Q10G56 · OAT_ORYSJ

Function

function

Confers drought and oxidative stress tolerance mainly through enhancing ROS-scavenging capacity and Pro pre-accumulation.

Catalytic activity

Cofactor

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

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1.

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
Cellular Componentmitochondrial matrix
Molecular Functionidentical protein binding
Molecular Functionornithine aminotransferase activity
Molecular Functionpyridoxal phosphate binding
Biological Processarginine catabolic process to glutamate
Biological Processarginine catabolic process to proline via ornithine
Biological ProcessL-proline biosynthetic process
Biological Processresponse to abscisic acid
Biological Processresponse to auxin
Biological Processresponse to brassinosteroid
Biological Processresponse to flooding
Biological Processresponse to heat
Biological Processresponse to jasmonic acid
Biological Processresponse to oxidative stress
Biological Processresponse to salt stress
Biological Processresponse to water deprivation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ornithine aminotransferase, mitochondrial
  • EC number
  • Alternative names
    • Ornithine delta-aminotransferase
    • Ornithine--oxo-acid aminotransferase

Gene names

    • Name
      OAT
    • ORF names
      OSJNBa0038E17.15
    • Ordered locus names
      Os03g0643300, LOC_Os03g44150

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
    Q10G56
  • Secondary accessions
    • A0A0N7KHQ2
    • Q60DP3

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
Transit peptide1-32UniProtMitochondrion
ChainPRO_000042129933-473UniProtOrnithine aminotransferase, mitochondrial
Modified residue293UniProtN6-(pyridoxal phosphate)lysine
Modified residue (large scale data)425PTMeXchangePhosphoserine
Modified residue (large scale data)427PTMeXchangePhosphoserine

Proteomic databases

Expression

Induction

Up-regulated by SNAC2. Also induced by high-salinity, heat, and submergence. Strongly induced by abscisic acid (ABA) and auxin (IAA), and slightly induced by brassinosteroid (BR) and jasmonic acid (JA).

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    473
  • Mass (Da)
    51,442
  • Last updated
    2006-08-22 v1
  • Checksum
    16E42093718DC21F
MAAALARRGGGGLARALARGRGMCSATAAERAAGAALTSEELMRMERERSAHNYHPIPVVFSKGEGSHILDPEGNKYIDFLSAYSAVNQGHCHPKVLRALKEQAERLTLSSRAFYNDKFPIFAEYLTSMFGYEMMLPMNTGAEGVETAIKLVRKWGYEKKKIPKNEALIVSCCGCFHGRTLGVISMSCDNDATRGFGPLVPGHLKVDFGDTDGLEKIFKDHGERICGFLFEPIQGEAGVIIPPDGYLKAVRDLCSRHNILMIADEIQTGIARTGKMLACDWENIRPDVVILGKALGAGVVPVSAVLADKDIMLCIKPGEHGSTFGGNPLASAVAVASLKVVTDEGLVERAAKLGQEFRDQLQKVQQRFPQIIREVRGRGLLNAVDLSNEALSPASAYDICIKLKERGVLAKPTHDTIIRLAPPLSISPEELAEASKAFSDVLEHDLPQLQKQIKKTESAAEKQSCDRCGRDLY

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0P0W0L3A0A0P0W0L3_ORYSJOs03g0643300159

Sequence caution

The sequence AAU90265.1 differs from that shown. Reason: Erroneous gene model prediction

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC145383
EMBL· GenBank· DDBJ
AAU90265.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
DP000009
EMBL· GenBank· DDBJ
ABF97848.1
EMBL· GenBank· DDBJ
Genomic DNA
AP008209
EMBL· GenBank· DDBJ
BAF12667.1
EMBL· GenBank· DDBJ
Genomic DNA
AP014959
EMBL· GenBank· DDBJ
BAS85449.1
EMBL· GenBank· DDBJ
Genomic DNA
AK099445
EMBL· GenBank· DDBJ
BAG94132.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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