A0A076EXY7 · A0A076EXY7_RHOOP

Function

function

The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO2 is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.

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
Cellular Componentcytosol
Cellular Componentglycine cleavage complex
Molecular Functionglycine binding
Molecular Functionglycine dehydrogenase (decarboxylating) activity
Molecular Functionpyridoxal phosphate binding
Biological Processglycine decarboxylation via glycine cleavage system

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycine dehydrogenase (decarboxylating)
  • EC number
  • Alternative names
    • Glycine cleavage system P-protein
    • Glycine decarboxylase
    • Glycine dehydrogenase (aminomethyl-transferring)

Gene names

    • Name
      gcvP
    • ORF names
      EP51_27815

Organism names

Accessions

  • Primary accession
    A0A076EXY7

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue717N6-(pyridoxal phosphate)lysine

Interaction

Subunit

The glycine cleavage system is composed of four proteins: P, T, L and H.

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-28Polar residues
Region1-39Disordered
Domain35-460Glycine cleavage system P-protein N-terminal
Domain489-749Glycine cleavage system P-protein N-terminal
Domain786-907Glycine dehydrogenase C-terminal

Sequence similarities

Belongs to the GcvP family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    984
  • Mass (Da)
    104,452
  • Last updated
    2014-10-29 v1
  • Checksum
    6B5BF70AD64E3816
MSGAVRTQRNRSHLVPAETRTATHGVPLTSDFPSRHIGPDADASRRMLGTLGYDTLANLIDSAVPEQIRSSQPLSLPAGRSEQQVLADLRALSERNETRVQMIGLGYSDTVTPAVLRRNILESPAWYTAYTPYQPEISQGRLEALLTFQTVIEDLTALPLAGASLLDEATAVMEAVLLMRRANKPKAATNRVVLDADCLPQTLAVVRGRAKAVGIEVVVADLSGELPDGDMFGVVFQAPGASGAVRDLAPMIAAAQTRGALTTVAADLLSLTILTPPGEQGADIAVGSAQRFGVPLFFGGPHAGYMAVRGGLERMLPGRLVGVSVDVDGKTAYRLALQTREQHIRRDKATSNICTAQALLANVAAMYAAYHGPEGLRAIANRVHAHATTIAGSLRAAGHTIVHDTFFDTVLVRVPAGAETIVALADRDGINLRRVDADHVAIACDECTTDDIVRRVVAVFGAQPTTVAVPELPSALARTSDYLQHGVFHSHRSETAMLRFLRTLSDKDLALDRTMIPLGSCTMKLNSAVEMEPISWPGFASIHPYAPAAQTSGYLELVADLERWLGEITGYDRVSLQPNAGSQGELAGLLAIHGYHESRGELGRNICLIPQSAHGTNAASAVLAGMKVVVVATAENGNIDLGDLRAKIAAHEGAVAAIMLTYPSTHGVYENDVRTVCDLVHEAGGQVYVDGANLNALVGLAQPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPVAVREHLAPFLPGNPLGGDDLGTPVSAANYGSAGILPITWAYLALMGPDGLTSATETAVLAANYVARSLDPHFPVLYTGPSGLVAHECILDLRPVTKATGVTAEDVAKRLIDYGFHAPTLSFPVNGTLMVEPTESEDLAELDRFIEAMVSIRREIDLVGDGVWPLERSPLRQAPHTAEQVTADNWDLPYPRHLAAYPVASLRAAKYWPPVRRIDGVHGDRNLVCSCPAPEAFENTTDIDTSAIAETPEEAFA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-28Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP008947
EMBL· GenBank· DDBJ
AII08224.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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