C5WNL8 · C5WNL8_SORBI

Function

Catalytic activity

Cofactor

heme b (UniProtKB | Rhea| CHEBI:60344 )

Features

Showing features for binding site.

125020406080100120140160180200220240
TypeIDPosition(s)Description
Binding site35L-ascorbate 2 (UniProtKB | ChEBI)
Binding site35L-ascorbate 1 (UniProtKB | ChEBI)
Binding site41L-ascorbate 3 (UniProtKB | ChEBI)
Binding site42L-ascorbate 3 (UniProtKB | ChEBI)
Binding site75L-ascorbate 4 (UniProtKB | ChEBI)
Binding site79L-ascorbate 4 (UniProtKB | ChEBI)
Binding site132L-ascorbate 3 (UniProtKB | ChEBI)
Binding site163Fe (UniProtKB | ChEBI); axial binding residue of heme b (UniProtKB | ChEBI)
Binding site167heme b (UniProtKB | ChEBI)
Binding site169heme b (UniProtKB | ChEBI)
Binding site172L-ascorbate 2 (UniProtKB | ChEBI)
Binding site172L-ascorbate 1 (UniProtKB | ChEBI)
Binding site173heme b (UniProtKB | ChEBI)

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 Componentchloroplast
Molecular Functionheme binding
Molecular FunctionL-ascorbate peroxidase activity
Molecular Functionmetal ion binding
Molecular Functionperoxidase activity
Biological Processcellular response to oxidative stress
Biological Processhydrogen peroxide catabolic process
Biological Processresponse to reactive oxygen species

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    L-ascorbate peroxidase
  • EC number

Gene names

    • ORF names
      SORBI_3001G410200

Organism names

  • Taxonomic identifier
  • Strain
    • cv. BTx623
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Sorghinae > Sorghum

Accessions

  • Primary accession
    C5WNL8

Proteomes

Genome annotation databases

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain74-250Plant heme peroxidase family profile
Region113-137Disordered
Compositional bias121-137Basic and acidic residues

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    250
  • Mass (Da)
    27,217
  • Last updated
    2009-09-01 v1
  • Checksum
    0C6676CD995F761C
MAKSYPTVSAEYSEAVEKARQKLRALIAEKSCAPLMLRLAWHSAGTFDVSSRTGGPFGTMKNPAELAHGANAGLDIAVRLLEPIKEEFPILSYADFYQLAGVVAVEVTGGPQIPFHPGREDKPQPPPEGRLPDATKGSDHLRQVFGKQMGLSDQDIVALSGGHTLGRCHKERSGFEGAWTSNPLVFDNSYFKELLSGDKEGLLQLPSDKALLSDPAFRPLVDKYAADEKAFFEDYKEAHLKLSELGFADA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias121-137Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM000760
EMBL· GenBank· DDBJ
EER95051.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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