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 16-JUN-2009, entry version 40. DE RecName: Full=Beta,beta-carotene 15,15'-monooxygenase; DE EC=1.14.99.36; DE AltName: Full=Beta-carotene dioxygenase 1; GN Name=Bcmo1; Synonyms=Bcdo, Bcdo1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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 CC of retinal. The reaction proceeds in three stages, epoxidation of CC the 15,15'-double bond, hydration of the double bond leading to CC ring opening, and oxidative cleavage of the diol formed (By CC similarity). CC -!- CATALYTIC ACTIVITY: Beta-carotene + O(2) = 2 retinal. CC -!- COFACTOR: Iron (By similarity). CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB062912; BAB60807.1; -; mRNA. DR IPI; IPI00208162; -. DR RefSeq; NP_446100.1; -. DR UniGene; Rn.126587; -. DR PRIDE; Q91XT5; -. DR Ensembl; ENSRNOG00000012027; Rattus norvegicus. DR GeneID; 114106; -. DR KEGG; rno:114106; -. DR RGD; 70981; Bcmo1. DR HOVERGEN; Q91XT5; -. DR BRENDA; 1.14.99.36; 248. DR NextBio; 618281; -. DR ArrayExpress; Q91XT5; -. DR GermOnline; ENSRNOG00000012027; Rattus norvegicus. DR GO; GO:0003834; F:beta-carotene 15,15'-monooxygenase activity; IDA:RGD. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR004294; Carotenoid_Oase. DR PANTHER; PTHR10543; Carotenoid_Oase; 1. DR Pfam; PF03055; RPE65; 1. PE 2: Evidence at transcript level; KW Dioxygenase; Iron; Oxidoreductase. FT CHAIN 1 566 Beta,beta-carotene 15,15'-monooxygenase. FT /FTId=PRO_0000143935. 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 //