PDS_ARATH
ID PDS_ARATH Reviewed; 566 AA.
AC Q07356; F4JUN0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=15-cis-phytoene desaturase, chloroplastic/chromoplastic {ECO:0000305};
DE EC=1.3.5.5 {ECO:0000269|PubMed:9914519};
DE AltName: Full=Phytoene dehydrogenase {ECO:0000305};
DE AltName: Full=Phytoene desaturase {ECO:0000303|PubMed:8290648};
DE Flags: Precursor;
GN Name=PDS; OrderedLocusNames=At4g14210; ORFNames=dl3145c;
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].
RX PubMed=8290648; DOI=10.1104/pp.103.4.1475;
RA Bartley G.E., Scolnik P.A.;
RT "Phytoene desaturase from Arabidopsis.";
RL Plant Physiol. 103:1475-1475(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [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 FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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).
CC -!- FUNCTION: Converts phytoene into zeta-carotene via the intermediary of
CC phytofluene by the symmetrical introduction of two double bonds at the
CC C-11 and C-11' positions of phytoene with a concomitant isomerization
CC of two neighboring double bonds at the C9 and C9' positions from trans
CC to cis. {ECO:0000269|PubMed:9914519}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-cis-phytoene + 2 a plastoquinone = 9,9',15-tri-cis-zeta-
CC carotene + 2 a plastoquinol; Xref=Rhea:RHEA:30287, Rhea:RHEA-
CC COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:17757, ChEBI:CHEBI:27787,
CC ChEBI:CHEBI:48717, ChEBI:CHEBI:62192; EC=1.3.5.5;
CC Evidence={ECO:0000269|PubMed:9914519};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:A2XDA1};
CC -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:A2XDA1}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:Q40406}. Plastid, chromoplast
CC {ECO:0000250|UniProtKB:Q40406}. Membrane
CC {ECO:0000250|UniProtKB:A2XDA1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:A2XDA1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q07356-1; Sequence=Displayed;
CC -!- DEVELOPMENTAL STAGE: Ripening fruit.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {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; L16237; AAA20109.1; -; mRNA.
DR EMBL; Z97335; CAB10200.1; -; Genomic_DNA.
DR EMBL; AL161538; CAB78463.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83393.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83394.2; -; Genomic_DNA.
DR EMBL; CP002687; ANM67189.1; -; Genomic_DNA.
DR EMBL; AF360196; AAK25906.1; -; mRNA.
DR EMBL; AY040007; AAK64084.1; -; mRNA.
DR PIR; F71403; F71403.
DR RefSeq; NP_001319934.1; NM_001340907.1. [Q07356-1]
DR RefSeq; NP_001329033.1; NM_001340908.1. [Q07356-1]
DR RefSeq; NP_193157.1; NM_117498.4. [Q07356-1]
DR AlphaFoldDB; Q07356; -.
DR SMR; Q07356; -.
DR STRING; 3702.AT4G14210.1; -.
DR iPTMnet; Q07356; -.
DR PaxDb; Q07356; -.
DR PRIDE; Q07356; -.
DR ProteomicsDB; 251394; -. [Q07356-1]
DR EnsemblPlants; AT4G14210.1; AT4G14210.1; AT4G14210. [Q07356-1]
DR EnsemblPlants; AT4G14210.2; AT4G14210.2; AT4G14210. [Q07356-1]
DR EnsemblPlants; AT4G14210.3; AT4G14210.3; AT4G14210. [Q07356-1]
DR GeneID; 827061; -.
DR Gramene; AT4G14210.1; AT4G14210.1; AT4G14210. [Q07356-1]
DR Gramene; AT4G14210.2; AT4G14210.2; AT4G14210. [Q07356-1]
DR Gramene; AT4G14210.3; AT4G14210.3; AT4G14210. [Q07356-1]
DR KEGG; ath:AT4G14210; -.
DR Araport; AT4G14210; -.
DR TAIR; locus:2129515; AT4G14210.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_022687_1_0_1; -.
DR InParanoid; Q07356; -.
DR OMA; THCFFGA; -.
DR PhylomeDB; Q07356; -.
DR BioCyc; MetaCyc:AT4G14210-MON; -.
DR BRENDA; 1.3.5.5; 399.
DR UniPathway; UPA00803; -.
DR PRO; PR:Q07356; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q07356; baseline and differential.
DR Genevisible; Q07356; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009509; C:chromoplast; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016166; F:phytoene dehydrogenase activity; IDA:TAIR.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IDA:TAIR.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR014102; Phytoene_desaturase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02731; phytoene_desat; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carotenoid biosynthesis; Chloroplast; Chromoplast;
KW FAD; Flavoprotein; Membrane; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..86
FT /note="Chloroplast and chromoplast"
FT /evidence="ECO:0000255"
FT CHAIN 87..566
FT /note="15-cis-phytoene desaturase,
FT chloroplastic/chromoplastic"
FT /id="PRO_0000006322"
FT BINDING 103
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 122..123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 147..148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 519
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 529
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
SQ SEQUENCE 566 AA; 62964 MW; BAA6E522CFBD2694 CRC64;
MVVFGNVSAA NLPYQNGFLE ALSSGGCELM GHSFRVPTSQ ALKTRTRRRS TAGPLQVVCV
DIPRPELENT VNFLEAASLS ASFRSAPRPA KPLKVVIAGA GLAGLSTAKY LADAGHKPLL
LEARDVLGGK IAAWKDEDGD WYETGLHIFF GAYPNVQNLF GELGINDRLQ WKEHSMIFAM
PSKPGEFSRF DFPDVLPAPL NGIWAILRNN EMLTWPEKIK FAIGLLPAMV GGQAYVEAQD
GLSVKEWMEK QGVPERVTDE VFIAMSKALN FINPDELSMQ CILIALNRFL QEKHGSKMAF
LDGNPPERLC MPVVDHIRSL GGEVQLNSRI KKIELNDDGT VKSFLLTNGS TVEGDAYVFA
APVDILKLLL PDPWKEIPYF KKLDKLVGVP VINVHIWFDR KLKNTYDHLL FSRSNLLSVY
ADMSLTCKEY YDPNRSMLEL VFAPAEEWIS RTDSDIIDAT MKELEKLFPD EISADQSKAK
ILKYHVVKTP RSVYKTIPNC EPCRPLQRSP IEGFYLAGDY TKQKYLASME GAVLSGKFCS
QSIVQDYELL AASGPRKLSE ATVSSS
