NCED9_ARATH
ID NCED9_ARATH Reviewed; 657 AA.
AC Q9M9F5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=9-cis-epoxycarotenoid dioxygenase NCED9, chloroplastic;
DE Short=AtNCED9;
DE EC=1.13.11.51;
DE Flags: Precursor;
GN Name=NCED9; OrderedLocusNames=At1g78390; ORFNames=F3F9.10;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, AND INDUCTION BY DROUGHT STRESS.
RX PubMed=11532178; DOI=10.1046/j.1365-313x.2001.01096.x;
RA Iuchi S., Kobayashi M., Taji T., Naramoto M., Seki M., Kato T., Tabata S.,
RA Kakubari Y., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Regulation of drought tolerance by gene manipulation of 9-cis-
RT epoxycarotenoid dioxygenase, a key enzyme in abscisic acid biosynthesis in
RT Arabidopsis.";
RL Plant J. 27:325-333(2001).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY DROUGHT STRESS.
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 [5]
RP FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16412079; DOI=10.1111/j.1365-313x.2005.02622.x;
RA Lefebvre V., North H., Frey A., Sotta B., Seo M., Okamoto M., Nambara E.,
RA Marion-Poll A.;
RT "Functional analysis of Arabidopsis NCED6 and NCED9 genes indicates that
RT ABA synthesized in the endosperm is involved in the induction of seed
RT dormancy.";
RL Plant J. 45:309-319(2006).
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. Contributes probably to abscisic acid synthesis for the
CC induction of seed dormancy. {ECO:0000269|PubMed:11532178,
CC ECO:0000269|PubMed:16412079}.
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;
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 -!- 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;
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 stroma
CC {ECO:0000269|PubMed:12834401}.
CC -!- TISSUE SPECIFICITY: Expressed in developing siliques, embryo and
CC endosperm. {ECO:0000269|PubMed:12834401, ECO:0000269|PubMed:16412079}.
CC -!- DEVELOPMENTAL STAGE: Expressed in seeds at early and mid-maturation
CC stages. {ECO:0000269|PubMed:16412079}.
CC -!- INDUCTION: Low induction by drought stress.
CC {ECO:0000269|PubMed:11532178, ECO:0000269|PubMed:12834401}.
CC -!- DISRUPTION PHENOTYPE: Plants exhibit abscisic-acid-deficient phenotypes
CC in seeds, but not in vegetative tissues. {ECO:0000269|PubMed:16412079}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; AC013430; AAF71797.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36100.1; -; Genomic_DNA.
DR PIR; E96812; E96812.
DR RefSeq; NP_177960.1; NM_106486.3.
DR AlphaFoldDB; Q9M9F5; -.
DR SMR; Q9M9F5; -.
DR STRING; 3702.AT1G78390.1; -.
DR PaxDb; Q9M9F5; -.
DR PRIDE; Q9M9F5; -.
DR ProteomicsDB; 251205; -.
DR EnsemblPlants; AT1G78390.1; AT1G78390.1; AT1G78390.
DR GeneID; 844175; -.
DR Gramene; AT1G78390.1; AT1G78390.1; AT1G78390.
DR KEGG; ath:AT1G78390; -.
DR Araport; AT1G78390; -.
DR TAIR; locus:2032085; AT1G78390.
DR eggNOG; KOG1285; Eukaryota.
DR HOGENOM; CLU_016472_0_0_1; -.
DR InParanoid; Q9M9F5; -.
DR OMA; ENAMISH; -.
DR OrthoDB; 524712at2759; -.
DR PhylomeDB; Q9M9F5; -.
DR BioCyc; MetaCyc:AT1G78390-MON; -.
DR BRENDA; 1.13.11.51; 399.
DR PRO; PR:Q9M9F5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9F5; baseline and differential.
DR Genevisible; Q9M9F5; AT.
DR GO; GO:0009570; C:chloroplast stroma; IDA: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:0009688; P:abscisic acid biosynthetic process; TAS:TAIR.
DR GO; GO:0016121; P:carotene catabolic process; IBA:GO_Central.
DR GO; GO:0010162; P:seed dormancy process; IGI:TAIR.
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; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..657
FT /note="9-cis-epoxycarotenoid dioxygenase NCED9,
FT chloroplastic"
FT /id="PRO_0000285998"
FT BINDING 357
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 406
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 471
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 642
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
SQ SEQUENCE 657 AA; 73015 MW; F41DECBE94806318 CRC64;
MTIITIISGM YIYSLLSQDA HHSQYGQNTN LVLKKPIPKP QTAAFNQEST MASTTLLPST
STQFLDRTFS TSSSSSRPKL QSLSFSSTLR NKKLVVPCYV SSSVNKKSSV SSSLQSPTFK
PPSWKKLCND VTNLIPKTTN QNPKLNPVQR TAAMVLDAVE NAMISHERRR HPHPKTADPA
VQIAGNFFPV PEKPVVHNLP VTGTVPECIQ GVYVRNGANP LHKPVSGHHL FDGDGMVHAV
RFDNGSVSYA CRFTETNRLV QERECGRPVF PKAIGELHGH LGIAKLMLFN TRGLFGLVDP
TGGLGVANAG LVYFNGHLLA MSEDDLPYHV KVTQTGDLET SGRYDFDGQL KSTMIAHPKI
DPETRELFAL SYDVVSKPYL KYFRFTSDGE KSPDVEIPLD QPTMIHDFAI TENFVVIPDQ
QVVFRLPEMI RGGSPVVYDE KKKSRFGILN KNAKDASSIQ WIEVPDCFCF HLWNSWEEPE
TDEVVVIGSC MTPPDSIFNE HDETLQSVLS EIRLNLKTGE STRRPVISEQ VNLEAGMVNR
NLLGRKTRYA YLALTEPWPK VSGFAKVDLS TGEIRKYIYG EGKYGGEPLF LPSGDGEEDG
GYIMVFVHDE EKVKSELQLI NAVNMKLEAT VTLPSRVPYG FHGTFISKED LSKQALC
