F1RQM2 · AGM1_PIG

  • Protein
    Phosphoacetylglucosamine mutase
  • Gene
    PGM3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Activity regulation

Inhibited by Mn2+, Cd2+, Zn2+, Cu2+ and Be2+.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.29 mMD-glucosamine 1-phosphate
0.39 mMD-glucose 1-phosphate
0.018 mMfructose 1,6-diphosphate
0.016 mMgalactose 1,6-diphosphate
0.005 mMmannose 1,6-diphosphate
0.002 mMglucose 1,6-diphosphate
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
39.4 μmol/min/mgfor D-glucosamine 1-phosphate
28.9 μmol/min/mgfor D-glucose 1-phosphate
10.1 μmol/min/mgfor fructose 1,6-diphosphate
14.3 μmol/min/mgfor galactose 1,6-diphosphate
26.7 μmol/min/mgfor mannose 1,6-diphosphate
34.4 μmol/min/mgfor glucose 1,6-diphosphate

pH Dependence

Optimum pH is 7-7.5.

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 site64Phosphoserine intermediate
Binding site64Mg2+ (UniProtKB | ChEBI); via phosphate group
Binding site276Mg2+ (UniProtKB | ChEBI)
Binding site278Mg2+ (UniProtKB | ChEBI)
Binding site280Mg2+ (UniProtKB | ChEBI)
Binding site370-372substrate
Binding site496-500substrate
Binding site505substrate

GO annotations

AspectTerm
Molecular Functionmagnesium ion binding
Molecular Functionphosphoacetylglucosamine mutase activity
Biological Processcarbohydrate metabolic process
Biological Processhemopoiesis
Biological ProcessUDP-N-acetylglucosamine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoacetylglucosamine mutase
  • EC number
  • Short names
    PAGM
    ; PGlcNAc mutase
  • Alternative names
    • Acetylglucosamine phosphomutase
    • N-acetylglucosamine-phosphate mutase
    • Phosphoglucomutase-3
      (PGM 3
      )

Gene names

    • Name
      PGM3
    • Synonyms
      AGM1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus

Accessions

  • Primary accession
    F1RQM2

Proteomes

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00004312961-542Phosphoacetylglucosamine mutase
Modified residue62Phosphothreonine
Modified residue64Phosphoserine

Keywords

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the phosphohexose mutase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    542
  • Mass (Da)
    59,474
  • Last updated
    2012-07-11 v2
  • Checksum
    A5C7A8492751E150
MDLDAITKHSASHAKPDGLILQYGTAGFRTKADRLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEDDNGVKLVDPLGEMLAPSWEEHATHLANAEEQDLARALVAISEEAAVNLHQDAFVVIGRDTRPSSEKLSESVIDGVTVLGGQFHDYGLLTTPQLHYMVCCRNTGGQYGEATIDGYYHKLSTAFVELSKQASCSGDDHRTLKVDCANGIGALKLKEMKHYLPQGLSVQLFNDGTKGKLNHFCGADFVKSHQKPPEGIEMKANERCCSFDGDADRIIYYYCDVDGHFHLIDGDKIATLISSFLKELLLEIGESLTVGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDLGVYFEANGHGTVLFSKAAEAKIRQLAKELEDKKGKAAKMLENVIDLFNQATGDAISDMLVIEAILALKGLTIQQWDALYTDLPNRQLKVKVADRQVISTTDAERQVVKPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQENADSLAYEVSLAVFQQAGGVGERPQPGF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AEMK01179872
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CU463150
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
GACC01000082
EMBL· GenBank· DDBJ
JAA53725.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp