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Database: UniProt
Entry: H3D2G9_TETNG
LinkDB: H3D2G9_TETNG
Original site: H3D2G9_TETNG 
ID   H3D2G9_TETNG            Unreviewed;       521 AA.
AC   H3D2G9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Carotenoid-cleaving dioxygenase, mitochondrial {ECO:0000256|ARBA:ARBA00040536};
DE            EC=1.13.11.71 {ECO:0000256|ARBA:ARBA00038847};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000014707.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000014707.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   AlphaFoldDB; H3D2G9; -.
DR   STRING; 99883.ENSTNIP00000014707; -.
DR   Ensembl; ENSTNIT00000014907.1; ENSTNIP00000014707.1; ENSTNIG00000011755.1.
DR   GeneTree; ENSGT00950000182913; -.
DR   HOGENOM; CLU_016472_1_1_1; -.
DR   InParanoid; H3D2G9; -.
DR   OMA; HEMTIDI; -.
DR   TreeFam; TF314019; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
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; IEA:InterPro.
DR   InterPro; IPR004294; Carotenoid_Oase.
DR   PANTHER; PTHR10543:SF122; BETA,BETA-CAROTENE 9',10'-OXYGENASE; 1.
DR   PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 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:UP000007303}.
FT   BINDING         173
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         233
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         304
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         516
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   521 AA;  59445 MW;  D1CFF333D9412E1D CRC64;
     GLETIAPLVR SVEETPEPIS TEVQGTIPSW IHGNLLRNGP GKFEFGNRHY NHWFDGMAML
     HQFRISEGRV TYMSRFLHSD VYKKNSEQDR IVMSEFGTLA LPDPCKNVFQ RFLSRFEMIE
     PTDNASVNFV KYKGDYYVST ETNFMHRVDP ENLETLEKVD WSKFVAVNGA TAHPHYDPDG
     TSYNMGNSYG RKGALYNIIR VPPEKSEATE TLHGAKVLCS IVPQHKSRPS YYHSFAMSEN
     YVVFIEQPIK MDLLKIVTCR LRGRALCEGI YWDGGQDTVF HLVSKHTGEV STVKYHTKAF
     ATFHQINAFE EDGFLMIDLC CSDNGQAINN YLIQNLRKSG EALDEVYNST GRAFPRRFVL
     PLHVTSQTAA GHNLNTRETC VKTDKDTVFC QHEDLHGDDL LEFGGLEFPQ INYGRCNTKP
     YRYFYGCGFR HLVGDSLLKM DLKDKTFKLQ RPAGALRWTP VTLVFTPHSR QRVVGCLQKR
     LLTSTDDLCL FRQVLDGRLP ELGRANVPVN MPYGFHGIYE A
//
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