Q5RBM6 · BUP1_PONAB
- ProteinBeta-ureidopropionase
- GeneUPB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids384 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Catalyzes a late step in pyrimidine degradation. Converts N-carbamoyl-beta-alanine (3-ureidopropanoate) into beta-alanine, ammonia and carbon dioxide. Likewise, converts N-carbamoyl-beta-aminoisobutyrate (3-ureidoisobutyrate) into beta-aminoisobutyrate, ammonia and carbon dioxide.
Catalytic activity
- 3-(carbamoylamino)propanoate + 2 H+ + H2O = beta-alanine + CO2 + NH4+
Pathway
Amino-acid biosynthesis; beta-alanine biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 119 | Proton acceptor | ||||
Sequence: E | ||||||
Active site | 196 | Proton donor | ||||
Sequence: K | ||||||
Active site | 233 | Nucleophile | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | beta-ureidopropionase activity | |
Biological Process | beta-alanine biosynthetic process via 3-ureidopropionate | |
Biological Process | protein homooligomerization | |
Biological Process | pyrimidine nucleoside catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBeta-ureidopropionase
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pongo
Accessions
- Primary accessionQ5RBM6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000204053 | 1-384 | Beta-ureidopropionase | |||
Sequence: MAGAEWKSLEECLEKHLPLPDLQEVKRVLYGKELRKLDLPREAFEAASREDFELQGYAFEAAEEQLRRPRIVHVGLVQNRIPLPANAPVAEQVSALHRRIKAIVEVAAMCGVNIICFQEAWTMPFAFCTREKLPWTEFAESAEDGPTTRFCQKLAKNHDMVVVSPILERDSEHGDVLWNTAVVISNSGAVLGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFNPSATIGALSESLWSIEARNAAIANHCFTCAINRVGTEHFPNEFTSGDGKKAHQDFGYFYGSSYVAAPDGSRTPGLSRSQDGLLVAKLDLNLCQQVNDVWNFKMTGRYEMYARELAEAVKSNYSPTIVKE | ||||||
Modified residue | 378 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Subunit
Homodimer, homotetramer, homooctamer; can also form higher homooligomers.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 72-344 | CN hydrolase | ||||
Sequence: VHVGLVQNRIPLPANAPVAEQVSALHRRIKAIVEVAAMCGVNIICFQEAWTMPFAFCTREKLPWTEFAESAEDGPTTRFCQKLAKNHDMVVVSPILERDSEHGDVLWNTAVVISNSGAVLGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFNPSATIGALSESLWSIEARNAAIANHCFTCAINRVGTEHFPNEFTSGDGKKAHQDFGYFYGSSYVAAPDGSRTPGLSRSQDGLLVAKLDL |
Sequence similarities
Belongs to the carbon-nitrogen hydrolase superfamily. BUP family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length384
- Mass (Da)43,098
- Last updated2004-12-21 v1
- Checksum8F7B1BC8E25077BA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR858612 EMBL· GenBank· DDBJ | CAH90834.1 EMBL· GenBank· DDBJ | mRNA |