NCED2_ARATH
ID NCED2_ARATH Reviewed; 583 AA.
AC O49505;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=9-cis-epoxycarotenoid dioxygenase NCED2, chloroplastic;
DE Short=AtNCED2;
DE EC=1.13.11.51;
DE Flags: Precursor;
GN Name=NCED2; OrderedLocusNames=At4g18350; ORFNames=F28J12.10;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
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 [5]
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 [6]
RP TISSUE SPECIFICITY.
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. {ECO:0000269|PubMed:11532178}.
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}. Note=Partially bound to the thylakoid.
CC -!- TISSUE SPECIFICITY: Very low in all tissues. Expressed at the point of
CC organ attachment and the abscission zones in the plant.
CC {ECO:0000269|PubMed:12834401, ECO:0000269|PubMed:16412079}.
CC -!- INDUCTION: Low induction by drought stress.
CC {ECO:0000269|PubMed:12834401}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL021710; CAA16715.1; -; Genomic_DNA.
DR EMBL; AL161548; CAB78837.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84030.1; -; Genomic_DNA.
DR EMBL; BT030365; ABO38778.1; -; mRNA.
DR PIR; T04531; T04531.
DR RefSeq; NP_193569.1; NM_117945.3.
DR AlphaFoldDB; O49505; -.
DR SMR; O49505; -.
DR STRING; 3702.AT4G18350.1; -.
DR PaxDb; O49505; -.
DR PRIDE; O49505; -.
DR ProteomicsDB; 251204; -.
DR EnsemblPlants; AT4G18350.1; AT4G18350.1; AT4G18350.
DR GeneID; 827562; -.
DR Gramene; AT4G18350.1; AT4G18350.1; AT4G18350.
DR KEGG; ath:AT4G18350; -.
DR Araport; AT4G18350; -.
DR TAIR; locus:2124489; AT4G18350.
DR eggNOG; KOG1285; Eukaryota.
DR HOGENOM; CLU_016472_0_0_1; -.
DR InParanoid; O49505; -.
DR OMA; SEVIWVN; -.
DR OrthoDB; 524712at2759; -.
DR PhylomeDB; O49505; -.
DR BioCyc; MetaCyc:AT4G18350-MON; -.
DR BRENDA; 1.13.11.51; 399.
DR PRO; PR:O49505; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49505; baseline and differential.
DR Genevisible; O49505; AT.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; 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; ISS:TAIR.
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; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..583
FT /note="9-cis-epoxycarotenoid dioxygenase NCED2,
FT chloroplastic"
FT /id="PRO_0000285990"
FT BINDING 280
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 329
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 394
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 570
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
SQ SEQUENCE 583 AA; 65067 MW; A138F93542E50852 CRC64;
MVSLLTMPMS GGIKTWPQAQ IDLGFRPIKR QPKVIKCTVQ IDVTELTKKR QLFTPRTTAT
PPQHNPLRLN IFQKAAAIAI DAAERALISH EQDSPLPKTA DPRVQIAGNY SPVPESSVRR
NLTVEGTIPD CIDGVYIRNG ANPMFEPTAG HHLFDGDGMV HAVKITNGSA SYACRFTKTE
RLVQEKRLGR PVFPKAIGEL HGHSGIARLM LFYARGLCGL INNQNGVGVA NAGLVYFNNR
LLAMSEDDLP YQLKITQTGD LQTVGRYDFD GQLKSAMIAH PKLDPVTKEL HALSYDVVKK
PYLKYFRFSP DGVKSPELEI PLETPTMIHD FAITENFVVI PDQQVVFKLG EMISGKSPVV
FDGEKVSRLG IMPKDATEAS QIIWVNSPET FCFHLWNAWE SPETEEIVVI GSCMSPADSI
FNERDESLRS VLSEIRINLR TRKTTRRSLL VNEDVNLEIG MVNRNRLGRK TRFAFLAIAY
PWPKVSGFAK VDLCTGEMKK YIYGGEKYGG EPFFLPGNSG NGEENEDDGY IFCHVHDEET
KTSELQIINA VNLKLEATIK LPSRVPYGFH GTFVDSNELV DQL