Q9I993 (BCDO1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	retinoid metabolic process Inferred from direct assay PubMed 12468597. Source: UniProtKB retinol metabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	beta-carotene 15,15'-monooxygenase activity Inferred from direct assay PubMed 12468597. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 526	526	Beta,beta-carotene 15,15'-monooxygenase		PRO_0000143936
Sites
	Metal binding	172	1	Iron; catalytic By similarity
	Metal binding	236	1	Iron; catalytic By similarity
	Metal binding	307	1	Iron; catalytic By similarity
	Metal binding	512	1	Iron; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9I993 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 82C6EAAF75FE345B	FASTA	526	60,385
	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

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.
IPI	IPI00595044.
RefSeq	NP_989966.1. NM_204635.1.
UniGene	Gga.41.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	9031.ENSGALP00000008671.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSGALT00000008685; ENSGALP00000008671; ENSGALG00000005408.
GeneID	395346.
KEGG	gga:395346.
Organism-specific databases
CTD	53630.
Phylogenomic databases
eggNOG	COG3670.
GeneTree	ENSGT00500000044783.
HOGENOM	HOG000232156.
HOVERGEN	HBG050679.
InParanoid	Q9I993.
KO	K00515.
OMA	ITENYIV.
OrthoDB	EOG4G7BZ5.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-17624.
UniPathway	UPA00912.
Family and domain databases
InterPro	IPR004294. Carotenoid_Oase. [Graphical view]
PANTHER	PTHR10543. PTHR10543. 1 hit.
Pfam	PF03055. RPE65. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20815431.

Entry information

Entry name

BCDO1_CHICK

Accession

Primary (citable) accession number: Q9I993

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program