Q99NF1 · BCDO2_MOUSE

  • Protein
    Carotenoid-cleaving dioxygenase, mitochondrial
  • Gene
    Bco2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Broad specificity mitochondrial dioxygenase that mediates the asymmetric oxidative cleavage of carotenoids (PubMed:11278918, PubMed:21106934).
Cleaves carotenes (pure hydrocarbon carotenoids) such as all-trans-beta-carotene and lycopene as well as xanthophylls (oxygenated carotenoids) such as zeaxanthin, lutein and beta-cryptoxanthin at both the 9,10 and the 9',10' carbon-carbon double bond (PubMed:11278918, PubMed:21106934).
Through its function in carotenoids metabolism regulates oxidative stress and the production of important signaling molecules (PubMed:21106934).

Catalytic activity

  • all-trans-beta-carotene + O2 = all-trans-10'-apo-beta-carotenal + beta-ionone
    This reaction proceeds in the forward direction.
    EC:1.13.11.71 (UniProtKB | ENZYME | Rhea)
  • 5-cis-lycopene + O2 = (3E,5E)-6,10-dimethylundeca-3,5,9-trien-2-one + 5-cis-10'-apo-lycopenal
    This reaction proceeds in the forward direction.
  • 13-cis-lycopene + O2 = (3E,5E)-6,10-dimethylundeca-3,5,9-trien-2-one + 13-cis-10'-apo-lycopenal
    This reaction proceeds in the forward direction.
  • lutein + O2 = (3R)-3-hydroxy-10'-apo-beta-carotenal + (3R,6R)-hydroxy-alpha-ionone
    This reaction proceeds in the forward direction.
  • lutein + O2 = (3R)-hydroxy-beta-ionone + (3R,6R)-3-hydroxy-10'-apo-alpha-carotenal
    This reaction proceeds in the forward direction.
  • all-trans-zeaxanthin + 2 O2 = 2 (3R)-hydroxy-beta-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial
    This reaction proceeds in the forward direction.
  • all-trans-zeaxanthin + O2 = (3R)-3-hydroxy-10'-apo-beta-carotenal + (3R)-hydroxy-beta-ionone
    This reaction proceeds in the forward direction.
  • beta-cryptoxanthin + O2 = (3R)-hydroxy-beta-ionone + all-trans-10'-apo-beta-carotenal
    This reaction proceeds in the forward direction.
  • all-trans-10'-apo-beta-carotenal + O2 = 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial + beta-ionone
    This reaction proceeds in the forward direction.
  • (3R)-3-hydroxy-10'-apo-beta-carotenal + O2 = (3R)-hydroxy-beta-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial
    This reaction proceeds in the forward direction.
  • (3R,6R)-3-hydroxy-10'-apo-alpha-carotenal + O2 = (3R,6R)-hydroxy-alpha-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial
    This reaction proceeds in the forward direction.

Cofactor

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 1 Fe2+ ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site179Fe cation (UniProtKB | ChEBI); catalytic
Binding site239Fe cation (UniProtKB | ChEBI); catalytic
Binding site310Fe cation (UniProtKB | ChEBI); catalytic
Binding site526Fe cation (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentmitochondrion
Molecular Function9,10 (9', 10')-carotenoid-cleaving dioxygenase activity
Molecular Functionbeta,beta-carotene-9',10'-cleaving oxygenase activity
Molecular Functionbeta-carotene 15,15'-dioxygenase activity
Molecular Functioncarotenoid dioxygenase activity
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
Biological Processcarotene catabolic process
Biological Processcarotene metabolic process
Biological Processcarotenoid metabolic process
Biological Processlutein catabolic process
Biological Processlycopene catabolic process
Biological Processregulation of mitochondrial membrane potential
Biological Processregulation of reactive oxygen species metabolic process
Biological Processretinal metabolic process
Biological Processretinoic acid metabolic process
Biological Processxanthophyll catabolic process
Biological Processxanthophyll metabolic process
Biological Processzeaxanthin catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Carotenoid-cleaving dioxygenase, mitochondrial
  • EC number
  • Alternative names
    • B-diox-II
    • Beta,beta-carotene 9',10'-oxygenase
    • Beta-carotene dioxygenase 2

Gene names

    • Name
      Bco2
    • Synonyms
      Bcdo2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q99NF1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Homozygous knockout mice lacking Bcdo2 develop normally, and both females and males are fertile when raised on standard diet (PubMed:21106934).
On a diet supplemented with xanthophylls, knockout mice accumulate derivatives of these xanthophylls in all tested tissues and develop liver steatosis with large lipid droplets in hepatocytes and a significantly increased triacylglyceride content (PubMed:21106934).
Accumulated carotenoids impair mitochondrial respiration, induce ROS production and cellular signaling pathways related to oxidative stress (PubMed:21106934).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 26 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001439391-532Carotenoid-cleaving dioxygenase, mitochondrial

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in small intestine, liver, kidney, testis and less abundantly in spleen, brain, lung, and heart.

Induction

Up-regulated by carotenoids.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the carotenoid oxygenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    532
  • Mass (Da)
    60,142
  • Last updated
    2001-06-01 v1
  • Checksum
    7461AD5A53FE86A3
MLGPKQSLPCIAPLLTTAEETLSAVSARVRGHIPEWLNGYLLRVGPGKFEFGKDRYNHWFDGMALLHQFRMERGTVTYKSKFLQSDTYKANSAGGRIVISEFGTLALPDPCKSIFERFMSRFEPPTMTDNTNVNFVQYKGDYYMSTETNFMNKVDIEMLERTEKVDWSKFIAVNGATAHPHYDPDGTAYNMGNSYGPRGSCYNIIRVPPKKKEPGETIHGAQVLCSIASTEKMKPSYYHSFGMTKNYIIFVEQPVKMKLWKIITSKIRGKPFADGISWEPQYNTRFHVVDKHTGQLLPGMYYSMPFLTYHQINAFEDQGCIVIDLCCQDDGRSLDLYQLQNLRKAGEGLDQVYELKAKSFPRRFVLPLDVSVDAAEGKNLSPLSYSSASAVKQGDGEIWCSPENLHHEDLEEEGGIEFPQINYGRFNGKKYSFFYGCGFRHLVGDSLIKVDVTNKTLRVWREEGFYPSEPVFVPVPGADEEDSGVILSVVITPNQSESNFLLVLDAKSFTELGRAEVPVQMPYGFHGTFVPI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ290392
EMBL· GenBank· DDBJ
CAC28026.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp