A0A0D6I812 · A0A0D6I812_SALTM

  • Protein
    Alpha-1,4 glucan phosphorylase
  • Gene
    malP_2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

Function

function

Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

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
Molecular Functionglycogen phosphorylase activity
Molecular Functionlinear malto-oligosaccharide phosphorylase activity
Molecular Functionpyridoxal phosphate binding
Molecular FunctionSHG alpha-glucan phosphorylase activity
Biological Processcarbohydrate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-1,4 glucan phosphorylase
  • EC number

Gene names

    • Name
      malP_2
    • ORF names
      AAB27_04095
      , AU613_00860
      , AVC05_05565
      , B1P38_08895
      , CE70_05985
      , CFF59_07650
      , CVR97_05625
      , DD95_06320
      , DMO92_12640
      , DPF41_07460
      , DPS76_12155
      , DRM14_11880
      , DU071_02150
      , E0935_01465
      , EER35_04655
      , F3R12_10560
      , G0J40_08680
      , GB466_14350
      , SE14_03748

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • 29290
    • 43916
    • 86846
    • 231108
    • 265852
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella

Accessions

  • Primary accession
    A0A0D6I812
  • Secondary accessions
    • A0A0F7JDZ3
    • A0A0M2J527

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue662N6-(pyridoxal phosphate)lysine

Family & Domains

Sequence similarities

Belongs to the glycogen phosphorylase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    815
  • Mass (Da)
    93,343
  • Last updated
    2015-05-27 v1
  • Checksum
    4464A9CBB044F1C2
MNAPFTYASPTLSVEALKHSIAYKLMFTIGKDPVIANKHEWLNATLFAVRDRLVERWLRSNRAQLSQETRQVYYLSMEFLIGRTLSNALLSLGIYDDVKGALEAMGLDLEELIDEENDPGLGNGGLGRLAACFLDSLATLGLPGRGYGIRYDYGMFKQNIVDGRQKESPDYWLEYGNPWEFKRHNTRYKVLFGGRIQQEGKKARWIETEEILAVAYDQIIPGYDTDATNTLRLWNAQASSEINLGKFNQGDYFAAVEDKNHSENVSRVLYPDDSTYSGRELRLRQEYFLVSATVQDILHRHYQLHKTYENLADKIAIHLNDTHPVLSIPELMRLLIDEHKFSWDDAFEVCCQVFSYTNHTLMSEALETWPVDMLGKILPRHLQIIFEINDYFLKTVQEQYPNDTSLLGRASIIDESNGRRVRMAWLAVVVSHKVNGVSELHSNLMVQSLFADFAKIFPTRFCNVTNGVTPRRWLALANPPLSDVLDENIGRTWRTDLSQLSELKQHCDYPLVNHAVRQAKLENKKRLAVVIAQQLNVVVNPKALFDVQIKRIHEYKRQLMNVLHVITRYNRIKENPEADWVPRVNIFAGKAASAYYMAKHIIHLINDVAKVINNDPQIGDKLKVVFIPNYSVSLAQVIIPAADLSEQISLAGTEASGTSNMKFALNGALTIGTLDGANVEMQEHIGEENIFIFGNTAEEVEALRRQGYKPRDYYEKDEELHQVLTQIGSGVFNPEEPGRYRDLVDSLINFGDHYQVLADYRSYVDCQDKVDELYRRPEEWTTKAMLNIANMGYFSSDRTIKEYAENIWHIDPVRL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP011428
EMBL· GenBank· DDBJ
AKH09164.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHDPU010000009
EMBL· GenBank· DDBJ
EBU9272898.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHIDF010000006
EMBL· GenBank· DDBJ
EBW3627930.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHIPE010000011
EMBL· GenBank· DDBJ
EBW5463193.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHNIA010000002
EMBL· GenBank· DDBJ
EBY1700767.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHRYM010000003
EMBL· GenBank· DDBJ
EBZ6920280.1
EMBL· GenBank· DDBJ
Genomic DNA
AAIGQE010000003
EMBL· GenBank· DDBJ
ECE0294748.1
EMBL· GenBank· DDBJ
Genomic DNA
AAIKGB010000001
EMBL· GenBank· DDBJ
ECF1541925.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKRET010000007
EMBL· GenBank· DDBJ
ECU8353703.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKUOT010000005
EMBL· GenBank· DDBJ
ECV8760070.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKVET010000005
EMBL· GenBank· DDBJ
ECW0640286.1
EMBL· GenBank· DDBJ
Genomic DNA
AALDNI010000008
EMBL· GenBank· DDBJ
ECY5340711.1
EMBL· GenBank· DDBJ
Genomic DNA
AAMLUT010000005
EMBL· GenBank· DDBJ
EDI6665133.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAFPQ010000010
EMBL· GenBank· DDBJ
HAB0971733.1
EMBL· GenBank· DDBJ
Genomic DNA
DAANAV010000004
EMBL· GenBank· DDBJ
HAC9070190.1
EMBL· GenBank· DDBJ
Genomic DNA
JYVU01000013
EMBL· GenBank· DDBJ
KTZ14029.1
EMBL· GenBank· DDBJ
Genomic DNA
RSUA01000001
EMBL· GenBank· DDBJ
MIT47449.1
EMBL· GenBank· DDBJ
Genomic DNA
RVDJ01000010
EMBL· GenBank· DDBJ
MLP86011.1
EMBL· GenBank· DDBJ
Genomic DNA
PHGX01000020
EMBL· GenBank· DDBJ
PJH62883.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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