ID D7L349_ARALL Unreviewed; 599 AA.
AC D7L349;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=9-cis-epoxycarotenoid dioxygenase {ECO:0000256|ARBA:ARBA00039007};
DE EC=1.13.11.51 {ECO:0000256|ARBA:ARBA00039007};
GN Name=NCED3 {ECO:0000313|EMBL:EFH61304.1};
GN ORFNames=ARALYDRAFT_478868 {ECO:0000313|EMBL:EFH61304.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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:0000256|ARBA:ARBA00036784};
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:0000256|ARBA:ARBA00035929};
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:0000256|ARBA:ARBA00036011};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006787}.
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DR EMBL; GL348715; EFH61304.1; -; Genomic_DNA.
DR RefSeq; XP_002885045.1; XM_002884999.1.
DR AlphaFoldDB; D7L349; -.
DR SMR; D7L349; -.
DR STRING; 81972.D7L349; -.
DR EnsemblPlants; fgenesh2_kg.3__1569__AT3G14440.1; fgenesh2_kg.3__1569__AT3G14440.1; fgenesh2_kg.3__1569__AT3G14440.1.
DR GeneID; 9321111; -.
DR Gramene; fgenesh2_kg.3__1569__AT3G14440.1; fgenesh2_kg.3__1569__AT3G14440.1; fgenesh2_kg.3__1569__AT3G14440.1.
DR KEGG; aly:9321111; -.
DR eggNOG; KOG1285; Eukaryota.
DR HOGENOM; CLU_016472_0_0_1; -.
DR OrthoDB; 318119at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:EnsemblPlants.
DR GO; GO:0045549; F:9-cis-epoxycarotenoid dioxygenase activity; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0042538; P:hyperosmotic salinity response; IEA:EnsemblPlants.
DR GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543:SF26; 9-CIS-EPOXYCAROTENOID DIOXYGENASE NCED3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR Pfam; PF03055; RPE65; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:EFH61304.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604294-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT BINDING 297
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 346
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 411
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 585
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 599 AA; 65989 MW; 7B68D5C59B6E4634 CRC64;
MASFTATAAV SRRWVGGNHT QPPLSSSQSS DLSYCSSLPM TSRVTRKLNV SSALHTPPAL
HFPKQSSNSP AIVVNPKAKE SDTKQMNLFQ RAAAAALDAA EGFLVRHERL HPLPKTSDPS
VQIAGNFAPV NEQPVRRNLP VVGKIPDSIK GVYVRNGANP LHEPVTGHHF FDGDGMVHAV
KFEDGSASYA CRFTQTNRFI QESELGRPVF PKAIGELHGH TGIARLMLFY ARAAAGIVDP
AHGTGVANAG LVYFNGRLLA MSEDDLPYQV RITPSGDLKT VGRFDFDGQL ESTMIAHPKV
DPESGELFAL SYDVVSKPYL KYFRFSPDGT KSPDVEIQLD QPTMMHDFAI TENFVVIPDQ
QVVFKLPEMI RGGSPVVYDK NKVSRFGILD KYAEDSSNIK WIDAPDCFCF HLWNAWEEPE
TEEVVVIGSC MTPPDSIFNE SDENLKSVLS EIRLNLKTGE STRRPIISDE DQQVNLEAGM
VNRNMLGRKT KFAYLALAEP WPKVSGFAKV DLTTGEVKKH LYGDNRYGGE PLFLPGEGGE
EDEGHILCFV HDEKTWTSEL QIVNAVSLEV EATVKLPSRV PYGFHGTFIG ADDLAKQVV
//
