A0A1S2MZS5 · A0A1S2MZS5_9MICC
- ProteinUrease subunit alpha
- GeneureC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids575 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 141 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 143 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 224 | Ni2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 224 | Ni2+ 2 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 226 | substrate | ||||
Sequence: H | ||||||
Binding site | 253 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 279 | Ni2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 327 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 367 | Ni2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D |
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
Names & Taxonomy
Protein names
- Recommended nameUrease subunit alpha
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Rothia
Accessions
- Primary accessionA0A1S2MZS5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 224 | N6-carboxylysine | ||||
Sequence: K |
Post-translational modification
Carbamylation allows a single lysine to coordinate two nickel ions.
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.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 136-575 | Urease | ||||
Sequence: GGIDTHVHLLGPGALEEALAAGITTVGGGGTGPAEGSKATTCTPGPANLMTIHRGLDAVPLNILLYGKGNTSSLEACREQIMAGAAGLKVHEDWGATPAAIDTALRAAEELGIQVALHADSLNEAGFVQDTLAAIGGRGIHIFHSEGAGGGHAPDIITVASHPNVLPASTNPTLPLTVNTVDEHLDMLMVCHHLNPRIPEDLAFAESRIRGTTMMAEDILHDMGALSITSSDAQAMGRIGETITRTWQVAHAMKALRGRTAEDEAAPADNARARRYVAKYTINPAIAHGIDDEVGSVTPGKLADLVLWSPAFFAVRPDAVIKGGGIVLAPTGDPNASLPTPQPVLMRRQLAGWGPSAADLATTFVAPAALEDGLRDRLGLRRRLTPVKDTRGIGKVDMVLNAATPRIDVDSETFQVSIDGEPVPHRPARRLPLTQRYHLF |
Sequence similarities
Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length575
- Mass (Da)60,070
- Last updated2017-04-12 v1
- ChecksumF482B169A01CCA79