CCD8B_ORYSJ
ID CCD8B_ORYSJ Reviewed; 569 AA.
AC Q8LIY8; A0A0P0V860; Q0JJD5;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Carotenoid cleavage dioxygenase 8 homolog B, chloroplastic;
DE Short=OsCCD8b;
DE EC=1.13.11.69 {ECO:0000269|PubMed:22422982};
DE EC=1.13.11.70 {ECO:0000269|PubMed:18637791};
DE AltName: Full=Protein DWARF-10;
DE AltName: Full=Protein MAX4 homolog;
DE Flags: Precursor;
GN Name=CCD8B; Synonyms=D10; OrderedLocusNames=Os01g0746400, LOC_Os01g54270;
GN ORFNames=OSJNBa0014K08.38;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Shiokari;
RX PubMed=15659436; DOI=10.1093/pcp/pci022;
RA Ishikawa S., Maekawa M., Arite T., Onishi K., Takamure I., Kyozuka J.;
RT "Suppression of tiller bud activity in tillering dwarf mutants of rice.";
RL Plant Cell Physiol. 46:79-86(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY AUXIN,
RP MUTAGENESIS OF LEU-112, AND DISRUPTION PHENOTYPE.
RX PubMed=17655651; DOI=10.1111/j.1365-313x.2007.03210.x;
RA Arite T., Iwata H., Ohshima K., Maekawa M., Nakajima M., Kojima M.,
RA Sakakibara H., Kyozuka J.;
RT "DWARF10, an RMS1/MAX4/DAD1 ortholog, controls lateral bud outgrowth in
RT rice.";
RL Plant J. 51:1019-1029(2007).
RN [7]
RP CATALYTIC ACTIVITY.
RX PubMed=18637791; DOI=10.1042/bj20080568;
RA Alder A., Holdermann I., Beyer P., Al-Babili S.;
RT "Carotenoid oxygenases involved in plant branching catalyse a highly
RT specific conserved apocarotenoid cleavage reaction.";
RL Biochem. J. 416:289-296(2008).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Shiokari;
RX PubMed=18690207; DOI=10.1038/nature07272;
RA Umehara M., Hanada A., Yoshida S., Akiyama K., Arite T., Takeda-Kamiya N.,
RA Magome H., Kamiya Y., Shirasu K., Yoneyama K., Kyozuka J., Yamaguchi S.;
RT "Inhibition of shoot branching by new terpenoid plant hormones.";
RL Nature 455:195-200(2008).
RN [9]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Shiokari;
RX PubMed=19470589; DOI=10.1105/tpc.109.065987;
RA Lin H., Wang R., Qian Q., Yan M., Meng X., Fu Z., Yan C., Jiang B., Su Z.,
RA Li J., Wang Y.;
RT "DWARF27, an iron-containing protein required for the biosynthesis of
RT strigolactones, regulates rice tiller bud outgrowth.";
RL Plant Cell 21:1512-1525(2009).
RN [10]
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 [11]
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 the C(27)
CC 9-cis-10'-apo-beta-carotenal produced by CCD7. Produces the C(19)
CC carlactone and a C(8) hydroxyaldehyde. Also shows lower activity with
CC all-trans-10'-apo-beta-carotenal producing a C(9) dialdehyde and the
CC C(18) 13-apo-beta-carotenone. Strigolactones are hormones that inhibit
CC tillering and shoot branching through the MAX-dependent pathway,
CC contribute to the regulation of shoot architectural response to
CC phosphate-limiting conditions and function as rhizosphere signal that
CC stimulates hyphal branching of arbuscular mycorrhizal fungi and trigger
CC seed germination of root parasitic weeds. {ECO:0000269|PubMed:17655651,
CC ECO:0000269|PubMed:18690207}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-10'-apo-beta-carotenal + 2 O2 = (2E,4E,6E)-7-hydroxy-4-
CC methylhepta-2,4,6-trienal + carlactone; Xref=Rhea:RHEA:34403,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:67190, ChEBI:CHEBI:67191,
CC ChEBI:CHEBI:67192; EC=1.13.11.69;
CC Evidence={ECO:0000269|PubMed:22422982};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-10'-apo-beta-carotenal + O2 = (2E,4E,6E)-4-
CC methylocta-2,4,6-trienedial + 13-apo-beta-carotenone;
CC Xref=Rhea:RHEA:26401, ChEBI:CHEBI:15379, ChEBI:CHEBI:53153,
CC ChEBI:CHEBI:53175, ChEBI:CHEBI:53176; EC=1.13.11.70;
CC Evidence={ECO:0000269|PubMed:18637791};
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: Plastid, chloroplast
CC {ECO:0000269|PubMed:17655651}.
CC -!- TISSUE SPECIFICITY: Expressed in parenchyma cells of the root stele,
CC shoot apex, leaf buds, xylem parenchyma cells of the stem,
CC inflorescences and panicles. {ECO:0000269|PubMed:17655651}.
CC -!- INDUCTION: By auxin. {ECO:0000269|PubMed:17655651}.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype with increased branching and
CC tiller number, and strong reduction of the root levels of
CC strigolactones. {ECO:0000269|PubMed:15659436,
CC ECO:0000269|PubMed:17655651, ECO:0000269|PubMed:18690207,
CC ECO:0000269|PubMed:19470589, ECO:0000269|PubMed:23204501}.
CC -!- MISCELLANEOUS: The branching phenotypes of the ccd7/max3 and ccd8b/max4
CC mutants can be rescued by exogenous treatment with the synthetic
CC strigolactone analogs GR24 and 4BD. {ECO:0000305|PubMed:23204501}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; AP003376; BAC05598.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF06143.2; -; Genomic_DNA.
DR EMBL; AP014957; BAS74320.1; -; Genomic_DNA.
DR RefSeq; XP_015642760.1; XM_015787274.1.
DR AlphaFoldDB; Q8LIY8; -.
DR SMR; Q8LIY8; -.
DR STRING; 4530.OS01T0746400-00; -.
DR PaxDb; Q8LIY8; -.
DR PRIDE; Q8LIY8; -.
DR EnsemblPlants; Os01t0746400-01; Os01t0746400-01; Os01g0746400.
DR GeneID; 4326177; -.
DR Gramene; Os01t0746400-01; Os01t0746400-01; Os01g0746400.
DR KEGG; osa:4326177; -.
DR eggNOG; KOG1285; Eukaryota.
DR HOGENOM; CLU_016472_1_2_1; -.
DR InParanoid; Q8LIY8; -.
DR OMA; RAHGKVC; -.
DR OrthoDB; 895046at2759; -.
DR PlantReactome; R-OSA-5367729; Strigolactone biosynthesis.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q8LIY8; OS.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0102396; F:9-cis-10'-apo-beta-carotenal cleavage oxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0102251; F:all-trans-beta-apo-10'-carotenal cleavage oxygenase activity; IEA:UniProtKB-EC.
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; IMP: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..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..569
FT /note="Carotenoid cleavage dioxygenase 8 homolog B,
FT chloroplastic"
FT /id="PRO_0000422061"
FT REGION 23..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 251
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 558
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MUTAGEN 112
FT /note="L->P: In d10-1; dwarf and high tillering
FT phenotypes."
FT /evidence="ECO:0000269|PubMed:17655651"
SQ SEQUENCE 569 AA; 61984 MW; AE4E1A0327AEF869 CRC64;
MSPAMLQASS LCVSAALSGA ASRPGRLASQ GHQGKRAVAQ PLAASAVTEA APPAPVVAPP
ARPVDAPRRR GGRGGGGGGG ELVAWKSVRQ ERWEGALEVD GELPLWLDGT YLRNGPGLWN
LGDYGFRHLF DGYATLVRVS FRGGRAVGAH RQIESEAYKA ARAHGKVCYR EFSEVPKPDN
FLSYVGQLAT LFSGSSLTDN SNTGVVMLGD GRVLCLTETI KGSIQVDPDT LDTVGKFQYT
DKLGGLIHSA HPIVTDTEFW TLIPDLIRPG YVVARMDAGS NERQFVGRVD CRGGPAPGWV
HSFPVTEHYV VVPEMPLRYC AKNLLRAEPT PLYKFEWHLE SGSYMHVMCK ASGKIVASVE
VPPFVTFHFI NAYEETDEEG RVTAIIADCC EHNANTAILD KLRLHNLRSS SGQDVLPDAR
VGRFRIPLDG SQFGELETAL DPEEHGRGMD MCSINPAHVG REYRYAYACG ARRPCNFPNT
LTKVDLVERT AKNWHEEGSV PSEPFFVPRP GATEEDDGVA ISMVSAKDGS GYALVLDGKT
FEEVARAKFP YGLPYGLHCC WVPRKRNSK
