A3ABS4 · A3ABS4_ORYSJ

Function

function

Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

Mo-molybdopterin (UniProtKB | Rhea| CHEBI:71302 )

Note: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
heme (UniProtKB | Rhea| CHEBI:30413 )

Features

Showing features for binding site.

1890100200300400500600700800
TypeIDPosition(s)Description
Binding site165Mo (UniProtKB | ChEBI) of Mo-molybdopterin (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 Componentcytoplasm
Cellular Componentintracellular membrane-bounded organelle
Cellular Componentorganelle membrane
Molecular Functionheme binding
Molecular Functionmolybdenum ion binding
Molecular Functionmolybdopterin cofactor binding
Molecular Functionnitrate reductase (NADPH) activity
Molecular Functionsulfite oxidase activity
Biological Processnitrate assimilation
Biological Processnitric oxide biosynthetic process
Biological Processsulfur compound metabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Nitrate reductase

Gene names

    • ORF names
      OsJ_08536

Organism names

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

Accessions

  • Primary accession
    A3ABS4

Proteomes

PTM/Processing

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-53Disordered
Compositional bias35-51Basic and acidic residues
Domain513-560Cytochrome b5 heme-binding
Domain630-742FAD-binding FR-type

Sequence similarities

Belongs to the nitrate reductase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    890
  • Mass (Da)
    98,612
  • Last updated
    2007-03-20 v1
  • Checksum
    1D57BECA4D1BE40E
MAASVEYKLAPHPWASNAPSSNLDLFPSGGGKRRSGSETDSDDEDSIPPDWRSLYHPRLEVAEPAVKDPRDEATSDAWVRRHPALVRLTGKHPFNSEPPLPRLMSHGFITPAPLHYVRNHGAVPKADWSTWAVEVTGLVKRPARLNMEQLVTGFEAVELPVTLVCAGNRRKEQNMVRQTVGFNWGPGAISTSVWRGVRLRDVLRWCGVMGASAGAANVCFEGAEDLPGGGGCKYGTSLRREVAMDPAHDVILAYMQNGEPLTPDHGFPVRVIVPGFIGGRMVKWLKRIIVASSESESYYHYRDNRVLPSHVDAELANAEAWWYKPEYMINELNINSVITTPGHDEVLPINALTTQRPYTMKGYAYSGGGRKVTRVEVTLDGGETWQVCNLDHPERPTKYGKYWCWCFWSVDVEVLELLAAKEIAVRAWDESLNTQPEKLIWNLMGMMNNCWFRVKTKTCRPHKGEIGLVFEHPTQPGNQAGGWMARQKHLETSESAVSTLKRSTSTPFLNTATTQYTMSEVRRHTTPESAWIIVHGHVYDCTGFLKDHPGGADSIMINAGHRLHRGIRTPSTPTRPVASSRCTGIGELIVTGSDYSPQSSSADLTSIVESPTATAAPAVPVSTVALSNPREKVKCRLMDKKSLSYNVRLFRFALPSPDQKLGLPVGKHVYVCASIGGKLCMRAYTPTSSVDEVGYIELLIKIYFKGEDPKFPDGGLMSQYLDYLPLGATIDIKGPIGHIEYAGRGAFTVNGERRFARRLAMVAGGTGITPVYQVIQAVLWDQPDDGTEMHVVYANRTEDDMLLREEIDRWAAAHPARLKVWYVVSKVARPEDGWEYGVGRVDERTLREHLPPGDGETLALVCGPPAMVECTVRPGLEKMGYDLDKSCLVF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias35-51Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM000139
EMBL· GenBank· DDBJ
EAZ24763.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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