ID   CCD_CROSA               Reviewed;         546 AA.
AC   Q84KG5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Carotenoid 9,10(9',10')-cleavage dioxygenase;
DE            EC=1.14.99.n4;
DE   AltName: Full=CsCCD;
GN   Name=CCD;
OS   Crocus sativus (Saffron).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Iridaceae;
OC   Crocoideae; Croceae; Crocus.
OX   NCBI_TaxID=82528;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=12509521; DOI=10.1105/tpc.006536;
RA   Bouvier F., Suire C., Mutterer J., Camara B.;
RT   "Oxidative remodeling of chromoplast carotenoids: identification of the
RT   carotenoid dioxygenase CsCCD and CsZCD genes involved in Crocus secondary
RT   metabolite biogenesis.";
RL   Plant Cell 15:47-62(2003).
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.
CC       {ECO:0000269|PubMed:12509521}.
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         Evidence={ECO:0000269|PubMed:12509521};
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:0000269|PubMed:12509521}.
CC   -!- TISSUE SPECIFICITY: In vegetative and floral tissues.
CC       {ECO:0000269|PubMed:12509521}.
CC   -!- INDUCTION: Constitutively expressed at low level in all tissues.
CC       {ECO:0000269|PubMed:12509521}.
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {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; AJ132927; CAC79592.1; -; mRNA.
DR   AlphaFoldDB; Q84KG5; -.
DR   SMR; Q84KG5; -.
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   1: Evidence at protein level;
KW   Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..546
FT                   /note="Carotenoid 9,10(9',10')-cleavage dioxygenase"
FT                   /id="PRO_0000282606"
FT   BINDING         226
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         340
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         530
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   546 AA;  61697 MW;  5267DA28454189D4 CRC64;
     MGEVAKEEVE ERRSIVAVNP QPSKGLVSSA VDLIEKAVVY LFHDKSKPCH YLSGNFAPVV
     DETPPCPDLP VRGHLPECLN GEFVRVGPNP KFMPVAGYHW FDGDGMIHGM RIKDGKATYA
     SRYVKTSRLK QEEYFEGPKF MKIGDLKGFF GLFMVQMQLL RAKLKVIDVS YGVGTGNTAL
     IYHHGKLLAL SEADKPYVVK VLEDGDLQTL GLLDYDKRLS HSFTAHPKVD PFTDEMFTFG
     YAHTPPYVTY RVISKDGVMR DPVPITIPAS VMMHDFAITE NYSIFMDLPL YFQPKEMVKG
     GKLIFSFDAT KKARFGVLPR YAKDDSLIRW FELPNCFIFH NANAWEEGDE VVLITCRLEN
     PDLDMVNGAV KEKLENFKNE LYEMRFNMKT GAASQKQLSV SAVDFPRINE SYTTRKQRYV
     YGTILDNITK VKGIIKFDLH AEPEAGKKKL EVGGNVQGIF DLGPGRYGSE AVFVPRERGI
     KSEEDDGYLI FFVHDENTGK SEVNVIDAKT MSAEPVAVVE LPNRVPYGFH AFFVNEEQLQ
     WQQTDV