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NCED5_ORYSJ
ID   NCED5_ORYSJ             Reviewed;         613 AA.
AC   Q5MBR3; A0A0P0YC36;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=9-cis-epoxycarotenoid dioxygenase NCED5, chloroplastic {ECO:0000305};
DE            Short=OsNCED5 {ECO:0000312|EMBL:AAW21321.1};
DE            EC=1.13.11.51 {ECO:0000250|UniProtKB:O24592};
DE   Flags: Precursor;
GN   Name=NCED5 {ECO:0000312|EMBL:AAW21321.1};
GN   OrderedLocusNames=Os12g0617400 {ECO:0000312|EMBL:BAH95791.1},
GN   LOC_Os12g42280 {ECO:0000312|EMBL:ABA99870.1};
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.
RA   Dian W.M.;
RT   "Oryza sativa japonica group 9-cis-epoxycarotenoid dioxygenase 5 (NCED5)
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=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   INDUCTION.
RX   PubMed=18326788; DOI=10.1104/pp.108.117028;
RA   Welsch R., Wuest F., Baer C., Al-Babili S., Beyer P.;
RT   "A third phytoene synthase is devoted to abiotic stress-induced abscisic
RT   acid formation in rice and defines functional diversification of phytoene
RT   synthase genes.";
RL   Plant Physiol. 147:367-380(2008).
RN   [7]
RP   INDUCTION BY D-ALLOSE.
RX   PubMed=23397192; DOI=10.1007/s00425-013-1853-9;
RA   Fukumoto T., Kano A., Ohtani K., Inoue M., Yoshihara A., Izumori K.,
RA   Tajima S., Shigematsu Y., Tanaka K., Ohkouchi T., Ishida Y., Nishizawa Y.,
RA   Tada Y., Ichimura K., Gomi K., Yoo S.D., Sheen J., Akimitsu K.;
RT   "Phosphorylation of D-allose by hexokinase involved in regulation of OsABF1
RT   expression for growth inhibition in Oryza sativa L.";
RL   Planta 237:1379-1391(2013).
RN   [8]
RP   INDUCTION BY DROUGHT STRESS.
RX   PubMed=25418692; DOI=10.1111/jipb.12313;
RA   Du H., Chang Y., Huang F., Xiong L.;
RT   "GID1 modulates stomatal response and submergence tolerance involving
RT   abscisic acid and gibberellic acid signaling in rice.";
RL   J. Integr. Plant Biol. 57:954-968(2015).
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 abscisic acid (ABA) and salt (PubMed:18326788).
CC       Induced by D-allose (PubMed:23397192). Induced by drought stress
CC       (PubMed:25418692, PubMed:25735958). {ECO:0000269|PubMed:18326788,
CC       ECO:0000269|PubMed:23397192, ECO:0000269|PubMed:25418692,
CC       ECO:0000269|PubMed:25735958}.
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAT18107.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY838901; AAW21321.1; -; mRNA.
DR   EMBL; DP000011; ABA99870.1; -; Genomic_DNA.
DR   EMBL; AP008218; BAH95791.1; -; Genomic_DNA.
DR   EMBL; AP014968; BAT18107.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_015618707.1; XM_015763221.1.
DR   AlphaFoldDB; Q5MBR3; -.
DR   SMR; Q5MBR3; -.
DR   STRING; 4530.OS12T0617400-01; -.
DR   PRIDE; Q5MBR3; -.
DR   GeneID; 9270250; -.
DR   KEGG; osa:9270250; -.
DR   eggNOG; KOG1285; Eukaryota.
DR   InParanoid; Q5MBR3; -.
DR   OrthoDB; 524712at2759; -.
DR   PlantReactome; R-OSA-1119374; Abscisic acid biosynthesis.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000059680; Chromosome 12.
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..36
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..613
FT                   /note="9-cis-epoxycarotenoid dioxygenase NCED5,
FT                   chloroplastic"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000440941"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         305
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O24592"
FT   BINDING         354
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O24592"
FT   BINDING         419
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O24592"
FT   BINDING         600
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:O24592"
SQ   SEQUENCE   613 AA;  65929 MW;  D307A12B08BF6AFA CRC64;
     MPTTFTPNSP ASSCSIHHRA SPSRGARNSV RFTRPRAAAA ATNSVLSAPS SVPPAYVPPP
     PPPPTKMFPE AGDAAAAKAA ARRCGKKKDG LNFFQRAAAV ALDAFEEGFI TNVLERPHAL
     PRTADPAVQI AGNFAPVGEQ PPVRSLPVSG RIPPFINGVY ARNGANPHFE PTAGHHLFDG
     DGMVHAVRIR NGAAESYACR FTETARLGQE RALGRAVFPK AIGELHGHSG IARLALFYAR
     GLCGLVDPSH GTGVANAGLV YFNGRLLAMS EDDLPYQVRV TADGDLETVG RYDFDGQLGC
     AMIAHPKLDP VSGELFALSY DVIKKPYLKY FYFDADGTKS PDVEIELEQP TMIHDFAITE
     NFVVVPDHQV VFKLGEMFRG GSPVVLDREK TSRFGVLPKH ATSSLEMVWV DVPDCFCFHL
     WNAWEEAESG EVVVVGSCMT PADSIFNESD EHLESVLTEI RLNTRTGEST RRAVLPPAAQ
     VNLEVGMVNR AMLGRKTRYA YLAVAEPWPK VSGFAKVDLA TGELTKFEYG EGRFGGEPCF
     VPMGGAGAAA SPARGEDDGY ILSFVRDEAA GTSELLVVNA ADMRLEATVQ LPSRVPYGFH
     GTFINAGELA TQA
 
 
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