Q6L4H5 · Q6L4H5_ORYSJ

Function

function

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.

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 Componentcytoplasm
Molecular Functionpyridoxal phosphate binding
Molecular Functionthreonine synthase activity
Biological Processcysteine biosynthetic process
Biological Processthreonine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    threonine synthase
  • EC number

Gene names

    • Name
      P0560C03.1
    • ORF names
      OSNPB_050549700
    • Ordered locus names
      Os05g0549700

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
    Q6L4H5

Proteomes

Genome annotation databases

Subcellular Location

PTM/Processing

Features

Showing features for modified residue (large scale data), modified residue.

Type
IDPosition(s)Source
Description
Modified residue (large scale data)197PTMeXchangePhosphoserine
Modified residue199UniProtN6-(pyridoxal phosphate)lysine
Modified residue (large scale data)300PTMeXchangePhosphoserine

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region13-34Disordered
Domain159-470Tryptophan synthase beta chain-like PALP

Sequence similarities

Belongs to the threonine synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    521
  • Mass (Da)
    57,216
  • Last updated
    2005-08-30 v1
  • Checksum
    C62ACB3285F2BFF2
MAATTHAASLSFLLSHPHPTSPNPNPNPNLPLRRAPHRVRCATDAAATRHRRAADENIREEAARHRAPNHNFSAWYAPFPPAPNGDPDERYSLDEIVYRSSSGGLLDVRHDMDALARFPGSYWRDLFDSRVGRTTWPFGSGVWSKKEFVLPEIDPDHIVSLFEGNSNLFWAERLGRDHLAGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRRAPLSRPIAGVGCASTGDTSAALSAYCAAAGIPAIVFLPANRISLEQLIQPIANGATVLSLDTDFDGCMRLIREVTAELPIYLANSLNSLRLEGQKTAAIEILQQFDWEVPDWVIVPGGNLGNIYAFYKGFEMCRVLGLVDRVPRLVCAQAANANPLYRYYKSGWTEFTPQVAEPTFASAIQIGDPVSVDRAVVALKATDGIVEEATEEELMNAMSLADRTGMFACPHTGVALAALFKLRDQRIIGPNDRTVVVSTAHGLKFSQSKIDYHDSKIEDMACKYANPPVSVKADFGAVMDVLKKRLKGKL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC135925
EMBL· GenBank· DDBJ
AAT39260.1
EMBL· GenBank· DDBJ
Genomic DNA
AP014961
EMBL· GenBank· DDBJ
BAS95201.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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