by C.neoformans (By similarity).
Affects fitness within the mammalian phagosome, promoting non-lytic exocytosis while delaying intracellular replication and thus reducing phagolysosomal membrane damage, events that could facilitate cryptococcal dissemination when transported inside macrophages (By similarity).
Urease activity is also associated with the regulation of key intracellular metabolic pathways, including melanin biosynthesis, polyamine biosynthesis, as well as intracellular levels of proline and reactive oxygen species (By similarity).
Catalytic activity
- 2 H+ + H2O + urea = CO2 + 2 NH4+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 Ni2+ ions per subunit.
Activity regulation
The urease accessory proteins URE4, URE6 and URE7 are required for urease activity, URE7 supplying nickel for the functional urease.
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 | 400 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 402 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 402 | urea (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 433 | urea (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 483 | Ni2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 483 | Ni2+ 2 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 485 | urea (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 512 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 512 | urea (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 538 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 586 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 626 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 629 | urea (UniProtKB | ChEBI) | ||||
Sequence: A |
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
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUrease
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Cryptococcus > Cryptococcus neoformans species complex
Accessions
- Primary accessionP0CS22
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000067527 | 1-833 | Urease | |||
Sequence: MHLLPRETDKLIVTTLGTLAQRRLARGLILNRAETIALISSQLQEFIRDGRHSVAELMDLGKKMLGRRHVRKGVPESIHTIQVEGTFPDGVFLVTVDDPISSDDGDLNNAFYGSFLPIPSADVFPAAPEPADTLLGALICRKEPIKINASRRRFKLEVKNAGDRPIQVGSHYHFLETNPALIFDRLLSYGYHLDIPAGTAVRFEPGEKKTVTMVEFGGKKIFHGGSGLASGSFDENLRETKVKEMVEKGGFGHKDQEKVEEGPTTEMNREVYASMFGPTTGDKIKLADMDLWIEVEKDYTVYGEECKFGGGKVLRDGGGQASGRHEHEVLDLVITNALIVDWNGIYKADIGVKNGIIVGIGKAGNPDMMDGVTDGMIVGSSTEVIAGEKLIITAGALDVHVHYICPQLMTEALASGITTVVGGGTGPADGSNATTCTSSSFYMQNMIKATDTVPLNFGFTGKGNDSGTNALRDVIEAGACGLKVHEDWGATPEVIDRALSIADEYDVQVNLHSDTLNESGYVESTLAAIKGRTIHSYHTEGAGGGHAPDIIVVCEYENVLPSSTNPTRPYAVNTLDEHLDMLMVCHHLDKSIPEDIAFADSRIRSETVAAEDVLQDTGAISMISSDCQAMGRIGEVITRTWRTAAKMKQFRGPLEGDEPTRDNNRVKRYVAKYTINPAITHGMSHLIGQVAVGCLADLVFWTAESFGARPEMILKGGVIAWAAMGDANASIPTVQPVIGRPMWGSQPEAAALNSIVWVSQASLDKDLVKRFNIKKRAEAVKNCRAIGKKDMKWNDSMPKMTVDPETYDVHADGVLCDVPPADKLPLTKRYFVY | ||||||
Modified residue | 483 | N6-carboxylysine | ||||
Sequence: K |
Post-translational modification
Carboxylation allows a single lysine to coordinate two nickel ions.
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 395-833 | Urease | ||||
Sequence: GALDVHVHYICPQLMTEALASGITTVVGGGTGPADGSNATTCTSSSFYMQNMIKATDTVPLNFGFTGKGNDSGTNALRDVIEAGACGLKVHEDWGATPEVIDRALSIADEYDVQVNLHSDTLNESGYVESTLAAIKGRTIHSYHTEGAGGGHAPDIIVVCEYENVLPSSTNPTRPYAVNTLDEHLDMLMVCHHLDKSIPEDIAFADSRIRSETVAAEDVLQDTGAISMISSDCQAMGRIGEVITRTWRTAAKMKQFRGPLEGDEPTRDNNRVKRYVAKYTINPAITHGMSHLIGQVAVGCLADLVFWTAESFGARPEMILKGGVIAWAAMGDANASIPTVQPVIGRPMWGSQPEAAALNSIVWVSQASLDKDLVKRFNIKKRAEAVKNCRAIGKKDMKWNDSMPKMTVDPETYDVHADGVLCDVPPADKLPLTKRYFVY |
Sequence similarities
In the C-terminal section; belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length833
- Mass (Da)90,455
- Last updated2011-06-28 v1
- ChecksumE090343FE3252584
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE017348 EMBL· GenBank· DDBJ | AAW45058.1 EMBL· GenBank· DDBJ | Genomic DNA |