A0A7C8ZQB5 · A0A7C8ZQB5_OPUST

Function

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Features

Showing features for binding site.

1119102030405060708090100110
TypeIDPosition(s)Description
Binding site63Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

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 Componentmembrane
Molecular Function(22S)-22-hydroxy-5alpha-campestan-3-one C-23 hydroxylase activity
Molecular Function3-epi-6-deoxocathasterone C-23 hydroxylase activity
Molecular Functionheme binding
Molecular Functioniron ion binding
Biological Processbrassinosteroid biosynthetic process
Biological Processbrassinosteroid homeostasis
Biological Processsterol metabolic process

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • 3-epi-6-deoxocathasterone 23-monooxygenase
      (EC:1.14.14.147
      )

Organism names

Accessions

  • Primary accession
    A0A7C8ZQB5

Subcellular Location

Membrane
; Single-pass membrane protein

Keywords

  • Cellular component

Family & Domains

Sequence similarities

Belongs to the cytochrome P450 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    119
  • Mass (Da)
    14,133
  • Last updated
    2020-12-02 v1
  • Checksum
    F4B3D9197DE0EC06
AMKDVEIKGYLIPKGWCVLAYFRSVHLDENLYDEPHQFDPWRWQNKDVNGNNFTPFGGGQRLCPGLDLGRLEASIFLHHFVMRFRWAAEDDSITHFPTVRMRKGMPVWLKRRKETQQKN

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GISG01158093
EMBL· GenBank· DDBJ
MBA4649038.1
EMBL· GenBank· DDBJ
Transcribed RNA

Similar Proteins

Disclaimer

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