A0A6A7JQJ8 · A0A6A7JQJ8_9BACT

  • 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.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for active site, binding site.

144550100150200250300350400
TypeIDPosition(s)Description
Active site99Phosphoserine intermediate
Binding site99Mg2+ (UniProtKB | ChEBI); via phosphate group
Binding site242Mg2+ (UniProtKB | ChEBI)
Binding site244Mg2+ (UniProtKB | ChEBI)
Binding site246Mg2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
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
      A2J15_007310
      , GC018_02105
      , GC019_01210
      , GC022_00415

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • HV10
    • QLD_2/QLD
    • VIC_4/VIC
    • VIC_5/VIC
  • Taxonomic lineage
    Bacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Campylobacteraceae > Campylobacter

Accessions

  • Primary accession
    A0A6A7JQJ8

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue99Phosphoserine

Post-translational modification

Activated by phosphorylation.

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-133Alpha-D-phosphohexomutase alpha/beta/alpha
Domain158-254Alpha-D-phosphohexomutase alpha/beta/alpha
Domain259-367Alpha-D-phosphohexomutase alpha/beta/alpha

Sequence similarities

Belongs to the phosphohexose mutase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    445
  • Mass (Da)
    49,027
  • Last updated
    2020-06-17 v1
  • Checksum
    2A7037C95B69F352
MKLFGTDGVRGKAGEFLDSFLAMRLAMAAGIYFKDKSITNNILVGKDTRRSGYMIENAIVSGLTSIGYNVIQIGPMPTPAIAFLTEDMRCDAGIMISASHNPYYDNGIKFFDGHGNKLSEDIEKKIEEIYFDDKLIQNSKVKMDEIGQAKRIDDVIGRYIVSIKNSFPKDLTLKSLRVVLDVANGAAYKVAPTVFKELGAEVIVINDTPNGLNINKNCGALHPANLATEVKYLRADVGFAFDGDADRLVVVDEKAQVANGDSLLGVLALYLKEQDKLKSGVVATIMSNGALKEFLNKHNIELNTCNVGDKYVLEKLKANGGNFGGEQSGHIIFSDYAKTGDGLIAALQFSALMLSKKKPASYILGQLKPYPQLLTNLQIAEKKDLDKIKGLKELKQNLENKNINTLFRYSGTENLIRLLLEAKDIRILENEMKHVVEFFKKALNG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP031611
EMBL· GenBank· DDBJ
AXP09454.1
EMBL· GenBank· DDBJ
Genomic DNA
WHMJ01000001
EMBL· GenBank· DDBJ
MPV90664.1
EMBL· GenBank· DDBJ
Genomic DNA
WHMG01000002
EMBL· GenBank· DDBJ
MPV95034.1
EMBL· GenBank· DDBJ
Genomic DNA
WHMF01000003
EMBL· GenBank· DDBJ
MPV97986.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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