P41020 · URE1_SPOPA
- ProteinUrease subunit alpha
- GeneureC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids570 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Catalytic activity
- 2 H+ + H2O + urea = CO2 + 2 NH4+
Cofactor
Note: Binds 2 nickel ions per subunit.
Activity regulation
Inhibited by fluoride.
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 | 137 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 139 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 139 | substrate | ||||
Sequence: H | ||||||
Binding site | 170 | substrate | ||||
Sequence: A | ||||||
Binding site | 220 | Ni2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 220 | Ni2+ 2 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 222 | substrate | ||||
Sequence: H | ||||||
Binding site | 249 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 249 | substrate | ||||
Sequence: H | ||||||
Binding site | 275 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 323 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 363 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 366 | substrate | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | nickel cation binding | |
Molecular Function | urease activity | |
Biological Process | urea catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUrease subunit alpha
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Planococcaceae > Sporosarcina
Accessions
- Primary accessionP41020
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000067536 | 1-570 | Urease subunit alpha | |||
Sequence: MKINRQQYAESYGPTVGDQVRLADTDLWIEVEKDTTYGDEAVNFGGGKVLREGMGENGTYTRTENVLDLLLTNALILDYTGIYKADIGVKDGYIVGIGKGGNPDIMDGVTPNMIVGTATEVIAAEGKIVTAGGIDTHVHFINPDQVDVALANGITTLFGGGTGPAEGSKATTVTPGPWNIEKMLKSTEGLPINVGILGKGHGSSIAPIMEQIDAGAAGLKIHEDWGATPASIDRSLTVADEADVQVAIHSDTLNEAGFLEDTLRAINGRVIHSFHVEGAGGGHAPDIMAMAGHPNVLPSSTNPTRPFTVNTIDEHLDMLMVCHHLKQNIPEDVAFADSRIRPETIAAEDILHDLGIISMMSTDALAMGRAGEMVLRTWQTADKMKKQRGPLAEEKNGSDNFRAKRYVSKYTINPAIAQGIAHEVGSIEEGKFADLVLWEPKFFGVKADRVIKGGIIAYAQIGDPSASIPTPQPVMGRRMYGTVGDLIHDTNITFMSKSSIQQGVPAKLGLKRRIGTVKNCRNIGKKDMKWNDVTTDIDINPETYEVKVDGEVLTCEPVKELPMAQRYFLF | ||||||
Modified residue | 220 | N6-carboxylysine | ||||
Sequence: K |
Post-translational modification
Carboxylation allows a single lysine to coordinate two nickel ions.
Interaction
Subunit
Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.
Chemistry
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 132-570 | Urease | ||||
Sequence: GGIDTHVHFINPDQVDVALANGITTLFGGGTGPAEGSKATTVTPGPWNIEKMLKSTEGLPINVGILGKGHGSSIAPIMEQIDAGAAGLKIHEDWGATPASIDRSLTVADEADVQVAIHSDTLNEAGFLEDTLRAINGRVIHSFHVEGAGGGHAPDIMAMAGHPNVLPSSTNPTRPFTVNTIDEHLDMLMVCHHLKQNIPEDVAFADSRIRPETIAAEDILHDLGIISMMSTDALAMGRAGEMVLRTWQTADKMKKQRGPLAEEKNGSDNFRAKRYVSKYTINPAIAQGIAHEVGSIEEGKFADLVLWEPKFFGVKADRVIKGGIIAYAQIGDPSASIPTPQPVMGRRMYGTVGDLIHDTNITFMSKSSIQQGVPAKLGLKRRIGTVKNCRNIGKKDMKWNDVTTDIDINPETYEVKVDGEVLTCEPVKELPMAQRYFLF |
Sequence similarities
Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length570
- Mass (Da)61,400
- Last updated2021-06-02 v2
- Checksum4F6DC7E2703A7568
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 19 | in Ref. 1; CAA55175 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 28-29 | in Ref. 1; CAA55175 | ||||
Sequence: WI → G | ||||||
Sequence conflict | 35-41 | in Ref. 1; CAA55175 | ||||
Sequence: TTYGDEA → YYLGDEV | ||||||
Sequence conflict | 263 | in Ref. 1; CAA55175 | ||||
Sequence: L → V | ||||||
Sequence conflict | 403 | in Ref. 1; CAA55175 | ||||
Sequence: A → L | ||||||
Sequence conflict | 420 | in Ref. 1; CAA55175 | ||||
Sequence: I → M | ||||||
Sequence conflict | 498-502 | in Ref. 4; AAA73986 | ||||
Sequence: SSIQQ → ELNSE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X78411 EMBL· GenBank· DDBJ | CAA55175.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
KR133628 EMBL· GenBank· DDBJ | AKN22164.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UGYZ01000002 EMBL· GenBank· DDBJ | SUJ11615.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U29368 EMBL· GenBank· DDBJ | AAA73986.1 EMBL· GenBank· DDBJ | Genomic DNA |