A0A4Q4STI3 · A0A4Q4STI3_9PLEO
- ProteinN-acetylglucosamine-6-phosphate deacetylase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids432 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate
Cofactor
Note: Binds 1 divalent metal cation per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 155 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 166 | substrate | ||||
Sequence: I | ||||||
Binding site | 227 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 248 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 251-252 | substrate | ||||
Sequence: NA | ||||||
Binding site | 259 | substrate | ||||
Sequence: R | ||||||
Binding site | 287 | substrate | ||||
Sequence: H | ||||||
Active site | 309 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Binding site | 344-346 | substrate | ||||
Sequence: IAG |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | N-acetylgalactosamine-6-phosphate deacetylase activity | |
Molecular Function | N-acetylglucosamine-6-phosphate deacetylase activity | |
Biological Process | N-acetylglucosamine catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-acetylglucosamine-6-phosphate deacetylase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Pleosporomycetidae > Pleosporales > Pleosporineae > Pleosporaceae > Alternaria > Alternaria sect. Alternaria
Accessions
- Primary accessionA0A4Q4STI3
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 67-422 | Amidohydrolase-related | ||||
Sequence: ILSPGLIDTQLNGAYGFDFSVLPDEGTSAYAKGVHRVNRSLVATGVTSYLPTLTSQLPEVYQQTLPFLGPSGAARDASYGSESLGAHCEGPFLSPTKNGIHNALVLREPTNNASDLEACYGSDNLQKPSPIKLITLAPELPGALSSIPHLNSLGIHVSIGHSEATYEEAKSSIKSGARMITHLFNAMRPLHHRNPGIFGLLGTPSLSIQKPYFGIIADGIHLHPTSIKIAWNAHPDGLILVTDAMGLAGMPDGTYDWTNGSRIVKQGPLLTLEENGKIAGSSIQLVDCVSNFLNWTGASVPEALKAVTETPAKMLGLQGIKGTLEEGADADLVVLDLQEDEGGEKKFVVDEVWKFG |
Sequence similarities
Belongs to the metallo-dependent hydrolases superfamily. NagA family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length432
- Mass (Da)46,154
- Last updated2019-07-31 v1
- ChecksumE04B493512954FD6