ID A0A2I3HLK5_NOMLE Unreviewed; 578 AA.
AC A0A2I3HLK5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Carotenoid-cleaving dioxygenase, mitochondrial {ECO:0000256|ARBA:ARBA00040536};
DE EC=1.13.11.71 {ECO:0000256|ARBA:ARBA00038847};
GN Name=BCO2 {ECO:0000313|Ensembl:ENSNLEP00000044392.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000044392.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000044392.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000044392.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036952};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68425;
CC Evidence={ECO:0000256|ARBA:ARBA00036952};
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:0000256|ARBA:ARBA00036274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68437;
CC Evidence={ECO:0000256|ARBA:ARBA00036274};
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:0000256|ARBA:ARBA00036158};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68449;
CC Evidence={ECO:0000256|ARBA:ARBA00036158};
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:0000256|ARBA:ARBA00036646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68445;
CC Evidence={ECO:0000256|ARBA:ARBA00036646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-10'-apo-beta-carotenal + O2 = 4,9-
CC dimethyldodeca-2,4,6,8,10-pentaenedial + beta-ionone;
CC Xref=Rhea:RHEA:68452, ChEBI:CHEBI:15379, ChEBI:CHEBI:32325,
CC ChEBI:CHEBI:53153, ChEBI:CHEBI:53171;
CC Evidence={ECO:0000256|ARBA:ARBA00036783};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68453;
CC Evidence={ECO:0000256|ARBA:ARBA00036783};
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:0000256|ARBA:ARBA00036788};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26390;
CC Evidence={ECO:0000256|ARBA:ARBA00036788};
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:0000256|ARBA:ARBA00036423};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26394;
CC Evidence={ECO:0000256|ARBA:ARBA00036423};
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:0000256|ARBA:ARBA00035797};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68105;
CC Evidence={ECO:0000256|ARBA:ARBA00035797};
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:0000256|ARBA:ARBA00036195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68441;
CC Evidence={ECO:0000256|ARBA:ARBA00036195};
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:0000256|ARBA:ARBA00036209};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68429;
CC Evidence={ECO:0000256|ARBA:ARBA00036209};
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:0000256|ARBA:ARBA00036885};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68433;
CC Evidence={ECO:0000256|ARBA:ARBA00036885};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006787, ECO:0000256|RuleBase:RU003799}.
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DR EMBL; ADFV01056567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01056568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3HLK5; -.
DR STRING; 61853.ENSNLEP00000044392; -.
DR Ensembl; ENSNLET00000056575.1; ENSNLEP00000044392.1; ENSNLEG00000036150.1.
DR GeneTree; ENSGT00950000182913; -.
DR InParanoid; A0A2I3HLK5; -.
DR OMA; WKSVRQE; -.
DR Proteomes; UP000001073; Chromosome 15.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0102076; F:beta,beta-carotene-9',10'-cleaving oxygenase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016121; P:carotene catabolic process; IEA:Ensembl.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0042574; P:retinal metabolic process; IEA:Ensembl.
DR GO; GO:0016124; P:xanthophyll catabolic process; IEA:Ensembl.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR PANTHER; PTHR10543:SF122; CAROTENOID-CLEAVING DIOXYGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF03055; RPE65; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604294-1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..578
FT /note="Carotenoid-cleaving dioxygenase, mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014157501"
FT BINDING 225
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 285
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 356
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 572
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 578 AA; 65455 MW; AAFFFC0A526C0795 CRC64;
FFRVFLHFIR SLSATAVDFL PVMAHRLPVF KRYLRNTHQK KAVFGQCRGL PCVAPLLTTV
EEAPRGISAR VWGHFPKWLN GSLLRIGPGK FEFGKDKYNH WFDGMALLHQ FRMAKGTVTY
RSKFLQSDTY KANSAKNRIV ISEFGTLALP DPCKNVFERF MSRFELPGKA AAMTDNTNVN
YVRYKGDYYL CTETNFMNKV DIETLEKTEK VDWSKFIAVN GATAHPHYDP DGTAYNMGNS
FGPYGFSYKV IRVPPEKVDL GETIHGAQVI CSIASTEKGK PSYYHSFGMT RNYIIFIEQP
LKMNLWKIAT SKIRGKAFSD GISWEPQCNT RFHVVDKCTG QLLPGRYYSK PFVTFHQINA
FEDQGCVIID LCCQDNGRTL EVYQLQNLRK AGEGLDQVYN SAAKSFPRRF VLPLNVSLNA
PEGDNLSPLS YTSASAVKQA DGTIWCSHEN LHQEDLEKEG GIEFPQIYYG QFNGKKYHFF
YGCGFRHLVG DSLIKVDVVN KTLKVWREDG FYPSEPVFVP APGTSEEDGG IILSVVITPN
QNESNFLLVL DAKNFEELGR AEVPVQMPYG FHGTFIPI
//
