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   24-JAN-2024, entry version 120.
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; 9031-ENSGALP00000008671; -.
DR   Ensembl; ENSGALT00000008685; ENSGALP00000008671; ENSGALG00000005408.
DR   Ensembl; ENSGALT00010018751.1; ENSGALP00010010301.1; ENSGALG00010007880.1.
DR   Ensembl; ENSGALT00015029548; ENSGALP00015017062; ENSGALG00015012147.
DR   KEGG; gga:395346; -.
DR   VEuPathDB; HostDB:geneid_395346; -.
DR   eggNOG; KOG1285; Eukaryota.
DR   GeneTree; ENSGT00950000182913; -.
DR   HOGENOM; CLU_016472_1_1_1; -.
DR   InParanoid; Q9I993; -.
DR   OMA; MHTIGDS; -.
DR   OrthoDB; 294919at2759; -.
DR   PhylomeDB; Q9I993; -.
DR   TreeFam; TF314019; -.
DR   BioCyc; MetaCyc:MONOMER-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 cell types or 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:SF132; BETA,BETA-CAROTENE 15,15'-DIOXYGENASE; 1.
DR   PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 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
//