A0A2R6QNW3 · A0A2R6QNW3_ACTCC
- ProteinPhosphoacetylglucosamine mutase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids535 (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 | 274 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 365-367 | substrate | ||||
Sequence: EAN | ||||||
Binding site | 496-500 | substrate | ||||
Sequence: RPSGT | ||||||
Binding site | 505 | 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
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > Ericales > Actinidiaceae > Actinidia
Accessions
- Primary accessionA0A2R6QNW3
Proteomes
Genome annotation databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 56-90 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: TQSVIGLMITASHNKISDNGVKIADPSGGMLSQDW | ||||||
Domain | 124-177 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: AQSAEISLGRDTRPSGESLLESAKQGINSIAGAVAVDMGILTTPQLHWMVRARN | ||||||
Domain | 283-435 | Phosphoacetylglucosamine mutase AMG1 | ||||
Sequence: DGDKILSLFALFIEEQLNTLNKRDGDTENKCYRPTLGVVQTAYANGASTDYLKHSGLEVVFTKTGVKYLHQKAAEYDIGIYFEANGHGTILFSEGFLHWLDGRRSELALTSKGSGQQKAALRLLAVSKLINQAVGDALSGLLLVEAILQHMGW | ||||||
Domain | 455-525 | Alpha-D-phosphohexomutase C-terminal | ||||
Sequence: KVVDRTAIVTENAETVVVSPLGIQEAINAETAKYPRGRCFIRPSGTEDVVRVYAEATTEEAAVNLANAVAQ |
Sequence similarities
Belongs to the phosphohexose mutase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length535
- Mass (Da)57,985
- Last updated2018-06-20 v1
- ChecksumDC42C161AF38EC45
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NKQK01000014 EMBL· GenBank· DDBJ | PSS11611.1 EMBL· GenBank· DDBJ | Genomic DNA |