Q2VA41 · Q2VA41_CHLRE

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.

Catalytic activity

Cofactor

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

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother 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

Protein family/group databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      PHOB

Organism names

Accessions

  • Primary accession
    Q2VA41

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue849N6-(pyridoxal phosphate)lysine

Proteomic databases

Expression

Gene expression databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region32-58Disordered

Sequence similarities

Belongs to the glycogen phosphorylase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,010
  • Mass (Da)
    114,076
  • Last updated
    2006-01-10 v1
  • Checksum
    6A0B4BD50B1E25DD
MQLASRALAASAAALSAPRAAKCAVPAPVAVSASRSKAVAPTRRSQGPGRQVSVKVAAPESPASSGEVIVNFDNTTDSGYTVISVQANNKPGLLTSITALFRDLGVDVGKAVVEGDEDRINDKFYVRSLSGGKLSEDKAADCVKALDVLLRSKPTGTEATRPKFENTAATGGTGKARLYTLMDTYMKNDVLSIQEDIVNHVEYTLARSRVNFDNFEAYQATSFSLRDRLIERWNDTQTWFKEKDPKRVYYLSMEFLMGRSLLNTLYNLDIKESYQEALAELGYDLETLADLERDAALGNGGLGRLAACFLDSMATLNLPAWGYGIRYQYGMFRQTIQNGFQHEQPDYWLTFGNPWEIERLIVSYPIKFYGHVSVVNEDGRQLFRWNAGETVTAVAYDNPIPGFGTRNCINLRLWAAKPSKEFDLEAFNTGDYVAAILSKQRAETLSSVLYPDDRTYEGKELRLKQQHFFVSATIQDCVRRYRDAHPNDWEQFPEKVAFQLNDTHPTIAVAELMRVLMDDHKLGWTKSWDICNKVFAFTNHTVLPEALERWPVALIEKLLPRHMQIIYDINWRFLQTVRNKFGDDWERISRMSVIEEQPNGEKMVRMAFMAVVASHTVNGVAAIHSEIIKETIFKDFYELWPNKFQNKTNGVTQRRWLAFCNPPLRQLITKKLGNDDWTLHLDNLRELRKYANDPEFQTEWRGVKSEAKKKAAALIHRLTGVRVSTDAMFDIQIKRIHEYKRQLLNVLGIIYRYDQIKKMTPQQRKSVVPRVCVIGGKAAPGYEMAKRIIKLICAVGDKINQDPDMGDLLKLVFLPDYNVSSAEVIIPATELSQHISTAGTEASGTSNMKFTMNGSLIIGTLDGANVEIAEEIGDENIFIFGAKAHEVARLRAERRNLHVDERFNHVVNMIRTGHFGWEDYFGPVVDAITTGGDYYLVANDFPGYLETQFRADEVYKNQTEWTRMSIMATAGGGKFSTDRTIAEYARDIWHAEPCQVPQPEAKSKSKPASS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ279077
EMBL· GenBank· DDBJ
ABB88567.1
EMBL· GenBank· DDBJ
mRNA
DQ279078
EMBL· GenBank· DDBJ
ABB88568.1
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.
FeedbackHelp