Q8GXV5 · UGHY_ARATH
- Protein(S)-ureidoglycine aminohydrolase
- GeneUGLYAH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids298 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the catabolism of purine nucleotides. Can use (S)-2-ureidoglycine as substrate, but not allantoate. The sequential activity of AAH, UGLYAH and UAH allows a complete purine breakdown without the intermediate generation of urea.
Catalytic activity
- (S)-2-ureidoglycine + H2O = (S)-ureidoglycolate + NH4+
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.77 mM | (S)-2-ureidoglycine |
kcat is 761 sec-1 for (S)-2-ureidoglycine.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 235 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 235 | substrate | ||||
Sequence: E | ||||||
Binding site | 237 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 241 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 275 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 275 | substrate | ||||
Sequence: Q | ||||||
Binding site | 287 | substrate | ||||
Sequence: Y | ||||||
Binding site | 291 | substrate | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Molecular Function | DNA-binding transcription factor activity | |
Molecular Function | metal ion binding | |
Molecular Function | ureidoglycine aminohydrolase activity | |
Biological Process | allantoin catabolic process | |
Biological Process | purine nucleobase catabolic process | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | ureide catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name(S)-ureidoglycine aminohydrolase
- EC number
- Short namesAtUGLYAH
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8GXV5
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 221 | Decreased activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 235 | Loss of manganese binding and loss of activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 235 | No effect on manganese binding, but loss of activity. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 237 | Loss of activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 241 | Loss of activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 252 | No effect on the affinity for the substrate, but decreased activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 275 | Loss of activity. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 287 | Loss of activity. | ||||
Sequence: Y → A or F | ||||||
Mutagenesis | 291 | Loss of activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 291 | Increased affinity for the substrate, but decreased activity. | ||||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 65 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MRSLYLIVFIVISLVKASKS | ||||||
Chain | PRO_0000423444 | 21-298 | (S)-ureidoglycine aminohydrolase | |||
Sequence: DDGFCSAPSIVESDEKTNPIYWKATNPTLSPSHLQDLPGFTRSVYKRDHALITPESHVYSPLPDWTNTLGAYLITPATGSHFVMYLAKMKEMSSSGLPPQDIERLIFVVEGAVTLTNTSSSSKKLTVDSYAYLPPNFHHSLDCVESATLVVFERRYEYLGSHTTELIVGSTDKQPLLETPGEVFELRKLLPMSVAYDFNIHTMDFQPGEFLNVKEVHYNQHGLLLLEGQGIYRLGDNWYPVQAGDVIWMAPFVPQWYAALGKTRSRYLLYKDVNRNPL |
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 222-288 | Cupin type-2 | ||||
Sequence: TMDFQPGEFLNVKEVHYNQHGLLLLEGQGIYRLGDNWYPVQAGDVIWMAPFVPQWYAALGKTRSRYL |
Sequence similarities
Belongs to the UGHY family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length298
- Mass (Da)33,673
- Last updated2003-03-01 v1
- Checksum50CED7DBA1C40A99
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 138 | in Ref. 6; BAD44550 | ||||
Sequence: T → S | ||||||
Sequence conflict | 224 | in Ref. 6; BAD43635 | ||||
Sequence: D → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GQ303359 EMBL· GenBank· DDBJ | ADH04164.1 EMBL· GenBank· DDBJ | mRNA | ||
Z97342 EMBL· GenBank· DDBJ | CAB10485.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161545 EMBL· GenBank· DDBJ | CAB80976.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE83843.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK118019 EMBL· GenBank· DDBJ | BAC42652.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176787 EMBL· GenBank· DDBJ | BAD44550.1 EMBL· GenBank· DDBJ | mRNA | ||
AK175872 EMBL· GenBank· DDBJ | BAD43635.1 EMBL· GenBank· DDBJ | mRNA |