ID A0A3M0IU65_HIRRU Unreviewed; 588 AA.
AC A0A3M0IU65;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Carotenoid-cleaving dioxygenase, mitochondrial {ECO:0000256|ARBA:ARBA00040536};
DE EC=1.13.11.71 {ECO:0000256|ARBA:ARBA00038847};
GN ORFNames=DUI87_31507 {ECO:0000313|EMBL:RMB91978.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB91978.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMB91978.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMB91978.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMB91978.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMB91978.1}.
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DR EMBL; QRBI01000231; RMB91978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0IU65; -.
DR STRING; 333673.A0A3M0IU65; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 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:UP000269221}.
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 282
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 353
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 582
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 588 AA; 66245 MW; 1E136901525DE9CA CRC64;
MFAEILLSSA SFLLAHLLHF LCSLMRFIPG FKNYLPSPSK EQILRHRPRG LQCISPLVQS
VEETPEPIPA RVKGHIPKWI NGNLLRNGPG KFEFGNDKFN HWFDGMALLH QFQLAHGTVT
YRSRFLRSSS YLRNSQHNRI VASEFGTLAM PDPCKSLFGR FLSRFEPLQP SDNCNVNYVL
YKGDYYVSNE NVFMHKVDPE TLETKEKVDW SKFIAVNGAT AHPHYESDGT TYNMGNSYGK
HGSSYNIIKV PPQEPGRGDT LEGAEVLCSI PPMDRAKPSY YHSFGMTENY IVFIEQPLRL
NLLKIITSKL CGKAIYDGIS WEPQHNTYFH VVDKHTGKVL PGQWCSKPFV TFHQINAFEE
RGCVVLDLCC QDEGTSLALY TLQNLRRSGE GLDQVYASVP RAFPRRFVLP LDVDPDTPVG
KNLNPLPYSQ AKAVRGADGK VWCTHEDLHP EGFEKVGGLE FPQINYSRYN GRRYRYFYGC
GFGNLVGDSL IKVDVETKNF KVSSPSPSTE VDLKIWQEEG CYPSEPVFVP VPNATAEDSG
VILSVVVSPT EDQSAFLLVL DAETFRELGR AEVGVPMPYG FHGVFTAR
//
