BCDO1_RAT
ID BCDO1_RAT Reviewed; 566 AA.
AC Q91XT5;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Beta,beta-carotene 15,15'-dioxygenase {ECO:0000305};
DE EC=1.13.11.63 {ECO:0000250|UniProtKB:Q9HAY6};
DE AltName: Full=Beta-carotene dioxygenase 1;
DE AltName: Full=Beta-carotene oxygenase 1 {ECO:0000312|RGD:70981};
GN Name=Bco1 {ECO:0000312|RGD:70981}; Synonyms=Bcdo, Bcdo1, Bcmo1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Intestine;
RA Takitani K., Ban R., Tamai H.;
RT "Regulation of beta-carotene 15,15'-dioxygenase in oxidative stress.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Symmetrically cleaves beta-carotene into two molecules of
CC retinal using a dioxygenase mechanism. {ECO:0000250|UniProtKB:Q9HAY6}.
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:0000250|UniProtKB:Q9HAY6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32888;
CC Evidence={ECO:0000250|UniProtKB:Q9HAY6};
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:0000250|UniProtKB:Q9HAY6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9I993}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB062912; BAB60807.1; -; mRNA.
DR AlphaFoldDB; Q91XT5; -.
DR SMR; Q91XT5; -.
DR STRING; 10116.ENSRNOP00000016880; -.
DR PaxDb; Q91XT5; -.
DR UCSC; RGD:70981; rat.
DR RGD; 70981; Bco1.
DR eggNOG; KOG1285; Eukaryota.
DR InParanoid; Q91XT5; -.
DR PhylomeDB; Q91XT5; -.
DR BRENDA; 1.13.11.63; 5301.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR UniPathway; UPA00912; -.
DR PRO; PR:Q91XT5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0003834; F:beta-carotene 15,15'-dioxygenase activity; IDA:RGD.
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:1901810; P:beta-carotene metabolic process; ISO:RGD.
DR GO; GO:0016121; P:carotene catabolic process; ISS:UniProtKB.
DR GO; GO:0042574; P:retinal metabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cytoplasm; Dioxygenase; Iron; Lipid metabolism; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..566
FT /note="Beta,beta-carotene 15,15'-dioxygenase"
FT /id="PRO_0000143935"
FT REGION 529..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 308
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 514
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
SQ SEQUENCE 566 AA; 63637 MW; A1FF8A47BA6CE6E5 CRC64;
MEIIFGRNKK EQLEPLRATV TGSIPAWLQG TLLRNGPGMH TVGDSKYNHW FDGLALLHSF
SIRDGEVFYR SKYLQSDTYN ANIEANRIVV SEFGTMAYPD PCKNIFSKAF SYLSHTIPDF
TDNCLINIMK CGEDFYATTE TNYIRKIDPQ TLETLEKVDY RKYVAVNLAT SHPHYDEAGN
VLNMGTSIAD KGGTKYVMFK IPATAPGSKK KGKNPLKHSE VFCSIPSRSL LSPSYYHSFG
VTENYVVFLE QPFKLDILKM ATAYMRGVSW ASCMTFCKED KTYIHIIDQK TRKPVPTKFY
TDPMVVFHHV NAYEEDGCVL FDVIAYEDNS LYQLFYLANL NKDFEEKSRL TSVPTLRRFA
VPLHVDKDAE VGSNLVKVSS TTATALKEKD DHVYCQPEVL YEGLELPRIN YAHNGKPYRY
IFAAEVQWSP VPTKILKYDV LTKSSLKWSE ESCWPAEPLF VPTPGAKDED DGVILSAIIS
TDPQKLPFLL ILDAKSFTEL ARASVDVDMH LDLHGLFIPD AGWNAVKQTP AKTQEDENSD
HPTGLTAPGL GHGENDFTAG HGGKSL