CCD1_ONCHC
ID CCD1_ONCHC Reviewed; 562 AA.
AC C3VEQ4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Carotenoid 9,10(9',10')-cleavage dioxygenase 1;
DE EC=1.14.99.n4;
DE AltName: Full=Carotenoid cleavage dioxygenase 1;
DE Short=OgCCD1;
GN Name=CCD1;
OS Oncidium hybrid cultivar (Orchid).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Epidendroideae; Cymbidieae; Oncidiinae; Oncidium.
OX NCBI_TaxID=141207;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20635095; DOI=10.1007/s00425-010-1222-x;
RA Chiou C.Y., Pan H.A., Chuang Y.N., Yeh K.W.;
RT "Differential expression of carotenoid-related genes determines diversified
RT carotenoid coloration in floral tissues of Oncidium cultivars.";
RL Planta 232:937-948(2010).
CC -!- FUNCTION: Cleaves a variety of carotenoids symmetrically at both the 9-
CC 10 and 9'-10' double bonds. Catalyzes the formation of 4,9-
CC dimethyldodeca-2,4,6,8,10-pentaene-1,12-dialdehyde and probably
CC hydroxydihydro-beta-ionone from zeaxanthin (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:20635095}.
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; EC=1.14.99.n4;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Probably on the
CC exterior surface of the plastids.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. Detected in roots and flower
CC buds. {ECO:0000269|PubMed:20635095}.
CC -!- MISCELLANEOUS: The carotenoid cleavage dioxygenase 1 (CCD1), which
CC catabolizes carotenoid metabolites, is up-regulated in the floral
CC tissues of the White Jade cultivar, resulting in a pure white flower.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; FJ859995; ACP27629.1; -; mRNA.
DR AlphaFoldDB; C3VEQ4; -.
DR SMR; C3VEQ4; -.
DR PRIDE; C3VEQ4; -.
DR GO; GO:0005737; C:cytoplasm; 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; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..562
FT /note="Carotenoid 9,10(9',10')-cleavage dioxygenase 1"
FT /id="PRO_0000426715"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 546
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 562 AA; 63412 MW; CA7DD67400693311 CRC64;
MGESASTETL EKKQPFTAEE EAADGKKSHR SVVAVQPKPR KGILSSTIDL IEKVIVYFAH
DSSKPLHYLT GNFAPVRDET PPFAALTVHG SLPVCLNGEF VRVGPNPKFS PVAGYHWFDG
DGMIHGLRIK DGKATYVSRY VKTSKLMQEE YFEGAKFMKI GDLKGLFGLF MVQMELLRAK
LKILDVSYGR STANTAMIYH HGKLLALSEG DKPYVIKVLE DGDLQTLGLL DYNKRLAHSF
TAHPKVDPFT DEMFTFGYSH TSPYITYRVI TKDGVMLNPV PITIPEPIMM HDFAITENYA
IFLDLPLYFR PKETIKGKLI FTFDPTKKAK FGVLPRYAKD EQLIRWFDLP NCFIFHNANA
WEDGDEVVLI TCRLKNIDLD LVNGAVKEKL ENFSNQLYEM RFNMKTGAAT QKELSAPMVD
FPRINENYTG RKQRYVYCTS FANIDKVNGI VKFDLHAEPE TGKKVLEVGG NVLGIFDLGP
GRFGSEAVFV PREAGTRVEE DDGYLIFFVY DETTGESKVY VIDAKTMSPE PVAVVDLPCR
VPYGFHAFFV NEEQIQKQQA EI