A0A0G4PLG7 · A0A0G4PLG7_PENC3
- ProteinPhosphoacetylglucosamine mutase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids539 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins.
Catalytic activity
- N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 69 | Phosphoserine intermediate | |||
Binding site | 69 | Mg2+ (UniProtKB | ChEBI); via phosphate group | |||
Binding site | 281 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 283 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 285 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 377-379 | substrate | |||
Binding site | 502-506 | substrate | |||
Binding site | 511 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | magnesium ion binding | |
Molecular Function | phosphoacetylglucosamine mutase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | UDP-N-acetylglucosamine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoacetylglucosamine mutase
- EC number
- Short namesPAGM
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium
Accessions
- Primary accessionA0A0G4PLG7
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 63-92 | Alpha-D-phosphohexomutase alpha/beta/alpha | |||
Domain | 123-175 | Alpha-D-phosphohexomutase alpha/beta/alpha | |||
Domain | 187-288 | Phosphoacetylglucosamine mutase AMG1 | |||
Domain | 302-441 | Phosphoacetylglucosamine mutase AMG1 | |||
Domain | 457-531 | Alpha-D-phosphohexomutase C-terminal | |||
Sequence similarities
Belongs to the phosphohexose mutase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length539
- Mass (Da)58,625
- Last updated2015-09-16 v1
- MD5 Checksum76EC2841448E785981B5A32C28B8390C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HG793154 EMBL· GenBank· DDBJ | CRL27214.1 EMBL· GenBank· DDBJ | Genomic DNA |