A0A0L0RY62 · A0A0L0RY62_ALLM3
- ProteinPhosphoacetylglucosamine mutase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids537 (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 | 67 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 67 | Mg2+ (UniProtKB | ChEBI); via phosphate group | ||||
Sequence: S | ||||||
Binding site | 275 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 277 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 279 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 369-371 | substrate | ||||
Sequence: EAN | ||||||
Binding site | 491-495 | substrate | ||||
Sequence: RPSGT | ||||||
Binding site | 500 | 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
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Blastocladiomycota > Blastocladiomycetes > Blastocladiales > Blastocladiaceae > Allomyces
Accessions
- Primary accessionA0A0L0RY62
Proteomes
Organism-specific databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 60-89 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: IGVMVTASHNPVRDNGVKLVDPMGEMLKQS | ||||||
Domain | 102-174 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: THEEVADLYFSIAQECEIDLDQSASVVVGRDTRPSGEALVASLIDGLTASGAIVTDLGLKTTPQLHFVTRCLN | ||||||
Domain | 191-282 | Phosphoacetylglucosamine mutase AMG1 | ||||
Sequence: SDAYKTLVAGLEPLKITVDCAHGVGAPKLRDLTTYLGDALDVTVVNGDVEHGILNYHVGADFVKVNVKQPEGFDLAPNGIYCSFDGDADRIV | ||||||
Domain | 296-430 | Phosphoacetylglucosamine mutase AMG1 | ||||
Sequence: DGDRITALVGAFIIETVRQAGLDLQVGVVQTAYANGNSTHYLRDSLQVPVAFTQTGVKHLHHKAEEYDIGVYFEANGHGTVIFSTAARNTIRNATHGDAKALHILRSLINVINETVGDAISDMLVVLGVLAHRQW | ||||||
Domain | 464-519 | Alpha-D-phosphohexomutase C-terminal | ||||
Sequence: TQLEEPADLQARIDAEVAKVSRGRSFVRPSGTEDVVRVYAEAETREECDTLAYTVA |
Sequence similarities
Belongs to the phosphohexose mutase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length537
- Mass (Da)57,925
- Last updated2015-11-11 v1
- ChecksumDE3B844D020FF0EC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GG745328 EMBL· GenBank· DDBJ | KNE55019.1 EMBL· GenBank· DDBJ | Genomic DNA |