CCD7_ARATH
ID CCD7_ARATH Reviewed; 618 AA.
AC Q7XJM2; F4IV47; Q0WMG3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Carotenoid cleavage dioxygenase 7, chloroplastic;
DE Short=AtCCD7;
DE AltName: Full=AtNCED7;
DE AltName: Full=Beta,beta-carotene 9',10'-oxygenase;
DE EC=1.13.11.68;
DE AltName: Full=Protein MORE AXILLARY BRANCHING 3;
DE AltName: Full=Protein MORE AXILLARY GROWTH 3;
DE Flags: Precursor;
GN Name=CCD7; Synonyms=MAX3, NCED7; OrderedLocusNames=At2g44990;
GN ORFNames=T14P1.21;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-254.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15268852; DOI=10.1016/j.cub.2004.06.061;
RA Booker J., Auldridge M., Wills S., McCarty D., Klee H., Leyser O.;
RT "MAX3/CCD7 is a carotenoid cleavage dioxygenase required for the synthesis
RT of a novel plant signaling molecule.";
RL Curr. Biol. 14:1232-1238(2004).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=15342640; DOI=10.1074/jbc.m409004200;
RA Schwartz S.H., Qin X., Loewen M.C.;
RT "The biochemical characterization of two carotenoid cleavage enzymes from
RT Arabidopsis indicates that a carotenoid-derived compound inhibits lateral
RT branching.";
RL J. Biol. Chem. 279:46940-46945(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE 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).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=21243360; DOI=10.1007/s00299-010-0999-1;
RA Liang Y.S., Jeon Y.A., Lim S.H., Kim J.K., Lee J.Y., Kim Y.M., Lee Y.H.,
RA Ha S.H.;
RT "Vascular-specific activity of the Arabidopsis carotenoid cleavage
RT dioxygenase 7 gene promoter.";
RL Plant Cell Rep. 30:973-980(2011).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=22422982; DOI=10.1126/science.1218094;
RA Alder A., Jamil M., Marzorati M., Bruno M., Vermathen M., Bigler P.,
RA Ghisla S., Bouwmeester H., Beyer P., Al-Babili S.;
RT "The path from beta-carotene to carlactone, a strigolactone-like plant
RT hormone.";
RL Science 335:1348-1351(2012).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=23204501; DOI=10.1093/mp/sss138;
RA Fukui K., Ito S., Asami T.;
RT "Selective mimics of strigolactone actions and their potential use for
RT controlling damage caused by root parasitic weeds.";
RL Mol. Plant 6:88-99(2013).
CC -!- FUNCTION: Involved in strigolactones biosynthesis by cleaving
CC asymmetrically a variety of linear and cyclic carotenoids at the 9-10
CC double bond. Produces one C(13) beta-ionone and the C(27) 10'-apo-beta-
CC carotenal. Strigolactones are hormones that inhibit tillering and shoot
CC branching through the MAX-dependent pathway, contribute to the
CC regulation of shoot architectural response to phosphate-limiting
CC conditions and function as rhizosphere signal that stimulates hyphal
CC branching of arbuscular mycorrhizal fungi and trigger seed germination
CC of root parasitic weeds. No activity on lycopene, lutein, zeaxanthin,
CC violaxanthin or neoxanthin. Probably not involved in abscisic acid
CC biosynthesis. {ECO:0000269|PubMed:15268852,
CC ECO:0000269|PubMed:16507088}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-beta-carotene + O2 = 9-cis-10'-apo-beta-carotenal +
CC beta-ionone; Xref=Rhea:RHEA:34399, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32325, ChEBI:CHEBI:67188, ChEBI:CHEBI:67192;
CC EC=1.13.11.68; Evidence={ECO:0000269|PubMed:22422982};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.2 uM for beta-carotene {ECO:0000269|PubMed:15342640};
CC Vmax=4.5 pmol/min/mg enzyme {ECO:0000269|PubMed:15342640};
CC Note=addition of methanol to in vitro assays has a strong stimulatory
CC effect.;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15268852, ECO:0000269|PubMed:16507088}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, siliques, inflorescence
CC stems, petiole, leaves and roots. {ECO:0000269|PubMed:15268852,
CC ECO:0000269|PubMed:16507088, ECO:0000269|PubMed:21243360}.
CC -!- DISRUPTION PHENOTYPE: Increased shoot branching.
CC {ECO:0000269|PubMed:15342640, ECO:0000269|PubMed:23204501}.
CC -!- MISCELLANEOUS: The branching phenotypes of the max1, ccd7/max3 and
CC ccd8/max4 mutants can be rescued by exogenous treatment with the
CC synthetic strigolactone analogs GR24 and 4BD.
CC {ECO:0000305|PubMed:23204501}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF01693.1; Type=Miscellaneous discrepancy; Note=Introns retention.; Evidence={ECO:0000305};
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DR EMBL; CP002685; AEC10494.2; -; Genomic_DNA.
DR EMBL; AK229864; BAF01693.1; ALT_SEQ; mRNA.
DR PIR; C84885; C84885.
DR RefSeq; NP_001318427.1; NM_001337111.1.
DR AlphaFoldDB; Q7XJM2; -.
DR SMR; Q7XJM2; -.
DR STRING; 3702.AT2G44990.1; -.
DR PaxDb; Q7XJM2; -.
DR PRIDE; Q7XJM2; -.
DR EnsemblPlants; AT2G44990.1; AT2G44990.1; AT2G44990.
DR GeneID; 819107; -.
DR Gramene; AT2G44990.1; AT2G44990.1; AT2G44990.
DR KEGG; ath:AT2G44990; -.
DR Araport; AT2G44990; -.
DR eggNOG; KOG1285; Eukaryota.
DR HOGENOM; CLU_016472_6_1_1; -.
DR InParanoid; Q7XJM2; -.
DR OMA; EGGQPYE; -.
DR PhylomeDB; Q7XJM2; -.
DR BioCyc; ARA:AT2G44990-MON; -.
DR BioCyc; MetaCyc:AT2G44990-MON; -.
DR BRENDA; 1.13.11.68; 399.
DR BRENDA; 1.13.11.71; 399.
DR SABIO-RK; Q7XJM2; -.
DR PRO; PR:Q7XJM2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7XJM2; baseline and differential.
DR Genevisible; Q7XJM2; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102395; F:9-cis-beta-carotene 9',10'-cleavage oxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0045549; F:9-cis-epoxycarotenoid dioxygenase activity; IBA:GO_Central.
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:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:UniProtKB.
DR GO; GO:0016121; P:carotene catabolic process; IDA:UniProtKB.
DR GO; GO:0010223; P:secondary shoot formation; IMP:UniProtKB.
DR GO; GO:1901601; P:strigolactone biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 32..618
FT /note="Carotenoid cleavage dioxygenase 7, chloroplastic"
FT /id="PRO_0000285996"
FT REGION 11..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 612
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 618 AA; 69453 MW; 28CFDABAD5E3C485 CRC64;
MSLPIPPKFL PPLKSPPIHH HQTPPPLAPP RAAISISIPD TGLGRTGTIL DESTSSAFRD
YQSLFVSQRS ETIEPVVIKP IEGSIPVNFP SGTYYLAGPG LFTDDHGSTV HPLDGHGYLR
AFHIDGNKRK ATFTAKYVKT EAKKEEHDPV TDTWRFTHRG PFSVLKGGKR FGNTKVMKNV
ANTSVLKWAG RLLCLWEGGE PYEIESGSLD TVGRFNVENN GCESCDDDDS SDRDLSGHDI
WDTAADLLKP ILQGVFKMPP KRFLSHYKVD GRRKRLLTVT CNAEDMLLPR SNFTFCEYDS
EFKLIQTKEF KIDDHMMIHD WAFTDTHYIL FANRVKLNPI GSIAAMCGMS PMVSALSLNP
SNESSPIYIL PRFSDKYSRG GRDWRVPVEV SSQLWLIHSG NAYETREDNG DLKIQIQASA
CSYRWFDFQK MFGYDWQSNK LDPSVMNLNR GDDKLLPHLV KVSMTLDSTG NCNSCDVEPL
NGWNKPSDFP VINSSWSGKK NKYMYSAASS GTRSELPHFP FDMVVKFDLD SNLVRTWSTG
ARRFVGEPMF VPKNSVEEGE EEDDGYIVVV EYAVSVERCY LVILDAKKIG ESDAVVSRLE
VPRNLTFPMG FHGLWASD
