A0A1W2GKW9 · A0A1W2GKW9_REIFA
- ProteinUrocanate hydratase
- GenehutU
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids558 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
Catalytic activity
- 4-imidazolone-5-propanoate = trans-urocanate + H2O
Cofactor
Note: Binds 1 NAD+ per subunit.
Pathway
Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 57-58 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GG | ||||||
Binding site | 135 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 181-183 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GMG | ||||||
Binding site | 201 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 206 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 268-272 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QTSAH | ||||||
Binding site | 278-279 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: YV | ||||||
Binding site | 327 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 415 | |||||
Sequence: C | ||||||
Binding site | 497 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | urocanate hydratase activity | |
Biological Process | L-histidine catabolic process to glutamate and formamide | |
Biological Process | L-histidine catabolic process to glutamate and formate |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUrocanate hydratase
- EC number
- Short namesUrocanase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Cytophagia > Cytophagales > Reichenbachiellaceae > Reichenbachiella
Accessions
- Primary accessionA0A1W2GKW9
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-142 | Urocanase N-terminal | ||||
Sequence: KAPTGSQLHAKSWQTESALRMLLNNLDAEVAEDPSELVVYGGTGQAARNVESLQKIIELLLKLENDESLLVQSGKPVGIVRTHAEAPRVLIANSNLVPAWSNWEHFQSLKERGLMMYGQMTAGSWI | ||||||
Domain | 145-353 | Urocanase Rossmann-like | ||||
Sequence: GSQGILQGTYETFVACGEKHFGGSLKGKLVVTAGLGGMGGAQPLAATMAGATFLGADIDPTRIQKRLDTKYIDRMTHSYEEARDWVMEAKAKGENLSVGLVADAGDMLEQLIADGIVPEVLTDQTSAHDPVFGYVPNGMSLEEAVDLRKKDQVKYKDLSLKSMARHVGLMLDLQKKGSKTFDYGNNIREFARQGGEPNAFDFNGFVPEY | ||||||
Domain | 356-549 | Urocanase C-terminal | ||||
Sequence: PLFCEGKGPFRWAALSGDPEDIYVTDQALIEAFPENKHMINWLQEAQKKVSFQGLPCRICWLGMGEREKAGLIFNDLVKTGKVKAPIVIGRDHLDCGSVASPNRETEGMKDGTDAVSDWPLLNLMSNATGGATWISFHHGGGVGMGYSQHAGMVVLADGTERAEKCLKRVLHNDPAMGIFRHHDAGYDKASKFA |
Sequence similarities
Belongs to the urocanase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length558
- Mass (Da)61,350
- Last updated2017-06-07 v1
- Checksum539F35FB1B76E822
Keywords
- Technical term