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Q9I993 (BCDO1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta,beta-carotene 15,15'-monooxygenase

EC=1.14.99.36
Alternative name(s):
Beta-carotene dioxygenase 1
Gene names
Name:BCMO1
Synonyms:BCDO
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Symmetrically cleaves beta-carotene into two molecules of retinal. The reaction proceeds in three stages, epoxidation of the 15,15'-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed.

Catalytic activity

Beta-carotene + O2 = 2 all-trans-retinal.

Cofactor

Binds 1 Fe2+ ion per subunit.

Pathway

Cofactor metabolism; retinol metabolism.

Sequence similarities

Belongs to the carotenoid oxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Beta,beta-carotene 15,15'-monooxygenase
PRO_0000143936

Sites

Metal binding1721Iron; catalytic By similarity
Metal binding2361Iron; catalytic By similarity
Metal binding3071Iron; catalytic By similarity
Metal binding5121Iron; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9I993 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 82C6EAAF75FE345B

FASTA52660,385
        10         20         30         40         50         60 
METIFNRNKE EHPEPIKAEV QGQLPTWLQG VLLRNGPGMH TIGDTKYNHW FDGLALLHSF 

        70         80         90        100        110        120 
TFKNGEVYYR SKYLRSDTYN CNIEANRIVV SEFGTMAYPD PCKNIFAKAF SYLSHTIPEF 

       130        140        150        160        170        180 
TDNCLINIMK TGDDYYATSE TNFIRKIDPQ TLETLDKVDY SKYVAVNLAT SHPHYDSAGN 

       190        200        210        220        230        240 
ILNMGTSIVD KGRTKYVLFK IPSSVPEKEK KKSCFKHLEV VCSIPSRSLL QPSYYHSFGI 

       250        260        270        280        290        300 
TENYIVFIEQ PFKLDIVKLA TAYIRGVNWA SCLSFHKEDK TWFHFVDRKT KKEVSTKFYT 

       310        320        330        340        350        360 
DALVLYHHIN AYEEDGHVVF DIVAYRDNSL YDMFYLKKLD KDFEVNNKLT SIPTCKRFVV 

       370        380        390        400        410        420 
PLQYDKDAEV GSNLVKLPTS ATAVKEKDGS IYCQPEILCE GIELPRVNYD YNGKKYKYVY 

       430        440        450        460        470        480 
ATEVQWSPVP TKIAKLNVQT KEVLHWGEDH CWPSEPIFVP SPDAREEDEG VVLTCVVVSE 

       490        500        510        520 
PNKAPFLLIL DAKTFKELGR ATVNVEMHLD LHGMFIPQND LGAETE 

« Hide

References

[1]"Cloning and expression of beta,beta-carotene-15,15'-dioxygenase."
Wyss A., Wirtz G.M., Woggon W.D., Brugger R., Wyss M., Friedlein A., Bachmann H., Hunziker W.
Biochem. Biophys. Res. Commun. 271:334-336(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: LSL Lohmann.
Tissue: Duodenum.
[2]"Expression pattern and localization of beta,beta-carotene 15,15'-dioxygenase in different tissues."
Wyss A., Wirtz G.M., Woggon W.D., Brugger R., Wyss M., Friedlein A., Riss G., Bachmann H., Hunziker W.
Biochem. J. 354:521-529(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: LSL Lohmann.
Tissue: Duodenum.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ271386 mRNA. Translation: CAB90825.1.
RefSeqNP_989966.1. NM_204635.1.
UniGeneGga.41.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000008671.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000008685; ENSGALP00000008671; ENSGALG00000005408.
GeneID395346.
KEGGgga:395346.

Organism-specific databases

CTD53630.

Phylogenomic databases

eggNOGCOG3670.
GeneTreeENSGT00500000044783.
HOGENOMHOG000232156.
HOVERGENHBG050679.
InParanoidQ9I993.
KOK00515.
OMAITENYIV.
OrthoDBEOG7353WB.
PhylomeDBQ9I993.
TreeFamTF314019.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17624.
UniPathwayUPA00912.

Family and domain databases

InterProIPR004294. Carotenoid_Oase.
[Graphical view]
PANTHERPTHR10543. PTHR10543. 1 hit.
PfamPF03055. RPE65. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20815431.
PROQ9I993.

Entry information

Entry nameBCDO1_CHICK
AccessionPrimary (citable) accession number: Q9I993
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways