A0A1J9RE54 · A0A1J9RE54_9PEZI
- ProteinPhosphoacetylglucosamine mutase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids545 (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 | 63 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 63 | Mg2+ (UniProtKB | ChEBI); via phosphate group | ||||
Sequence: S | ||||||
Binding site | 287 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 289 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 291 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 383-385 | substrate | ||||
Sequence: EAN | ||||||
Binding site | 508-512 | substrate | ||||
Sequence: RASGT | ||||||
Binding site | 517 | substrate | ||||
Sequence: R |
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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetes incertae sedis > Botryosphaeriales > Botryosphaeriaceae > Diplodia
Accessions
- Primary accessionA0A1J9RE54
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 54-89 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: QTIGVMITASHNPPEDNGVKLVDPMGEMLESSWEAH | ||||||
Domain | 95-175 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: NAETDEKLVEAYNKLAAELKVNQAAPAKVIFARDTRASGSRLVGCLVDALEAAGAEYTDHKFLTTPQLHYLVRCVNTKGTV | ||||||
Domain | 181-294 | Phosphoacetylglucosamine mutase AMG1 | ||||
Sequence: ASEKGYYKKIGAALKKALKHRQIPEDAPEDKGVVVDCANGVGGPKLRELIKYLPGPEEKGIKIQVVNDDVHKPENLNSQCGADYVKTGQRAPPQSKAGPLERSASLDGDADRIV | ||||||
Domain | 308-447 | Phosphoacetylglucosamine mutase AMG1 | ||||
Sequence: DGDRIATLAASFIGDLSRHAGLGEQLKVGVVQTAYANGASTKYITSGLNLPVVCTPTGVKHLHHAALRFDVGVYFEANGHGTIVFSPAALKTIEKHEPQSPAQHEALETLQALTDLINQTVGDALSDLLVVEVILAHKKW | ||||||
Domain | 463-536 | Alpha-D-phosphohexomutase C-terminal | ||||
Sequence: LVRVEVKDRNIFQAVDAERKLESPAGIQDEIDKLVGKYKQGRSFARASGTEDAVRVYAEAETRTEADDLAQKVA |
Sequence similarities
Belongs to the phosphohexose mutase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length545
- Mass (Da)59,185
- Last updated2017-02-15 v1
- Checksum0A9430DBDB7AE6A7
Keywords
- Technical term