ID   CCD1_PHAVU              Reviewed;         543 AA.
AC   Q94IR2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Carotenoid 9,10(9',10')-cleavage dioxygenase 1;
DE            EC=1.14.99.n4;
DE   AltName: Full=Neoxanthin cleavage enzyme NC2;
DE   AltName: Full=PvCCD1;
DE   AltName: Full=PvNCED2;
GN   Name=CCD1; Synonyms=NCED2;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=11316814; DOI=10.1074/jbc.m102146200;
RA   Schwartz S.H., Qin X., Zeevaart J.A.;
RT   "Characterization of a novel carotenoid cleavage dioxygenase from plants.";
RL   J. Biol. Chem. 276:25208-25211(2001).
RN   [2]
RP   INDUCTION.
RX   PubMed=10611388; DOI=10.1073/pnas.96.26.15354;
RA   Qin X., Zeevaart J.A.;
RT   "The 9-cis-epoxycarotenoid cleavage reaction is the key regulatory step of
RT   abscisic acid biosynthesis in water-stressed bean.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:15354-15361(1999).
CC   -!- FUNCTION: Cleaves a variety of carotenoids at the 9-10 and 9'-10'
CC       double bonds. Probably not involved in abscisic acid biosynthesis.
CC       {ECO:0000269|PubMed:11316814}.
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:11316814};
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   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:11316814}.
CC   -!- INDUCTION: Constitutively expressed in embryos.
CC       {ECO:0000269|PubMed:10611388}.
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR   EMBL; AY029525; AAK38744.1; -; mRNA.
DR   AlphaFoldDB; Q94IR2; -.
DR   SMR; Q94IR2; -.
DR   STRING; 3885.XP_007133813.1; -.
DR   eggNOG; KOG1285; Eukaryota.
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   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..543
FT                   /note="Carotenoid 9,10(9',10')-cleavage dioxygenase 1"
FT                   /id="PRO_0000285988"
FT   BINDING         224
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         528
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   543 AA;  61100 MW;  F22C9883A05325F7 CRC64;
     MGDDGKKNGA EGGLVKVDPK PTNGFSSKVI DLLEKLLVKF LYDSSLPHHY LTGNFGPVTE
     TPPTKDLPVK GHLPDCLNGE FVRVGPNPKF APVAGYHWFD GDGMIHGLRI KDGKATYVSR
     FVETSRLKQE EYFGRSKFMK IGDLKGLFGL LMVNIHMLRT KLKVLDLSYG GGTTNTALVY
     HHGKLLALSE ADKPYAIKVF EDGDLQTLGM LDYDKRLGHS FTAHPKVDPF TGEMFSFGYA
     HTPPYITYRV ISKDGYMHDP VPITISDPIM MHDFAITENY AVFMDLPLIF RPKEMVKNKT
     LIFSFDSTKK ARFGVLPRYA KDEQHIRWFE LPNCFIFHNA NAWEEEDEVV LITCRLQNPK
     LDNVGGTVQE KLENFSNELY EMRFNMKTGE ASQKKLSAST VDFPRVNENY TGRKQRYVYG
     TTLDSIAKVT GIIKFDLHAE PDHGKEKLEV GGNVQGLYDL GPGKFGSEAV YIPRVPGIES
     EEDDGYLVLF VHDENAGKSF VHVIDAKTMS ADPVAVVELP NRVPYGFHAF FVTEEQLQEQ
     AKL