A0A0P0XLG1 · A0A0P0XLG1_ORYSJ

Function

function

Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for active site.

1975100200300400500600700800900
TypeIDPosition(s)Description
Active site182
Active site610

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
Molecular Functionphosphoenolpyruvate carboxylase activity
Biological Processcarbon fixation
Biological Processleaf development
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    phosphoenolpyruvate carboxylase
  • EC number

Gene names

    • ORF names
      OSNPB_090315700
    • Ordered locus names
      Os09g0315700

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
    A0A0P0XLG1

Proteomes

Genome annotation databases

Subcellular Location

PTM/Processing

Features

Showing features for modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue (large scale data)21PTMeXchangePhosphoserine
Modified residue (large scale data)770PTMeXchangePhosphoserine

Proteomic databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the PEPCase type 1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    975
  • Mass (Da)
    110,474
  • Last updated
    2016-01-20 v1
  • Checksum
    0CD48D5B14AA8471
MSAMSAAGGGGGVGKVERLSSIDAQLRQLVPAKLSEDDKLIEYDALLLDRFLDVLHGLHGDDLKDLVQECYEVAAEYETKHDVQKLDELGNMITSLDPGDSIVIAKAFSHMLNLANLAEEVQIAYRRRIKLKKGDFADENSAMTESDIEETLKRLVFDLKKSPAEVFDALKSQTVDLVLTAHPTQSVRRSLLQKHSRIRNCLVQLYSKDITPDDKQELDEALQREIQAAFRTDEIRRTQPTPQDEMRAGMSYFHETIWKGVPKFLRRVDTALKNIGIDERVPYNAPLIQFSSWMGGDRDGNPRVTPEVTRDVCLLARMMAANLYCSQIEDLMFELSMWRCNEELRSRADDLHRSSKKDAKHYIEFWKKVPLNEPYRVILSDVRDKLYNTRERSRELLSSGYCDIPEEATLTNVEQLLEPLELCYRSLCACGDRAIADGSLLDFLRQVSTFGLSLVRLDIRQESDRHTDVLDAITTYLGIGSYREWSEERRQEWLLSELNGKRPLFGPDLPRTDEVADVLDTFHVIAELPADSFGAYVISMATAPSDVLAVELLQRECHVKTPLRVVPLFEKLADLESAPAALTRLFSISWYRQRINGKQEVMIGYSDSGKDAGRLSAAWQMYKAQEQLVKVAKDFGVKLTMFHGRGGTVGRGGGPTHLAILSQPPDTINGSLRVTVQGEVIEQSFGEEHLCFRTLQRFTAATLEHGMHPPSAPKPEWRALLDEMAVVATKEYRSVVFQEPRFVEYFRLATPETEYGRMNIGSRPSKRKPSGGIESLRAIPWIFAWTQTRFHLPVWLGFGAAFKHALQKDIRNLHMLQEMYNEWPFFRVTLDLIEMVFAKGNPGIAALYDKLLVSEDLQPLGEKLRANYVETQKLLLQVAGHRDLLEGDPYLKQRLRLRDAYITTLNVCQAYTLKRIRDPDYHVTLRPHLSKEVMDGSKPAAELVKLNPGSEYAPGLEDTLILTMKGIAAGLQNTG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP014965
EMBL· GenBank· DDBJ
BAT07416.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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