A0A2S8JYT1 · A0A2S8JYT1_ECOLX
- ProteinAllantoinase
- GeneallB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids453 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.
Catalytic activity
- (S)-allantoin + H2O = allantoate + H+
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Pathway
Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 59 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 61 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 146 | Zn2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 146 | Zn2+ 2 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 186 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 242 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 315 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | allantoinase activity | |
Molecular Function | cobalt ion binding | |
Molecular Function | zinc ion binding | |
Biological Process | allantoin catabolic process | |
Biological Process | purine nucleobase catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAllantoinase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A2S8JYT1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 146 | N6-carboxylysine | ||||
Sequence: K |
Post-translational modification
Carboxylation allows a single lysine to coordinate two zinc ions.
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 50-431 | Amidohydrolase-related | ||||
Sequence: VVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDALGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEKIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDV |
Sequence similarities
Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length453
- Mass (Da)49,530
- Last updated2018-07-18 v1
- Checksum3099386081CA3C00