Q0DIU9 · Q0DIU9_ORYSJ

Function

Catalytic activity

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.

Features

Showing features for active site.

158150100150200250300350400450500550
TypeIDPosition(s)Description
Active site410

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 Functionenzyme inhibitor activity
Molecular Functionpectinesterase activity
Biological Processcell wall modification
Biological Processpectin catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pectinesterase
  • EC number

Gene names

    • Ordered locus names
      Os05g0361500

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Nipponbare
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    Q0DIU9

Proteomes

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-25
ChainPRO_500514243126-581Pectinesterase

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain35-191Pectinesterase inhibitor
Region200-226Disordered
Region432-501Disordered
Compositional bias461-475Basic residues
Compositional bias524-558Basic residues
Region524-581Disordered
Compositional bias559-573Basic and acidic residues

Sequence similarities

In the C-terminal section; belongs to the pectinesterase family.
In the N-terminal section; belongs to the PMEI family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    581
  • Mass (Da)
    63,417
  • Last updated
    2006-10-17 v1
  • Checksum
    10121C44BCFC89BC
MAVRYEKKAMCALLLSLIMVALSVAAAGDGDAPPSTPVSPTTACNDTTDPSFCRTVLPPRGSSDLYTYGRFSVARSLDSARRFAGLVGRYLARHRGLSPAAVGALRDCQLMSELNVDFLSAAGATLRSAADALPDPQADDVHTLLSAILTNQQTCLDGLQAASSSWSERGGGGLAAPIANGTKLYSLSLSLFTRAWVPTAKGSKHHGGGKKPHQGHGKKQPPAAAASMRRGLFDAADGEMARRVAMEGPEATVAVNGVVTVDQGGGGNYTTVGDAVAAAPSNLDGSTGHYVIYVAGGVYEENVVVPKHKRYIMMVGDGVGQTVITGNRSVVDGWTTFNSATFAVVGQGFVAMNMTFRNTAGPSKHQAVALRSGADLSAFYGCSFEAYQDTLYAHSLRQFYRRCDVYGTVDYVFGNAAVVFQSCAFLSRLPRPRPVQHRHGAGPIRPQPEHRHLHPGLLPPRRPGPRRRRRRRPDAHLPRPAVEELLQDGGHGVLRRRPRRPGRVDAVVRRLRARHALLRRVQQLRPRRRHQPPRRLAGLPRPRRRRRRRQLHRHQHGARRQLAAPDRRPLHQRLPHFRSTY

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias461-475Basic residues
Compositional bias524-558Basic residues
Compositional bias559-573Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP008211
EMBL· GenBank· DDBJ
BAF17224.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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