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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}.
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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
 
 
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