NCED1_MAIZE
ID NCED1_MAIZE Reviewed; 604 AA.
AC O24592;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=9-cis-epoxycarotenoid dioxygenase 1, chloroplastic;
DE EC=1.13.11.51 {ECO:0000269|PubMed:12495810, ECO:0000269|PubMed:20884803};
DE AltName: Full=Protein VIVIPAROUS14 {ECO:0000303|PubMed:9188535};
DE Short=VP-14;
DE Short=VP14 {ECO:0000303|PubMed:9188535};
DE Flags: Precursor;
GN Name=VP14;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Wisconsin 22;
RX PubMed=9342392; DOI=10.1073/pnas.94.22.12235;
RA Tan B.C., Schwartz S.H., Zeevaart J.A., McCarty D.R.;
RT "Genetic control of abscisic acid biosynthesis in maize.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12235-12240(1997).
RN [2]
RP FUNCTION.
RX PubMed=9188535; DOI=10.1126/science.276.5320.1872;
RA Schwartz S.H., Tan B.C., Gage D.A., Zeevaart J.A., McCarty D.R.;
RT "Specific oxidative cleavage of carotenoids by VP14 of maize.";
RL Science 276:1872-1874(1997).
RN [3]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ALA-90.
RX PubMed=11576422; DOI=10.1046/j.1365-313x.2001.01102.x;
RA Tan B.C., Cline K., McCarty D.R.;
RT "Localization and targeting of the VP14 epoxy-carotenoid dioxygenase to
RT chloroplast membranes.";
RL Plant J. 27:373-382(2001).
RN [4]
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12495810; DOI=10.1016/s0304-4165(02)00422-1;
RA Schwartz S.H., Tan B.C., McCarty D.R., Welch W., Zeevaart J.A.;
RT "Substrate specificity and kinetics for VP14, a carotenoid cleavage
RT dioxygenase in the ABA biosynthetic pathway.";
RL Biochim. Biophys. Acta 1619:9-14(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 76-604 IN COMPLEX WITH IRON ION,
RP COFACTOR, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=20884803; DOI=10.1105/tpc.110.074815;
RA Messing S.A., Gabelli S.B., Echeverria I., Vogel J.T., Guan J.C., Tan B.C.,
RA Klee H.J., McCarty D.R., Amzel L.M.;
RT "Structural insights into maize viviparous14, a key enzyme in the
RT biosynthesis of the phytohormone abscisic acid.";
RL Plant Cell 22:2970-2980(2010).
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. Not active on the all-trans isomers of violaxanthin and
CC neoxanthin. Contributes probably to abscisic acid synthesis for the
CC induction of seed dormancy. {ECO:0000269|PubMed:20884803,
CC ECO:0000269|PubMed:9188535, ECO:0000269|PubMed:9342392}.
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:0000269|PubMed:12495810,
CC ECO:0000269|PubMed:20884803};
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:0000269|PubMed:12495810, ECO:0000269|PubMed:20884803};
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:0000269|PubMed:12495810,
CC ECO:0000269|PubMed:20884803};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:20884803};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:20884803};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for 9-cis antheraxanthin {ECO:0000269|PubMed:12495810};
CC KM=15 uM for 9-cis luteoxanthin 8'S {ECO:0000269|PubMed:12495810};
CC KM=8 uM for 9-cis luteoxanthin 8'R {ECO:0000269|PubMed:12495810};
CC KM=27 uM for 9-cis neoxanthin {ECO:0000269|PubMed:12495810};
CC KM=58 uM for 9-cis violaxanthin {ECO:0000269|PubMed:12495810};
CC Note=Vmax with 9-cis violaxanthin as substrate is more than twice the
CC Vmax with 9-cis neoxanthin as substrate.;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:11576422, ECO:0000269|PubMed:9342392}.
CC Note=Partially bound to the thylakoid membranes.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots and embryos.
CC {ECO:0000269|PubMed:9342392}.
CC -!- INDUCTION: By drought stress. {ECO:0000269|PubMed:9342392}.
CC -!- DOMAIN: The N-terminal amphipathic alpha-helix (81-100) is essential,
CC but not sufficient, for the thylakoid membrane targeting.
CC -!- DISRUPTION PHENOTYPE: Plants show a viviparous phenotype.
CC {ECO:0000269|PubMed:9342392}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; U95953; AAB62181.2; -; mRNA.
DR PIR; T04351; T04351.
DR RefSeq; NP_001105902.2; NM_001112432.2.
DR PDB; 3NPE; X-ray; 3.20 A; A=76-604.
DR PDBsum; 3NPE; -.
DR AlphaFoldDB; O24592; -.
DR SMR; O24592; -.
DR STRING; 4577.GRMZM2G014392_P01; -.
DR SwissLipids; SLP:000001487; -.
DR PaxDb; O24592; -.
DR GeneID; 732819; -.
DR KEGG; zma:732819; -.
DR MaizeGDB; 726071; -.
DR eggNOG; KOG1285; Eukaryota.
DR OrthoDB; 524712at2759; -.
DR BRENDA; 1.13.11.51; 6752.
DR EvolutionaryTrace; O24592; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; O24592; baseline and differential.
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 1: Evidence at protein level;
KW 3D-structure; Abscisic acid biosynthesis; Chloroplast; Dioxygenase; Iron;
KW Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW Stress response; Transit peptide.
FT TRANSIT 1..23
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 24..604
FT /note="9-cis-epoxycarotenoid dioxygenase 1, chloroplastic"
FT /id="PRO_0000282607"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:20884803,
FT ECO:0007744|PDB:3NPE"
FT BINDING 347
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:20884803,
FT ECO:0007744|PDB:3NPE"
FT BINDING 412
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:20884803,
FT ECO:0007744|PDB:3NPE"
FT BINDING 590
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:20884803,
FT ECO:0007744|PDB:3NPE"
FT MUTAGEN 90
FT /note="A->AGGG: Loss of binding to the thylakoid membrane."
FT /evidence="ECO:0000269|PubMed:11576422"
FT MUTAGEN 90
FT /note="A->APPP: Loss of binding to the thylakoid membrane."
FT /evidence="ECO:0000269|PubMed:11576422"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:3NPE"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:3NPE"
FT TURN 214..219
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3NPE"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:3NPE"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 409..418
FT /evidence="ECO:0007829|PDB:3NPE"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 425..432
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 449..455
FT /evidence="ECO:0007829|PDB:3NPE"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 462..468
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 506..511
FT /evidence="ECO:0007829|PDB:3NPE"
FT TURN 512..514
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 540..543
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 549..559
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:3NPE"
FT TURN 570..573
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 574..583
FT /evidence="ECO:0007829|PDB:3NPE"
FT STRAND 591..595
FT /evidence="ECO:0007829|PDB:3NPE"
FT HELIX 596..599
FT /evidence="ECO:0007829|PDB:3NPE"
SQ SEQUENCE 604 AA; 65495 MW; 710FDF61BD0F5BD5 CRC64;
MQGLAPPTSV SIHRHLPARS RARASNSVRF SPRAVSSVPP AECLQAPFHK PVADLPAPSR
KPAAIAVPGH AAAPRKAEGG KKQLNLFQRA AAAALDAFEE GFVANVLERP HGLPSTADPA
VQIAGNFAPV GERPPVHELP VSGRIPPFID GVYARNGANP CFDPVAGHHL FDGDGMVHAL
RIRNGAAESY ACRFTETARL RQERAIGRPV FPKAIGELHG HSGIARLALF YARAACGLVD
PSAGTGVANA GLVYFNGRLL AMSEDDLPYH VRVADDGDLE TVGRYDFDGQ LGCAMIAHPK
LDPATGELHA LSYDVIKRPY LKYFYFRPDG TKSDDVEIPL EQPTMIHDFA ITENLVVVPD
HQVVFKLQEM LRGGSPVVLD KEKTSRFGVL PKHAADASEM AWVDVPDCFC FHLWNAWEDE
ATGEVVVIGS CMTPADSIFN ESDERLESVL TEIRLDARTG RSTRRAVLPP SQQVNLEVGM
VNRNLLGRET RYAYLAVAEP WPKVSGFAKV DLSTGELTKF EYGEGRFGGE PCFVPMDPAA
AHPRGEDDGY VLTFVHDERA GTSELLVVNA ADMRLEATVQ LPSRVPFGFH GTFITGQELE
AQAA
