Q9SVG3 · BBE21_ARATH

Function

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit in a bicovalent manner.

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 Componentapoplast
Cellular Componentcytosol
Cellular Componentplant-type cell wall
Cellular Componentplasma membrane
Molecular FunctionFAD binding
Molecular Functionoxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Berberine bridge enzyme-like 21
  • EC number
  • Short names
    AtBBE-like 21

Gene names

    • ORF names
      F21C20.190
    • Ordered locus names
      At4g20840

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9SVG3

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, cross-link.

TypeIDPosition(s)Description
Signal1-26
ChainPRO_500818048327-539Berberine bridge enzyme-like 21
Disulfide bond41↔104
Glycosylation79N-linked (GlcNAc...) asparagine
Cross-link119↔1816-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys)
Glycosylation340N-linked (GlcNAc...) asparagine

Post-translational modification

The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage.

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain82-256FAD-binding PCMH-type

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
    539
  • Mass (Da)
    60,144
  • Last updated
    2000-05-01 v1
  • Checksum
    6645E9376E216426
MIATQTFVSVFFFVFFLVSLPFFSSAAPPSSDSIYESFVQCFSDKTKSPQAQITDNVFSRTNPSFSSVLRAYIRNGRFNTSSTPKPAIIVTPRSDIHVSAAVTCSKSLNFLLKIRSGGHDYEGLSYISDKPFFILDMSNLRDVSVDIADQSAWISAGATLGEVYYRIWEKSKVHGFPAGVCPTVGVGGHISGGGYGNMLRKFGLSVDNLIDAKIVDVNGQILDRKSMGEDLFWAISGGGGASFGVVLGYKVKLVPVPETVTVFRVEKYMDSGAVDMVHKWQSVGPKTDRNLFLRMLIQPVTRKKVKTVRATVVALFLGRAEEVVALLGKEFPELSLKKENCSEMTWFQSALWWDNRVNPTQIDPKVFLDRNLDRANFGKRKSDYVASEIPRDGIESLFKKMTELGKIGLVFNPYGGKMAEVTVNATPFPHRSKLFKIQYSVTWQENSVEIEKGFLNQANVLYSFMTGFVSKNPRNAYLNYRDVDIGVNDHGTNSYEEGEVYGRKYFGDNFDRLVKVKTAADPDNFFRNEQSIPTVLSKA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL080254
EMBL· GenBank· DDBJ
CAB45850.1
EMBL· GenBank· DDBJ
Genomic DNA
AL161553
EMBL· GenBank· DDBJ
CAB79084.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE84367.1
EMBL· GenBank· DDBJ
Genomic DNA
AK317639
EMBL· GenBank· DDBJ
BAH20300.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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