BCDO2_MACFA
ID BCDO2_MACFA Reviewed; 556 AA.
AC Q8HXG8;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 70.
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}; ORFNames=QmoA-15570;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Medulla oblongata;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (DEC-2002) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41782.1; Type=Erroneous initiation; Evidence={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; AB097557; BAC41782.1; ALT_INIT; mRNA.
DR RefSeq; NP_001271880.1; NM_001284951.1.
DR AlphaFoldDB; Q8HXG8; -.
DR SMR; Q8HXG8; -.
DR STRING; 9541.XP_005579693.1; -.
DR GeneID; 102136772; -.
DR CTD; 83875; -.
DR eggNOG; KOG1285; Eukaryota.
DR OrthoDB; 895046at2759; -.
DR Proteomes; UP000233100; 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:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; ISS:UniProtKB.
DR GO; GO:0016121; P:carotene catabolic process; ISS:UniProtKB.
DR GO; GO:0016119; P:carotene metabolic 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..556
FT /note="Carotenoid-cleaving dioxygenase, mitochondrial"
FT /id="PRO_0000143938"
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 550
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
SQ SEQUENCE 556 AA; 62966 MW; 2A7BD970DE2AE6A6 CRC64;
MVHPLPVFKR YTGNTHQKKA IFGQCRGLPC VAPLLTTVEE APRGISARVW GHFPKWLNGS
LLRIGPGKFE FGKDKYNHWF DGMALLHQFR MAKGTVTYRS KFLQSDTYKA NSAKNRIVMS
EFGTLATPDP CKNVFERFMS RFELPGKAAA MTDNTNVNYV RYKGDYYLCT ETNFMNKVDI
ETLEKTEKVD WSKFIAVNGA TAHPHYDPDG TAYNMGNSFG PFGFSYKVIR VPPEKVDLEE
TTHGAQVICS IAPTEKGKPS YYHSFGMTRN YIIFIEQPLK MNLWKIATSK IRGKAFSDGI
SWEPQCNTRF HVVDKHTGQL LPGRYYSKPF VAFHHINAFE DQGCVIIDLC CQDNGRILEV
YQLQNLRKAG EELDQVYNSA GRSFPRRFVL PLNVSLNAPE GDNLSPLSYT SASAVKQADG
TIWCSHENLH QEDLEKEGGI EFPQIYYGQF SGKKYRFFYG CGFRHLVGDS LIKVDVVNKT
LKVWREDGFY PSEPVFVPVP GTNEEDGGVI LSVVITPNQN ESNFLLVLDA KNFEELGRAE
VPVQMPYGFH GTFIPI
