ID ZDS_ARATH Reviewed; 558 AA.
AC Q38893; A0A1I9LPJ6; Q8LD88; Q93YN2; Q9CAV3; Q9LLY1;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 27-MAR-2024, entry version 161.
DE RecName: Full=Zeta-carotene desaturase, chloroplastic/chromoplastic {ECO:0000305};
DE EC=1.3.5.6 {ECO:0000269|PubMed:9914519};
DE AltName: Full=9,9'-di-cis-zeta-carotene desaturase {ECO:0000305};
DE AltName: Full=Carotene 7,8-desaturase {ECO:0000305};
DE AltName: Full=Protein CHLOROPLAST BIOGENESIS 5 {ECO:0000303|PubMed:24907342};
DE AltName: Full=Protein PIGMENT DEFECTIVE 181 {ECO:0000305};
DE AltName: Full=Protein SPONTANEOUS CELL DEATH 1 {ECO:0000303|PubMed:17468780};
DE Flags: Precursor;
GN Name=ZDS1 {ECO:0000305};
GN Synonyms=CLB5 {ECO:0000303|PubMed:24907342}, PDE181 {ECO:0000305},
GN SPC1 {ECO:0000303|PubMed:17468780}, ZDS {ECO:0000303|Ref.1};
GN OrderedLocusNames=At3g04870 {ECO:0000312|Araport:AT3G04870};
GN ORFNames=T9J14.18 {ECO:0000312|EMBL:AAG51402.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Scolnik P.A., Bartley G.E.;
RT "Nucleotide sequence of zeta-carotene desaturase from Arabidopsis.";
RL (er) Plant Gene Register PGR95-111(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Giuliano G., Rosati C., Santangelo G.;
RT "Gene structure and regulation of the carotenoid biosynthetic pathway in
RT Arabidopsis.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9914519; DOI=10.1046/j.1432-1327.1999.00051.x;
RA Bartley G.E., Scolnik P.A., Beyer P.;
RT "Two Arabidopsis thaliana carotene desaturases, phytoene desaturase and
RT zeta-carotene desaturase, expressed in Escherichia coli, catalyze a poly-
RT cis pathway to yield pro-lycopene.";
RL Eur. J. Biochem. 259:396-403(1999).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17468780; DOI=10.1038/cr.2007.37;
RA Dong H., Deng Y., Mu J., Lu Q., Wang Y., Xu Y., Chu C., Chong K., Lu C.,
RA Zuo J.;
RT "The Arabidopsis Spontaneous Cell Death1 gene, encoding a zeta-carotene
RT desaturase essential for carotenoid biosynthesis, is involved in
RT chloroplast development, photoprotection and retrograde signalling.";
RL Cell Res. 17:458-470(2007).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24907342; DOI=10.1105/tpc.114.123349;
RA Avendano-Vazquez A.O., Cordoba E., Llamas E., San Roman C., Nisar N.,
RA De la Torre S., Ramos-Vega M., Gutierrez-Nava M.D., Cazzonelli C.I.,
RA Pogson B.J., Leon P.;
RT "An uncharacterized apocarotenoid-derived signal generated in zeta-carotene
RT desaturase mutants regulates leaf development and the expression of
RT chloroplast and nuclear genes in Arabidopsis.";
RL Plant Cell 26:2524-2537(2014).
CC -!- FUNCTION: Plays a crucial role in plant growth and development. Is
CC essential for the biosynthesis of carotenoids. Carotenoids are involved
CC in different physiological processes, including coloration,
CC photoprotection, biosynthesis of abscisic acid (ABA) and chloroplast
CC biogenesis (PubMed:17468780, PubMed:24907342). Catalyzes the conversion
CC of zeta-carotene to lycopene via the intermediary of neurosporene. It
CC carries out two consecutive desaturations (introduction of double
CC bonds) at positions C-7 and C-7'. Shows stereoselectivity toward trans
CC C15-C15'zeta-carotene double bond. The zeta-carotene produced by the
CC phytoene desaturase PDS has a C15-C15' double bond in the cis
CC configuration and it requires isomerization before being recognized as
CC substrate by ZDS. The main product is 7,9,7',9'-tetra-cis-lycopene
CC (pro-lycopene) (PubMed:9914519). {ECO:0000269|PubMed:17468780,
CC ECO:0000269|PubMed:24907342, ECO:0000269|PubMed:9914519}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9,9'-di-cis-zeta-carotene + 2 a quinone = 7,7',9,9'-tetra-cis-
CC lycopene + 2 a quinol; Xref=Rhea:RHEA:30955, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:48716, ChEBI:CHEBI:62466, ChEBI:CHEBI:132124; EC=1.3.5.6;
CC Evidence={ECO:0000269|PubMed:9914519};
CC -!- COFACTOR:
CC Name=decylplastoquinone; Xref=ChEBI:CHEBI:72953;
CC Evidence={ECO:0000250};
CC Name=6-decylubiquinone; Xref=ChEBI:CHEBI:52020; Evidence={ECO:0000250};
CC Note=Lipophilic quinones such as decyl-plastoquinone or decyl-
CC ubiquinone. {ECO:0000250};
CC -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, chromoplast
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves. Expressed at low levels
CC in flowers and siliques. {ECO:0000269|PubMed:17468780}.
CC -!- DISRUPTION PHENOTYPE: Albino seedling due to defect in pigmentation,
CC growth arrest shortly after germination, altered leaf development, and
CC seedling lethality. {ECO:0000269|PubMed:17468780,
CC ECO:0000269|PubMed:24907342}.
CC -!- SIMILARITY: Belongs to the zeta carotene desaturase family.
CC {ECO:0000305}.
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DR EMBL; U38550; AAA91161.1; -; mRNA.
DR EMBL; AF121947; AAF85796.1; -; Genomic_DNA.
DR EMBL; AC009465; AAG51402.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74148.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74149.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64503.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64504.1; -; Genomic_DNA.
DR EMBL; AY059920; AAL24402.1; -; mRNA.
DR EMBL; AY072096; AAL59918.1; -; mRNA.
DR EMBL; AY096583; AAM20233.1; -; mRNA.
DR EMBL; AY086144; AAM63349.1; -; mRNA.
DR RefSeq; NP_001319473.1; NM_001337544.1.
DR RefSeq; NP_001319474.1; NM_001337545.1.
DR RefSeq; NP_187138.1; NM_111359.4.
DR RefSeq; NP_974222.1; NM_202493.3.
DR AlphaFoldDB; Q38893; -.
DR SMR; Q38893; -.
DR BioGRID; 4982; 1.
DR STRING; 3702.Q38893; -.
DR PaxDb; 3702-AT3G04870-2; -.
DR ProteomicsDB; 242927; -.
DR DNASU; 819647; -.
DR EnsemblPlants; AT3G04870.1; AT3G04870.1; AT3G04870.
DR EnsemblPlants; AT3G04870.2; AT3G04870.2; AT3G04870.
DR EnsemblPlants; AT3G04870.3; AT3G04870.3; AT3G04870.
DR EnsemblPlants; AT3G04870.4; AT3G04870.4; AT3G04870.
DR GeneID; 819647; -.
DR Gramene; AT3G04870.1; AT3G04870.1; AT3G04870.
DR Gramene; AT3G04870.2; AT3G04870.2; AT3G04870.
DR Gramene; AT3G04870.3; AT3G04870.3; AT3G04870.
DR Gramene; AT3G04870.4; AT3G04870.4; AT3G04870.
DR KEGG; ath:AT3G04870; -.
DR Araport; AT3G04870; -.
DR TAIR; AT3G04870; ZDS.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_022687_1_1_1; -.
DR InParanoid; Q38893; -.
DR OMA; LNMTWYS; -.
DR OrthoDB; 348089at2759; -.
DR PhylomeDB; Q38893; -.
DR BioCyc; ARA:AT3G04870-MONOMER; -.
DR BioCyc; MetaCyc:AT3G04870-MONOMER; -.
DR UniPathway; UPA00803; -.
DR PRO; PR:Q38893; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38893; baseline and differential.
DR Genevisible; Q38893; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0052887; F:7,9,9'-tricis-neurosporene:quinone oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016719; F:9,9'-di-cis-zeta-carotene desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0052886; F:9,9'-dicis-carotene:quinone oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0052889; P:9,9'-di-cis-zeta-carotene desaturation to 7,9,7',9'-tetra-cis-lycopene; IDA:UniProtKB.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IMP:UniProtKB.
DR GO; GO:1901177; P:lycopene biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR014103; Zeta_caro_desat.
DR NCBIfam; TIGR02732; zeta_caro_desat; 1.
DR PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR PANTHER; PTHR42923:SF41; ZETA-CAROTENE DESATURASE, CHLOROPLASTIC_CHROMOPLASTIC; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Chloroplast; Chromoplast; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..27
FT /note="Chloroplast and chromoplast"
FT /evidence="ECO:0000255"
FT CHAIN 28..558
FT /note="Zeta-carotene desaturase,
FT chloroplastic/chromoplastic"
FT /id="PRO_0000041605"
FT CONFLICT 9
FT /note="A -> P (in Ref. 1; AAA91161)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="S -> F (in Ref. 6; AAM63349)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="G -> A (in Ref. 1; AAA91161)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="N -> S (in Ref. 1; AAA91161)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="V -> G (in Ref. 1; AAA91161 and 2; AAF85796)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="S -> P (in Ref. 1; AAA91161)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="W -> C (in Ref. 1; AAA91161 and 2; AAF85796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 61634 MW; 120E0B0614FE0CB7 CRC64;
MASSVVFAAT GSLSVPPLKS RRFYVNSSLD SDVSDMSVNA PKGLFPPEPV PYKGPKLKVA
IIGAGLAGMS TAVELLDQGH EVDIYDSRTF IGGKVGSFVD RRGNHIEMGL HVFFGCYNNL
FRLMKKVGAE KNLLVKDHTH TFINKDGTIG ELDFRFPVGA PIHGIRAFLV TNQLKPYDKL
RNSLALALSP VVKALVDPDG AMRDIRNLDS ISFSDWFLSK GGTRASIQRM WDPVAYALGF
IDCDNMSARC MLTIFSLFAT KTEASLLRML KGSPDVYLSG PIKQYITDRG GRIHLRWGCR
EILYDKSADG ETYVTGLAIS KATNKKIVKA DVYVAACDVP GIKRLLPKEW RESRFFNDIY
ELEGVPVVTV QLRYNGWVTE LQDIELARQL KRAVGLDNLL YTPDADFSCF ADLALASPAD
YYIEGQGTLL QCVLTPGDPY MRMPNDKIIE KVAMQVTELF PSSRGLEVTW SSVVKIAQSL
YREAPGKDPF RPDQKTPIKN FFLAGSYTKQ DYIDSMEGAT LSGRQASSYI CDAGEELAEL
NKKLSSSATA VPDELSLV
//
