P38628 · AGM1_YEAST
- ProteinPhosphoacetylglucosamine mutase
- GenePCM1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids557 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 (PubMed:8174553).
Also has phosphoglucomutase activity (PubMed:8119301).
Also has phosphoglucomutase activity (PubMed:8119301).
Miscellaneous
Present with 14700 molecules/cell in log phase SD medium.
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 | 298 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 300 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 302 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 395-397 | substrate | ||||
Sequence: EAN | ||||||
Binding site | 522-526 | substrate | ||||
Sequence: RASGT | ||||||
Binding site | 531 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphoacetylglucosamine mutase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | cell wall organization | |
Biological Process | fungal-type cell wall chitin biosynthetic process | |
Biological Process | UDP-N-acetylglucosamine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoacetylglucosamine mutase
- EC number
- Short namesPAGM
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP38628
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Results in undivided strings of cells and growth arrest after approximately 5 division cycles.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 21 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000148019 | 1-557 | Phosphoacetylglucosamine mutase | |||
Sequence: MKVDYEQLCKLYDDTCRTKNVQFSYGTAGFRTLAKNLDTVMFSTGILAVLRSLKLQGQYVGVMITASHNPYQDNGVKIVEPDGSMLLATWEPYAMQLANAASFATNFEEFRVELAKLIEHEKIDLNTTVVPHIVVGRDSRESSPYLLRCLTSSMASVFHAQVLDLGCVTTPQLHYITDLSNRRKLEGDTAPVATEQDYYSFFIGAFNELFATYQLEKRLSVPKLFIDTANGIGGPQLKKLLASEDWDVPAEQVEVINDRSDVPELLNFECGADYVKTNQRLPKGLSPSSFDSLYCSFDGDADRVVFYYVDSGSKFHLLDGDKISTLFAKFLSKQLELAHLEHSLKIGVVQTAYANGSSTAYIKNTLHCPVSCTKTGVKHLHHEAATQYDIGIYFEANGHGTIIFSEKFHRTIKSELSKSKLNGDTLALRTLKCFSELINQTVGDAISDMLAVLATLAILKMSPMDWDEEYTDLPNKLVKCIVPDRSIFQTTDQERKLLNPVGLQDKIDLVVAKYPMGRSFVRASGTEDAVRVYAECKDSSKLGQFCDEVVEHVKASA | ||||||
Modified residue | 67 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Length557
- Mass (Da)62,067
- Last updated1995-02-01 v2
- Checksum76F17D47D07C920A
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 15 | in Ref. 1; CAA53452 | ||||
Sequence: T → M | ||||||
Sequence conflict | 196 | in Ref. 1; CAA53452 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 406 | in Ref. 1; CAA53452 | ||||
Sequence: E → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X75816 EMBL· GenBank· DDBJ | CAA53452.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U18795 EMBL· GenBank· DDBJ | AAB65029.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006939 EMBL· GenBank· DDBJ | DAA07596.1 EMBL· GenBank· DDBJ | Genomic DNA |