P77425 · ALLC_ECOLI
- ProteinAllantoate amidohydrolase
- GeneallC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids411 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the anaerobic nitrogen utilization via the assimilation of allantoin (PubMed:10601204, PubMed:20038185).
Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 (PubMed:20038185).
In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen (PubMed:20038185).
Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 (PubMed:20038185).
In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen (PubMed:20038185).
Catalytic activity
- allantoate + 2 H+ + H2O = (S)-2-ureidoglycine + CO2 + NH4+
Cofactor
Activity regulation
Sulfate could be an allosteric effector of the enzyme that is responsible for stabilizing substrate binding. In addition, this anion effector may act as a counterion during enzyme-mediated catalysis.
pH Dependence
Optimum pH is 8. Less active under acidic conditions.
Pathway
Nitrogen metabolism; (S)-allantoin degradation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 81 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 92 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 127 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 190 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 215 | allantoate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 275 | allantoate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 288 | allantoate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 382 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | allantoate deiminase activity | |
Molecular Function | manganese ion binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | zinc ion binding | |
Biological Process | allantoin assimilation pathway | |
Biological Process | purine nucleobase metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAllantoate amidohydrolase
- EC number
- Short namesAAH
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP77425
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 126 | Loss of amidohydrolase activity. Large movement of the catalytic domain into a closed conformation. | ||||
Sequence: E → A |
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000061957 | 1-411 | Allantoate amidohydrolase | |||
Sequence: MITHFRQAIEETLPWLSSFGADPAGGMTRLLYSPEWLETQQQFKKRMAASGLETRFDEVGNLYGRLNGTEYPQEVVLSGSHIDTVVNGGNLDGQFGALAAWLAIDWLKTQYGAPLRTVEVVAMAEEEGSRFPYVFWGSKNIFGLANPDDVRNICDAKGNSFVDAMKACGFTLPNAPLTPRQDIKAFVELHIEQGCVLESNGQSIGVVNAIVGQRRYTVTLNGESNHAGTTPMGYRRDTVYAFSRICHQSVEKAKRMGDPLVLTFGKVEPRPNTVNVVPGKTTFTIDCRHTDAAVLRDFTQQLENDMRAICDEMDIGIDIDLWMDEEPVPMNKELVATLTELCEREKLNYRVMHSGAGHDAQIFAPRVPTCMIFIPSINGISHNPAERTNITDLAEGVKTLALMLYQLAWQK |
Proteomic databases
Expression
Induction
By glyoxylate and allantoin under anaerobic conditions.
Structure
Sequence
- Sequence statusComplete
- Length411
- Mass (Da)45,694
- Last updated1997-02-01 v1
- ChecksumC55D1EF854A8F513
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U89279 EMBL· GenBank· DDBJ | AAB93857.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U82664 EMBL· GenBank· DDBJ | AAB40268.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73618.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76294.1 EMBL· GenBank· DDBJ | Genomic DNA |