NCED1_ORYSJ
ID NCED1_ORYSJ Reviewed; 638 AA.
AC Q6YVJ0; Q7XXP8;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=9-cis-epoxycarotenoid dioxygenase NCED1, chloroplastic {ECO:0000305};
DE Short=OsNCED1 {ECO:0000312|EMBL:AAW21317.1};
DE EC=1.13.11.51 {ECO:0000250|UniProtKB:O24592};
DE Flags: Precursor;
GN Name=NCED1 {ECO:0000312|EMBL:AAW21317.1};
GN OrderedLocusNames=Os02g0704000 {ECO:0000312|EMBL:BAF09772.1},
GN LOC_Os02g47510 {ECO:0000305};
GN ORFNames=P0724B10.24 {ECO:0000312|EMBL:BAD08075.1};
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 [MRNA].
RA Dian W.M.;
RT "Oryza sativa japonica group 9-cis-epoxycarotenoid dioxygenase 1 (NCED1)
RT mRNA.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-323.
RC TISSUE=Panicle;
RX PubMed=15659629; DOI=10.1105/tpc.104.028456;
RA Moriguchi K., Suzuki T., Ito Y., Yamazaki Y., Niwa Y., Kurata N.;
RT "Functional isolation of novel nuclear proteins showing a variety of
RT subnuclear localizations.";
RL Plant Cell 17:389-403(2005).
RN [7]
RP INDUCTION.
RX PubMed=17205969; DOI=10.1093/pcp/pcm003;
RA Saika H., Okamoto M., Miyoshi K., Kushiro T., Shinoda S., Jikumaru Y.,
RA Fujimoto M., Arikawa T., Takahashi H., Ando M., Arimura S., Miyao A.,
RA Hirochika H., Kamiya Y., Tsutsumi N., Nambara E., Nakazono M.;
RT "Ethylene promotes submergence-induced expression of OsABA8ox1, a gene that
RT encodes ABA 8'-hydroxylase in rice.";
RL Plant Cell Physiol. 48:287-298(2007).
RN [8]
RP INDUCTION BY GLUCOSE.
RX PubMed=19208695; DOI=10.1093/pcp/pcp022;
RA Zhu G., Ye N., Zhang J.;
RT "Glucose-induced delay of seed germination in rice is mediated by the
RT suppression of ABA catabolism rather than an enhancement of ABA
RT biosynthesis.";
RL Plant Cell Physiol. 50:644-651(2009).
RN [9]
RP INDUCTION BY DROUGHT STRESS.
RX PubMed=25735958; DOI=10.1093/pcp/pcv022;
RA Shi L., Guo M., Ye N., Liu Y., Liu R., Xia Y., Cui S., Zhang J.;
RT "Reduced ABA accumulation in the root system is caused by ABA exudation in
RT upland rice (Oryza sativa L. var. Gaoshan1) and this enhanced drought
RT adaptation.";
RL Plant Cell Physiol. 56:951-964(2015).
CC -!- FUNCTION: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity.
CC Catalyzes the first step of abscisic-acid biosynthesis from
CC carotenoids. {ECO:0000250|UniProtKB:O24592}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a
CC 12'-apo-carotenal; Xref=Rhea:RHEA:23328, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32304, ChEBI:CHEBI:51972, ChEBI:CHEBI:51973;
CC EC=1.13.11.51; Evidence={ECO:0000250|UniProtKB:O24592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-violaxanthin + O2 = (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-
CC dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-xanthoxin;
CC Xref=Rhea:RHEA:16541, ChEBI:CHEBI:15379, ChEBI:CHEBI:32304,
CC ChEBI:CHEBI:34597, ChEBI:CHEBI:35305; EC=1.13.11.51;
CC Evidence={ECO:0000250|UniProtKB:O24592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9'-cis-neoxanthin + O2 = (3S,5R,6R)-3,5-dihydroxy-6,7-
CC didehydro-5,6-dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-
CC xanthoxin; Xref=Rhea:RHEA:19677, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32304, ChEBI:CHEBI:34596, ChEBI:CHEBI:35306;
CC EC=1.13.11.51; Evidence={ECO:0000250|UniProtKB:O24592};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O24592};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:O24592};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- INDUCTION: Induced by glucose (PubMed:19208695). Induced by drought
CC stress (PubMed:25735958). Down-regulated by submergence
CC (PubMed:17205969). {ECO:0000269|PubMed:17205969,
CC ECO:0000269|PubMed:19208695, ECO:0000269|PubMed:25735958}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; AY838897; AAW21317.1; -; mRNA.
DR EMBL; AP005825; BAD08075.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09772.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80498.1; -; Genomic_DNA.
DR EMBL; AK099580; BAG94205.1; -; mRNA.
DR EMBL; AB110203; BAC78595.1; -; mRNA.
DR RefSeq; XP_015626662.1; XM_015771176.1.
DR AlphaFoldDB; Q6YVJ0; -.
DR SMR; Q6YVJ0; -.
DR STRING; 4530.OS02T0704000-01; -.
DR PaxDb; Q6YVJ0; -.
DR PRIDE; Q6YVJ0; -.
DR EnsemblPlants; Os02t0704000-01; Os02t0704000-01; Os02g0704000.
DR GeneID; 4330451; -.
DR Gramene; Os02t0704000-01; Os02t0704000-01; Os02g0704000.
DR KEGG; osa:4330451; -.
DR eggNOG; KOG1285; Eukaryota.
DR HOGENOM; CLU_016472_0_0_1; -.
DR InParanoid; Q6YVJ0; -.
DR OMA; SGFMKPC; -.
DR OrthoDB; 524712at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central.
DR GO; GO:0045549; F:9-cis-epoxycarotenoid dioxygenase 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:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016121; P:carotene catabolic process; IBA:GO_Central.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 2: Evidence at transcript level;
KW Abscisic acid biosynthesis; Chloroplast; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Plastid; Reference proteome; Stress response;
KW Transit peptide.
FT TRANSIT 1..80
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 81..638
FT /note="9-cis-epoxycarotenoid dioxygenase NCED1,
FT chloroplastic"
FT /id="PRO_0000440937"
FT REGION 28..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 331
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 380
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 446
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 624
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
SQ SEQUENCE 638 AA; 68620 MW; E11BAFCB97307B2F CRC64;
MQRICPAHCS VTHSLTMKSM RLSYIPPAAS AAPQSPSYGR KKNASAAPPS AAASTTVLTS
PLVTTTRTPK QTEQEDEQLV AKTKTTRTVI ATTNGRAAPS QSRPRRRPAP AAAASAASLP
MTFCNALEEV INTFIDPPAL RPAVDPRNVL TSNFVPVDEL PPTPCPVVRG AIPRCLAGGA
YIRNGPNPQH LPRGPHHLFD GDGMLHSLLL PSPASSGDDP VLCSRYVQTY KYLVERDAGA
PVLPNVFSGF HGVAGMARGA VVAARVLTGQ MNPLEGVGLA NTSLAYFAGR LYALGESDLP
YAVRVHPDTG EVTTHGRCDF GGRLVMGMTA HPKKDPVTGE LFAFRYGPVP PFVTYFRFDP
AGNKGADVPI FSVQQPSFLH DFAITERYAI FPEIQIVMKP MDMVVGGGSP VGSDPGKVPR
LGVIPRYATD ESEMRWFEVP GFNIMHSVNA WEEAGGEELV LVAPNVLSIE HALEHMELVH
SCVEKVRINL RTGVVTRTPL AAGNFDFPVI NPAFLGRRNR YGYFGVGDPA PKIGGVAKLD
FDRAGEGDCT VAQRDFGPGC FAGEPFFVAD DVEGNGNEDD GYLVCYVHDE ATGENRFVVM
DARSPDLEIV AEVQLPGRVP YGFHGLFVTQ AELQSQHQ