P38628 · AGM1_YEAST

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).

Miscellaneous

Present with 14700 molecules/cell in log phase SD medium.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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.

TypeIDPosition(s)Description
Active site67Phosphoserine intermediate
Binding site67Mg2+ (UniProtKB | ChEBI); via phosphate group
Binding site298Mg2+ (UniProtKB | ChEBI)
Binding site300Mg2+ (UniProtKB | ChEBI)
Binding site302Mg2+ (UniProtKB | ChEBI)
Binding site395-397substrate
Binding site522-526substrate
Binding site531substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionmagnesium ion binding
Molecular Functionphosphoacetylglucosamine mutase activity
Biological Processcarbohydrate metabolic process
Biological Processcell wall organization
Biological Processfungal-type cell wall chitin biosynthetic process
Biological ProcessUDP-N-acetylglucosamine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoacetylglucosamine mutase
  • EC number
  • Short names
    PAGM
  • Alternative names
    • Acetylglucosamine phosphomutase
    • N-acetylglucosamine-phosphate mutase
    • PGM-complementing protein 1

Gene names

    • Name
      PCM1
    • Synonyms
      AGM1
    • Ordered locus names
      YEL058W

Organism names

Accessions

  • Primary accession
    P38628
  • Secondary accessions
    • D3DLJ2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001480191-557Phosphoacetylglucosamine mutase
Modified residue67Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the phosphohexose mutase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    557
  • Mass (Da)
    62,067
  • Last updated
    1995-02-01 v2
  • Checksum
    76F17D47D07C920A
MKVDYEQLCKLYDDTCRTKNVQFSYGTAGFRTLAKNLDTVMFSTGILAVLRSLKLQGQYVGVMITASHNPYQDNGVKIVEPDGSMLLATWEPYAMQLANAASFATNFEEFRVELAKLIEHEKIDLNTTVVPHIVVGRDSRESSPYLLRCLTSSMASVFHAQVLDLGCVTTPQLHYITDLSNRRKLEGDTAPVATEQDYYSFFIGAFNELFATYQLEKRLSVPKLFIDTANGIGGPQLKKLLASEDWDVPAEQVEVINDRSDVPELLNFECGADYVKTNQRLPKGLSPSSFDSLYCSFDGDADRVVFYYVDSGSKFHLLDGDKISTLFAKFLSKQLELAHLEHSLKIGVVQTAYANGSSTAYIKNTLHCPVSCTKTGVKHLHHEAATQYDIGIYFEANGHGTIIFSEKFHRTIKSELSKSKLNGDTLALRTLKCFSELINQTVGDAISDMLAVLATLAILKMSPMDWDEEYTDLPNKLVKCIVPDRSIFQTTDQERKLLNPVGLQDKIDLVVAKYPMGRSFVRASGTEDAVRVYAECKDSSKLGQFCDEVVEHVKASA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict15in Ref. 1; CAA53452
Sequence conflict196in Ref. 1; CAA53452
Sequence conflict406in Ref. 1; CAA53452

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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