BCDO2_PONAB
ID BCDO2_PONAB Reviewed; 557 AA.
AC Q5RF16;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Carotenoid-cleaving dioxygenase, mitochondrial {ECO:0000250|UniProtKB:Q99NF1};
DE EC=1.13.11.- {ECO:0000250|UniProtKB:Q99NF1};
DE EC=1.13.11.71 {ECO:0000250|UniProtKB:Q99NF1};
DE AltName: Full=Beta-carotene dioxygenase 2 {ECO:0000250|UniProtKB:Q9BYV7};
GN Name=BCO2 {ECO:0000250|UniProtKB:Q9BYV7};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Broad specificity mitochondrial dioxygenase that mediates the
CC asymmetric oxidative cleavage of carotenoids. Cleaves carotenes (pure
CC hydrocarbon carotenoids) such as all-trans-beta-carotene and lycopene
CC as well as xanthophylls (oxygenated carotenoids) such as zeaxanthin,
CC lutein and beta-cryptoxanthin at both the 9,10 and the 9',10' carbon-
CC carbon double bond. Through its function in carotenoids metabolism
CC regulates oxidative stress and the production of important signaling
CC molecules. {ECO:0000250|UniProtKB:Q99NF1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-beta-carotene + O2 = all-trans-10'-apo-beta-
CC carotenal + beta-ionone; Xref=Rhea:RHEA:26389, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17579, ChEBI:CHEBI:32325, ChEBI:CHEBI:53153;
CC EC=1.13.11.71; Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26390;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-cis-lycopene + O2 = (3E,5E)-6,10-dimethylundeca-3,5,9-trien-
CC 2-one + 5-cis-10'-apo-lycopenal; Xref=Rhea:RHEA:68444,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:67207, ChEBI:CHEBI:177905,
CC ChEBI:CHEBI:177906; Evidence={ECO:0000250|UniProtKB:Q6QT07};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68445;
CC Evidence={ECO:0000250|UniProtKB:Q6QT07};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-lycopene + O2 = (3E,5E)-6,10-dimethylundeca-3,5,9-
CC trien-2-one + 13-cis-10'-apo-lycopenal; Xref=Rhea:RHEA:68448,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:67207, ChEBI:CHEBI:177907,
CC ChEBI:CHEBI:177908; Evidence={ECO:0000250|UniProtKB:Q6QT07};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68449;
CC Evidence={ECO:0000250|UniProtKB:Q6QT07};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lutein + O2 = (3R)-3-hydroxy-10'-apo-beta-carotenal + (3R,6R)-
CC hydroxy-alpha-ionone; Xref=Rhea:RHEA:68428, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28838, ChEBI:CHEBI:177902, ChEBI:CHEBI:177904;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68429;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lutein + O2 = (3R)-hydroxy-beta-ionone + (3R,6R)-3-hydroxy-
CC 10'-apo-alpha-carotenal; Xref=Rhea:RHEA:68432, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28838, ChEBI:CHEBI:53173, ChEBI:CHEBI:177903;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68433;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-zeaxanthin + 2 O2 = 2 (3R)-hydroxy-beta-ionone +
CC 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial; Xref=Rhea:RHEA:26393,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:53171,
CC ChEBI:CHEBI:53173; Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26394;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-zeaxanthin + O2 = (3R)-3-hydroxy-10'-apo-beta-
CC carotenal + (3R)-hydroxy-beta-ionone; Xref=Rhea:RHEA:68104,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:53173,
CC ChEBI:CHEBI:177902; Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68105;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-cryptoxanthin + O2 = (3R)-hydroxy-beta-ionone + all-
CC trans-10'-apo-beta-carotenal; Xref=Rhea:RHEA:68440,
CC ChEBI:CHEBI:10362, ChEBI:CHEBI:15379, ChEBI:CHEBI:53153,
CC ChEBI:CHEBI:53173; Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68441;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-10'-apo-beta-carotenal + O2 = 4,9-dimethyldodeca-
CC 2,4,6,8,10-pentaenedial + beta-ionone; Xref=Rhea:RHEA:68452,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32325, ChEBI:CHEBI:53153,
CC ChEBI:CHEBI:53171; Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68453;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxy-10'-apo-beta-carotenal + O2 = (3R)-hydroxy-
CC beta-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial;
CC Xref=Rhea:RHEA:68424, ChEBI:CHEBI:15379, ChEBI:CHEBI:53171,
CC ChEBI:CHEBI:53173, ChEBI:CHEBI:177902;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68425;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R,6R)-3-hydroxy-10'-apo-alpha-carotenal + O2 = (3R,6R)-
CC hydroxy-alpha-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial;
CC Xref=Rhea:RHEA:68436, ChEBI:CHEBI:15379, ChEBI:CHEBI:53171,
CC ChEBI:CHEBI:177903, ChEBI:CHEBI:177904;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68437;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q6QT07};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6QT07};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q99NF1}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; CR857345; CAH89641.1; -; mRNA.
DR AlphaFoldDB; Q5RF16; -.
DR SMR; Q5RF16; -.
DR STRING; 9601.ENSPPYP00000004443; -.
DR PRIDE; Q5RF16; -.
DR eggNOG; KOG1285; Eukaryota.
DR InParanoid; Q5RF16; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0010437; F:9,10 (9', 10')-carotenoid-cleaving dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0102076; F:beta,beta-carotene-9',10'-cleaving oxygenase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016121; P:carotene catabolic process; ISS:UniProtKB.
DR GO; GO:0062172; P:lutein catabolic process; ISS:UniProtKB.
DR GO; GO:1901176; P:lycopene catabolic process; ISS:UniProtKB.
DR GO; GO:0016124; P:xanthophyll catabolic process; ISS:UniProtKB.
DR GO; GO:1901826; P:zeaxanthin catabolic process; ISS:UniProtKB.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Lipid metabolism; Metal-binding; Mitochondrion;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..557
FT /note="Carotenoid-cleaving dioxygenase, mitochondrial"
FT /id="PRO_0000285999"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 263
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 334
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 551
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
SQ SEQUENCE 557 AA; 62867 MW; 5DF03713F922BFCE CRC64;
MVHRLPVFKR YMGNTPQKKA VFGQCRGLPC VAPLLTTVEE APRGISARVR GHFPKWLNGS
LLRTGPGKFE FGKDKYNHWF DGMALLHQFR MAKGTVTYRS KFLQSDTYKA NSAKNRIVIS
EFGTLALPDP CKNVFERFMS RFELPGKAAA MTDNTNVNYV RYKGDYYLCT ETNFMNKVDI
ETLEKTEKVD WSKFIAVNGA TAHPHYDPDG TAYNMGNSFG PYGFSYKVIR VPPEKVDLGE
TIHGAQVICS IASTEKGKPS YYHSFGMTRN YIIFIEQPLK MNLWKIATSK IRGKAFSDGI
SWEPQCNTWF HVVDKRTGQL LPGRYYSKPF VTFHQINAFE DQGCVIIDLC CQDNGRTLEV
YQLQNLRKAG EGLDQVYNSA AKSFPRRFVL PLNVSLNAPE GDNLSPLSYT SASAVKQADG
TIWCSHENLH QEDLEKEGGI EFPQIYYDQF SGKKYHFFYG CGFRHLVGGD SLIKVDVVNK
TLKVWREDGF YPSEPVFVPA PGTNEEDGGV ILSVVITPNQ NESNFLLVLD AKNFGELGRA
EVPVQMPYGF HGTFIPI
