A0A1J9RE54 · A0A1J9RE54_9PEZI

  • Protein
    Phosphoacetylglucosamine mutase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site63Phosphoserine intermediate
Binding site63Mg2+ (UniProtKB | ChEBI); via phosphate group
Binding site287Mg2+ (UniProtKB | ChEBI)
Binding site289Mg2+ (UniProtKB | ChEBI)
Binding site291Mg2+ (UniProtKB | ChEBI)
Binding site383-385substrate
Binding site508-512substrate
Binding site517substrate

GO annotations

AspectTerm
Molecular Functionmagnesium ion binding
Molecular Functionphosphoacetylglucosamine mutase activity
Biological Processcarbohydrate metabolic 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

Gene names

    • ORF names
      BKCO1_2000287

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CBS 112549
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetes incertae sedis > Botryosphaeriales > Botryosphaeriaceae > Diplodia

Accessions

  • Primary accession
    A0A1J9RE54

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain54-89Alpha-D-phosphohexomutase alpha/beta/alpha
Domain95-175Alpha-D-phosphohexomutase alpha/beta/alpha
Domain181-294Phosphoacetylglucosamine mutase AMG1
Domain308-447Phosphoacetylglucosamine mutase AMG1
Domain463-536Alpha-D-phosphohexomutase C-terminal

Sequence similarities

Belongs to the phosphohexose mutase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    545
  • Mass (Da)
    59,185
  • Last updated
    2017-02-15 v1
  • Checksum
    0A9430DBDB7AE6A7
MDQKILEASAKHPQPGKVFQYGTAGFRMKADLLDSVVYRVGLLAALRSRKLNGQTIGVMITASHNPPEDNGVKLVDPMGEMLESSWEAHATVLANAETDEKLVEAYNKLAAELKVNQAAPAKVIFARDTRASGSRLVGCLVDALEAAGAEYTDHKFLTTPQLHYLVRCVNTKGTVHEYGEASEKGYYKKIGAALKKALKHRQIPEDAPEDKGVVVDCANGVGGPKLRELIKYLPGPEEKGIKIQVVNDDVHKPENLNSQCGADYVKTGQRAPPQSKAGPLERSASLDGDADRIVYYFNDKDGKFNLLDGDRIATLAASFIGDLSRHAGLGEQLKVGVVQTAYANGASTKYITSGLNLPVVCTPTGVKHLHHAALRFDVGVYFEANGHGTIVFSPAALKTIEKHEPQSPAQHEALETLQALTDLINQTVGDALSDLLVVEVILAHKKWGPAEWLHTYNDLPNRLVRVEVKDRNIFQAVDAERKLESPAGIQDEIDKLVGKYKQGRSFARASGTEDAVRVYAEAETRTEADDLAQKVASLVKQFGSA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MNUE01000002
EMBL· GenBank· DDBJ
OJD39790.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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