A0A919LV02 · A0A919LV02_KLEPN

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

Function

function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.

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.

Features

Showing features for active site, binding site.

144550100150200250300350400
Type
IDPosition(s)Description
Active site102Phosphoserine intermediate
Binding site102Mg2+ (UniProtKB | ChEBI); via phosphate group
Binding site241Mg2+ (UniProtKB | ChEBI)
Binding site243Mg2+ (UniProtKB | ChEBI)
Binding site245Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionmagnesium ion binding
Molecular Functionphosphoglucosamine mutase activity
Molecular Functionphosphomannomutase activity
Biological Processcarbohydrate metabolic process
Biological Processpeptidoglycan biosynthetic process
Biological ProcessUDP-N-acetylglucosamine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoglucosamine mutase
  • EC number

Gene names

    • Name
      glmM
    • ORF names
      KPZU09_60590

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Zam_UTH_09
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Klebsiella

Accessions

  • Primary accession
    A0A919LV02

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue102Phosphoserine

Post-translational modification

Activated by phosphorylation.

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-136Alpha-D-phosphohexomutase alpha/beta/alpha
Domain157-254Alpha-D-phosphohexomutase alpha/beta/alpha
Domain258-366Alpha-D-phosphohexomutase alpha/beta/alpha
Domain373-441Alpha-D-phosphohexomutase C-terminal

Sequence similarities

Belongs to the phosphohexose mutase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    445
  • Mass (Da)
    47,933
  • Last updated
    2023-02-22 v1
  • Checksum
    BF5E5A2029FF0DB0
MSNRKYFGTDGIRGRVGDAPITPEFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAIAYLTRAFRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDDVEEAIEAEMEKELTCVDSAELGKASRIVDAAGRYIEFCKGTFPNELSLGTLKVVVDCAHGATYHIAPNVFRELGARVIAMGCEPDGLNINEEVGATDVRALQARVLAEKADLGIAYDGDGDRVIMVDHEGNKVDGDQILYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFARAKVGDRYVLEMLQEKGWRIGAENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLCSGMKMFPQLLVNVRFTEGSGNPLENEHVKAVTAEVEAALGKRGRVLLRKSGTEPLIRVMVEGEHEDQVHEFAHRIAEAVKSV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BNFF01000001
EMBL· GenBank· DDBJ
GHK56323.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
Help