BCDO1_CHICK
ID BCDO1_CHICK Reviewed; 526 AA.
AC Q9I993;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Beta,beta-carotene 15,15'-dioxygenase {ECO:0000305|PubMed:10799297};
DE EC=1.13.11.63 {ECO:0000269|PubMed:10799297};
DE AltName: Full=Beta-carotene dioxygenase 1;
DE AltName: Full=Beta-carotene oxygenase 1 {ECO:0000250|UniProtKB:Q9HAY6};
GN Name=BCO1 {ECO:0000250|UniProtKB:Q9HAY6}; Synonyms=BCDO, BCMO1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=LSL Lohmann; TISSUE=Duodenum;
RX PubMed=10799297; DOI=10.1006/bbrc.2000.2619;
RA Wyss A., Wirtz G.M., Woggon W.D., Brugger R., Wyss M., Friedlein A.,
RA Bachmann H., Hunziker W.;
RT "Cloning and expression of beta,beta-carotene-15,15'-dioxygenase.";
RL Biochem. Biophys. Res. Commun. 271:334-336(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=LSL Lohmann; TISSUE=Duodenum;
RX PubMed=11237856; DOI=10.1042/0264-6021:3540521;
RA Wyss A., Wirtz G.M., Woggon W.D., Brugger R., Wyss M., Friedlein A.,
RA Riss G., Bachmann H., Hunziker W.;
RT "Expression pattern and localization of beta,beta-carotene 15,15'-
RT dioxygenase in different tissues.";
RL Biochem. J. 354:521-529(2001).
CC -!- FUNCTION: Symmetrically cleaves beta-carotene into two molecules of
CC retinal using a dioxygenase mechanism. {ECO:0000269|PubMed:10799297}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-beta-carotene + O2 = 2 all-trans-retinal;
CC Xref=Rhea:RHEA:32887, ChEBI:CHEBI:15379, ChEBI:CHEBI:17579,
CC ChEBI:CHEBI:17898; EC=1.13.11.63;
CC Evidence={ECO:0000269|PubMed:10799297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32888;
CC Evidence={ECO:0000305|PubMed:10799297};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q9JJS6};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9JJS6};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000305|PubMed:10799297}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:10799297}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; AJ271386; CAB90825.1; -; mRNA.
DR RefSeq; NP_989966.1; NM_204635.1.
DR RefSeq; XP_015148005.1; XM_015292519.1.
DR RefSeq; XP_015148006.1; XM_015292520.1.
DR AlphaFoldDB; Q9I993; -.
DR SMR; Q9I993; -.
DR STRING; 9031.ENSGALP00000008671; -.
DR PaxDb; Q9I993; -.
DR Ensembl; ENSGALT00000008685; ENSGALP00000008671; ENSGALG00000005408.
DR GeneID; 395346; -.
DR KEGG; gga:395346; -.
DR CTD; 53630; -.
DR VEuPathDB; HostDB:geneid_395346; -.
DR eggNOG; KOG1285; Eukaryota.
DR GeneTree; ENSGT00950000182913; -.
DR HOGENOM; CLU_016472_1_1_1; -.
DR InParanoid; Q9I993; -.
DR OMA; ENYIIFL; -.
DR OrthoDB; 524712at2759; -.
DR PhylomeDB; Q9I993; -.
DR TreeFam; TF314019; -.
DR BioCyc; MetaCyc:MON-17624; -.
DR BRENDA; 1.13.11.63; 1306.
DR Reactome; R-GGA-975634; Retinoid metabolism and transport.
DR UniPathway; UPA00912; -.
DR PRO; PR:Q9I993; -.
DR Proteomes; UP000000539; Chromosome 11.
DR Bgee; ENSGALG00000005408; Expressed in liver and 12 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0003834; F:beta-carotene 15,15'-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0010436; F:carotenoid dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IDA:AgBase.
DR GO; GO:1901810; P:beta-carotene metabolic process; IDA:AgBase.
DR GO; GO:0016121; P:carotene catabolic process; ISS:UniProtKB.
DR GO; GO:0032526; P:response to retinoic acid; IDA:AgBase.
DR GO; GO:0042574; P:retinal metabolic process; IDA:AgBase.
DR GO; GO:0001523; P:retinoid metabolic process; IDA:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Dioxygenase; Direct protein sequencing; Iron; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..526
FT /note="Beta,beta-carotene 15,15'-dioxygenase"
FT /id="PRO_0000143936"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 236
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 307
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 512
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
SQ SEQUENCE 526 AA; 60385 MW; 82C6EAAF75FE345B CRC64;
METIFNRNKE EHPEPIKAEV QGQLPTWLQG VLLRNGPGMH TIGDTKYNHW FDGLALLHSF
TFKNGEVYYR SKYLRSDTYN CNIEANRIVV SEFGTMAYPD PCKNIFAKAF SYLSHTIPEF
TDNCLINIMK TGDDYYATSE TNFIRKIDPQ TLETLDKVDY SKYVAVNLAT SHPHYDSAGN
ILNMGTSIVD KGRTKYVLFK IPSSVPEKEK KKSCFKHLEV VCSIPSRSLL QPSYYHSFGI
TENYIVFIEQ PFKLDIVKLA TAYIRGVNWA SCLSFHKEDK TWFHFVDRKT KKEVSTKFYT
DALVLYHHIN AYEEDGHVVF DIVAYRDNSL YDMFYLKKLD KDFEVNNKLT SIPTCKRFVV
PLQYDKDAEV GSNLVKLPTS ATAVKEKDGS IYCQPEILCE GIELPRVNYD YNGKKYKYVY
ATEVQWSPVP TKIAKLNVQT KEVLHWGEDH CWPSEPIFVP SPDAREEDEG VVLTCVVVSE
PNKAPFLLIL DAKTFKELGR ATVNVEMHLD LHGMFIPQND LGAETE
