CCD1_ARATH
ID CCD1_ARATH Reviewed; 538 AA.
AC O65572; Q8GRI2; Q9LY63;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Carotenoid 9,10(9',10')-cleavage dioxygenase 1;
DE EC=1.14.99.n4;
DE AltName: Full=AtCCD1;
DE AltName: Full=Neoxanthin cleavage enzyme NC1;
DE Short=AtNCED1;
GN Name=CCD1; Synonyms=NC1, NCED1; OrderedLocusNames=At3g63520;
GN ORFNames=MAA21_150;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY DROUGHT STRESS.
RC STRAIN=cv. Landsberg erecta;
RA Neill S.J., Burnett E.C., Desikan R., Hancock J.T.;
RT "Cloning of a wilt-responsive cDNA from an Arabidopsis thaliana suspension
RT culture cDNA library that encodes a putative 9-cis-epoxy-carotenoid
RT dioxygenase.";
RL J. Exp. Bot. 49:1893-1894(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-538.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12834401; DOI=10.1046/j.1365-313x.2003.01786.x;
RA Tan B.-C., Joseph L.M., Deng W.-T., Liu L., Li Q.-B., Cline K.,
RA McCarty D.R.;
RT "Molecular characterization of the Arabidopsis 9-cis epoxycarotenoid
RT dioxygenase gene family.";
RL Plant J. 35:44-56(2003).
RN [7]
RP REACTION MECHANISM.
RX PubMed=16459333; DOI=10.1074/jbc.m511668200;
RA Schmidt H., Kurtzer R., Eisenreich W., Schwab W.;
RT "The carotenase AtCCD1 from Arabidopsis thaliana is a dioxygenase.";
RL J. Biol. Chem. 281:9845-9851(2006).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16507088; DOI=10.1111/j.1365-313x.2006.02666.x;
RA Auldridge M.E., Block A., Vogel J.T., Dabney-Smith C., Mila I.,
RA Bouzayen M., Magallanes-Lundback M., DellaPenna D., McCarty D.R.,
RA Klee H.J.;
RT "Characterization of three members of the Arabidopsis carotenoid cleavage
RT dioxygenase family demonstrates the divergent roles of this multifunctional
RT enzyme family.";
RL Plant J. 45:982-993(2006).
CC -!- FUNCTION: Cleaves a variety of carotenoids symmetrically at both the 9-
CC 10 and 9'-10' double bonds. Active on beta,beta-carotene, lutein,
CC zeaxanthin, all-trans-violaxanthin, 9-cis-violaxanthin and 9'-cis-
CC neoxanthin. With most substrates, the carotenoid is symmetrically
CC cleaved. Probably not involved in abscisic acid biosynthesis.
CC {ECO:0000269|PubMed:11316814, ECO:0000269|PubMed:16507088}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12834401,
CC ECO:0000269|PubMed:16507088}. Note=On the exterior surface of the
CC plastids.
CC -!- TISSUE SPECIFICITY: High expression in flowers and siliques. Also
CC detected in stems, leaves and roots. {ECO:0000269|PubMed:16507088}.
CC -!- INDUCTION: By drought stress. {ECO:0000269|Ref.1}.
CC -!- DISRUPTION PHENOTYPE: Plants do not show any phenotype alteration, but
CC leads to higher seed carotenoid content. {ECO:0000269|PubMed:16507088}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN17413.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AJ005813; CAA06712.1; -; mRNA.
DR EMBL; AL163818; CAB87805.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80498.1; -; Genomic_DNA.
DR EMBL; BT000436; AAN17413.1; ALT_INIT; mRNA.
DR EMBL; BT002102; AAN72113.1; -; mRNA.
DR PIR; T49193; T49193.
DR PIR; T51734; T51734.
DR RefSeq; NP_191911.1; NM_116217.3.
DR AlphaFoldDB; O65572; -.
DR SMR; O65572; -.
DR STRING; 3702.AT3G63520.1; -.
DR iPTMnet; O65572; -.
DR PaxDb; O65572; -.
DR PRIDE; O65572; -.
DR ProteomicsDB; 222792; -.
DR EnsemblPlants; AT3G63520.1; AT3G63520.1; AT3G63520.
DR GeneID; 825527; -.
DR Gramene; AT3G63520.1; AT3G63520.1; AT3G63520.
DR KEGG; ath:AT3G63520; -.
DR Araport; AT3G63520; -.
DR TAIR; locus:2087418; AT3G63520.
DR eggNOG; KOG1285; Eukaryota.
DR HOGENOM; CLU_016472_0_0_1; -.
DR OMA; WGARTLM; -.
DR OrthoDB; 524712at2759; -.
DR PhylomeDB; O65572; -.
DR BioCyc; MetaCyc:AT3G63520-MON; -.
DR PRO; PR:O65572; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O65572; baseline and differential.
DR Genevisible; O65572; AT.
DR GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0045549; F:9-cis-epoxycarotenoid dioxygenase activity; IDA:TAIR.
DR GO; GO:0010436; F:carotenoid dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016121; P:carotene catabolic process; IMP:TAIR.
DR GO; GO:0016118; P:carotenoid catabolic process; IDA:TAIR.
DR GO; GO:0016124; P:xanthophyll catabolic process; IMP:TAIR.
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;
KW Reference proteome; Stress response.
FT CHAIN 1..538
FT /note="Carotenoid 9,10(9',10')-cleavage dioxygenase 1"
FT /id="PRO_0000285987"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 523
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="S -> I (in Ref. 1; CAA06712 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="V -> I (in Ref. 1; CAA06712 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 60908 MW; FB205D1AA77B70A6 CRC64;
MAEKLSDGSS IISVHPRPSK GFSSKLLDLL ERLVVKLMHD ASLPLHYLSG NFAPIRDETP
PVKDLPVHGF LPECLNGEFV RVGPNPKFDA VAGYHWFDGD GMIHGVRIKD GKATYVSRYV
KTSRLKQEEF FGAAKFMKIG DLKGFFGLLM VNVQQLRTKL KILDNTYGNG TANTALVYHH
GKLLALQEAD KPYVIKVLED GDLQTLGIID YDKRLTHSFT AHPKVDPVTG EMFTFGYSHT
PPYLTYRVIS KDGIMHDPVP ITISEPIMMH DFAITETYAI FMDLPMHFRP KEMVKEKKMI
YSFDPTKKAR FGVLPRYAKD ELMIRWFELP NCFIFHNANA WEEEDEVVLI TCRLENPDLD
MVSGKVKEKL ENFGNELYEM RFNMKTGSAS QKKLSASAVD FPRINECYTG KKQRYVYGTI
LDSIAKVTGI IKFDLHAEAE TGKRMLEVGG NIKGIYDLGE GRYGSEAIYV PRETAEEDDG
YLIFFVHDEN TGKSCVTVID AKTMSAEPVA VVELPHRVPY GFHALFVTEE QLQEQTLI
