NCED1_PHAVU
ID NCED1_PHAVU Reviewed; 615 AA.
AC Q9M6E8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=9-cis-epoxycarotenoid dioxygenase NCED1, chloroplastic;
DE EC=1.13.11.51;
DE AltName: Full=PvNCED1;
DE Flags: Precursor;
GN Name=NCED1;
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=cv. Top Crop; TISSUE=Leaf;
RX PubMed=10611388; DOI=10.1073/pnas.96.26.15354;
RA Qin X., Zeevaart J.A.;
RT "The 9-cis-epoxycarotenoid cleavage reaction is the key regulatory step of
RT abscisic acid biosynthesis in water-stressed bean.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15354-15361(1999).
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, in response to water stress. Active on 9-cis-violaxanthin
CC and 9'-cis-neoxanthin, but not on the all-trans isomers of violaxanthin
CC and neoxanthin. {ECO:0000269|PubMed:10611388}.
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 thylakoid membrane
CC {ECO:0000269|PubMed:10611388}.
CC -!- INDUCTION: By drought stress. {ECO:0000269|PubMed:10611388}.
CC -!- MISCELLANEOUS: Overexpression of NCED1 results in increased
CC accumulation of abscisic acid and resistance to water stress.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; AF190462; AAF26356.1; -; mRNA.
DR AlphaFoldDB; Q9M6E8; -.
DR SMR; Q9M6E8; -.
DR STRING; 3885.XP_007149219.1; -.
DR SwissLipids; SLP:000001488; -.
DR KEGG; ag:AAF26356; -.
DR eggNOG; KOG1285; Eukaryota.
DR BRENDA; 1.13.11.51; 4746.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045549; F:9-cis-epoxycarotenoid dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
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; Coiled coil; Dioxygenase; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Plastid; Stress response;
KW Thylakoid; Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..615
FT /note="9-cis-epoxycarotenoid dioxygenase NCED1,
FT chloroplastic"
FT /id="PRO_0000285992"
FT REGION 20..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 571..592
FT /evidence="ECO:0000255"
FT BINDING 316
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 365
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 430
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
FT BINDING 602
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O24592"
SQ SEQUENCE 615 AA; 68075 MW; 0CC10F862D7DE130 CRC64;
MPSPASNTWI NTTLPSSCSS PFKDLASTSS SPTTLLPFKK RSSSNTNTIT CSLQTLHYPK
QYQPTSTSTT TTPTPIKPTT TTTTTTPHRE TKPLSDTKQP FPQKWNFLQK AAATGLDMVE
TALVSHESKH PLPKTADPKV QIAGNFAPVP EHAADQALPV VGKIPKCIDG VYVRNGANPL
YEPVAGHHFF DGDGMVHAVK FTNGAASYAC RFTETQRLAQ EKSLGRPVFP KAIGELHGHS
GIARLLLFYA RSLFQLVDGS HGMGVANAGL VYFNNHLLAM SEDDLPYHVR ITSNGDLTTV
GRYDFNGQLN STMIAHPKLD PVNGDLHALS YDVVQKPYLK YFRFSADGVK SPDVEIPLKE
PTMMHDFAIT ENFVVVPDQQ VVFKLTEMIT GGSPVVYDKN KTSRFGILDK NAKDANAMRW
IDAPECFCFH LWNAWEEPET DEIVVIGSCM TPADSIFNEC DESLKSVLSE IRLNLRTGKS
TRRPIISDAE QVNLEAGMVN RNKLGRKTQF AYLALAEPWP KVSGFAKVDL FSGEVQKYMY
GEEKFGGEPL FLPNGEEEGD GYILAFVHDE KEWKSELQIV NAQNLKLEAS IKLPSRVPYG
FHGTFIHSKD LRKQA