A0A0J8E3Z6 · A0A0J8E3Z6_BETVV
- ProteinPhosphoacetylglucosamine mutase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids557 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Interconverts GlcNAc-6-P and GlcNAc-1-P.
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 | 284 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 286 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 288 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 387-389 | substrate | ||||
Sequence: EAN | ||||||
Binding site | 516-520 | substrate | ||||
Sequence: RPSGT | ||||||
Binding site | 525 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal 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
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > Caryophyllales > Chenopodiaceae > Betoideae > Beta
Accessions
- Primary accessionA0A0J8E3Z6
Proteomes
Genome annotation databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 57-89 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: QSVIGLMITASHNKVSDNGVKIADPNGGMLSQQ | ||||||
Domain | 182-291 | Phosphoacetylglucosamine mutase AMG1 | ||||
Sequence: STEHDYFQQLSHSYKCLVELIPNGKDVSKSNDKVVVDGANGVGGDKLEVLKHLCGGLIIEVRNSSKGEGALNEGVGADFVQKEKVVPSGFSPSEIGLRCASLDGDADRLV | ||||||
Domain | 306-455 | Phosphoacetylglucosamine mutase AMG1 | ||||
Sequence: DGDKMLSLFALFIKEQLNVLKDNENETPCPYHPSLGIVQTAYANGASTSYLKNLGLDIFITPTGVKYLHEKASEYDIGIYFEANGHGTILFSDRILSWLEARNSDLSSSSTESQKAVLRLLAVSKLINQAVGDALSGLLLVEAILLHTGW | ||||||
Domain | 486-545 | Alpha-D-phosphohexomutase C-terminal | ||||
Sequence: NAETVVVQPAGIQEAIDSETAKYRHGRCFIRPSGTEDVIRVYAEAASQEEADSLANAVAK |
Sequence similarities
Belongs to the phosphohexose mutase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length557
- Mass (Da)60,405
- Last updated2015-10-14 v1
- Checksum2F6DEA697C54ABE4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KQ090290 EMBL· GenBank· DDBJ | KMS97835.1 EMBL· GenBank· DDBJ | Genomic DNA |