Q9VTZ4 · Q9VTZ4_DROME
- ProteinPhosphoacetylglucosamine mutase
- Genenst
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids549 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation.
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 | 68 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 68 | Mg2+ (UniProtKB | ChEBI); via phosphate group | ||||
Sequence: S | ||||||
Binding site | 283 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 285 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 287 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 377-379 | substrate | ||||
Sequence: EAN | ||||||
Binding site | 498-502 | substrate | ||||
Sequence: RPSGT | ||||||
Binding site | 507 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphoacetylglucosamine mutase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | mesodermal cell fate commitment | |
Biological Process | positive regulation of fibroblast growth factor receptor signaling pathway | |
Biological Process | trachea development | |
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 > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9VTZ4
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 60-93 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: VIGVMITASHNPEPDNGVKLVDPKGEMLEASWEA | ||||||
Domain | 108-175 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: QQVAKIIKDNNIDVTTSSQVFVGMDNRYHSPRLLKAVADGVIALKGNVKEYGIVTTPMLHYFVVAANT | ||||||
Domain | 183-290 | Phosphoacetylglucosamine mutase AMG1 | ||||
Sequence: TEEGYYDKLIKAFELLRNGRLENGNYRNSIIYDGANGVGARKMLQFIKRMKGTLNVTVINQGIGVGKINEDCGADYVKVQQSPPKSMPEDVKPYTRCVSVDGDADRVV | ||||||
Domain | 304-437 | Phosphoacetylglucosamine mutase AMG1 | ||||
Sequence: DGDRIATLIAGYLMELVTQSEISLRLGLVQTAYANGASTDYIVDQLKFPVSCVPTGVKHLHHKALEYDIGVYFEANGHGTIVFSDNAKATIAQVAQTKESAKTLLLLIDLINETVGDAISDMLLVETILNHKGW | ||||||
Domain | 475-524 | Alpha-D-phosphohexomutase C-terminal | ||||
Sequence: KPEGLQTEINQVVAKYKRGRSFVRPSGTEDVVRVYAEAATKEDTDNLAYE |
Sequence similarities
Belongs to the phosphohexose mutase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length549
- Mass (Da)60,581
- Last updated2000-05-01 v1
- Checksum62D2F691AC423465
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE014296 EMBL· GenBank· DDBJ | AAF49901.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY069309 EMBL· GenBank· DDBJ | AAL39454.1 EMBL· GenBank· DDBJ | mRNA |