P25855 · GCSH1_ARATH

Function

function

The glycine decarboxylase (GDC) or glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.

Cofactor

(R)-lipoate (UniProtKB | Rhea| CHEBI:83088 )
Note: Binds 1 lipoyl cofactor covalently.

Activity regulation

Inhibited by harpin, S-nitrosoglutathione (GSNO), nitric oxide, N-ethylmaleimide and 5,5'-dithiobis-(2-nitrobenzoic acid).

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
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum
Cellular Componentglycine cleavage complex
Cellular Componentmitochondrion
Cellular Componentnucleus
Cellular Componentthylakoid
Biological Processglycine decarboxylation via glycine cleavage system

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycine cleavage system H protein 1, mitochondrial

Gene names

    • Name
      GDH1
    • Synonyms
      GCDH, GDCH, GDCSH
    • ORF names
      T32F12.25
    • Ordered locus names
      At2g35370

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    P25855
  • Secondary accessions
    • Q0WR60

Proteomes

Organism-specific databases

Genome annotation databases

PTM/Processing

Features

Showing features for transit peptide, chain, modified residue.

TypeIDPosition(s)Description
Transit peptide1-34Mitochondrion
ChainPRO_000001072935-165Glycine cleavage system H protein 1, mitochondrial
Modified residue97N6-lipoyllysine
Modified residue140Phosphoserine

Post-translational modification

S-nitrosylated and/or glutathionylated at unknown positions in response to nitric oxide.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in leaves, lower expression in green veins, petioles, and stems, and detected in roots.

Induction

Up-regulated by light.

Gene expression databases

Interaction

Subunit

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

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain56-138Lipoyl-binding

Sequence similarities

Belongs to the GcvH family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    165
  • Mass (Da)
    17,947
  • Last updated
    1992-05-01 v1
  • Checksum
    48309650C88F9BE2
MALRMWASSTANALKLSSSVSKSHLSPFSFSRCFSTVLEGLKYANSHEWVKHEGSVATIGITAHAQDHLGEVVFVELPEDNTSVSKEKSFGAVESVKATSEILSPISGEIIEVNKKLTESPGLINSSPYEDGWMIKVKPSSPAELESLMGPKEYTKFCEEEDAAH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U27144
EMBL· GenBank· DDBJ
AAA87942.1
EMBL· GenBank· DDBJ
Genomic DNA
M82921
EMBL· GenBank· DDBJ
AAA32802.1
EMBL· GenBank· DDBJ
mRNA
AC005314
EMBL· GenBank· DDBJ
AAC36184.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002685
EMBL· GenBank· DDBJ
AEC09100.1
EMBL· GenBank· DDBJ
Genomic DNA
AY050446
EMBL· GenBank· DDBJ
AAK91461.1
EMBL· GenBank· DDBJ
mRNA
AY058854
EMBL· GenBank· DDBJ
AAL24242.1
EMBL· GenBank· DDBJ
mRNA
AY097349
EMBL· GenBank· DDBJ
AAM19865.1
EMBL· GenBank· DDBJ
mRNA
AK228462
EMBL· GenBank· DDBJ
BAF00389.1
EMBL· GenBank· DDBJ
mRNA
AY086345
EMBL· GenBank· DDBJ
AAM64413.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

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