A0A562CWR7 · A0A562CWR7_9GAMM
- ProteinBeta-hexosaminidase
- GenenagZ
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids332 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic activity
Pathway
Cell wall biogenesis; peptidoglycan recycling.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 60 | substrate | ||||
Sequence: D | ||||||
Binding site | 68 | substrate | ||||
Sequence: R | ||||||
Binding site | 133 | substrate | ||||
Sequence: R | ||||||
Binding site | 163-164 | substrate | ||||
Sequence: KH | ||||||
Site | 174 | Important for catalytic activity | ||||
Sequence: D | ||||||
Active site | 176 | Proton donor/acceptor | ||||
Sequence: H | ||||||
Active site | 247 | Nucleophile | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | beta-N-acetylhexosaminidase activity | |
Molecular Function | N-acetyl-beta-D-galactosaminidase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | cell division | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | peptidoglycan turnover | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBeta-hexosaminidase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Lysobacteraceae > Pseudoxanthomonas
Accessions
- Primary accessionA0A562CWR7
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-288 | Glycoside hydrolase family 3 N-terminal | ||||
Sequence: ELTAQERDWLQHDAVAGVILFKRNFASRAQVAELAAAIREAAPRPQLVCVDQEGGRVQRFREGYSDLPPLQRIGELYARDREAALALAEEHAWLMASEIRASGVDLSFAPVADLGRGNLAIGDRAFGPDPQAVAELVRAYVRGMHSVGMAATLKHFPGHGTVLEDTHVDHAVDPRPLQALRGEDLVPFVAGIEAGADAVMMAHVQYPAIAPDPAGYSPFWIGQFLRGELGFRGVVFSDDIGMAAAHAAGGVRARVLAHLDAGCDVVLVCHPELVAESLQ |
Sequence similarities
Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length332
- Mass (Da)35,189
- Last updated2019-10-16 v1
- Checksum2ACE9AB65C1509E8