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Database: UniProt
Entry: PDS_ARATH
LinkDB: PDS_ARATH
Original site: 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   24-JAN-2024, entry version 161.
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}.
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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.Q07356; -.
DR   iPTMnet; Q07356; -.
DR   PaxDb; 3702-AT4G14210-1; -.
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; AT4G14210; PDS3.
DR   eggNOG; KOG0029; Eukaryota.
DR   HOGENOM; CLU_022687_1_0_1; -.
DR   InParanoid; Q07356; -.
DR   OMA; HSMIFNQ; -.
DR   OrthoDB; 3597164at2759; -.
DR   PhylomeDB; Q07356; -.
DR   BioCyc; MetaCyc:AT4G14210-MONOMER; -.
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:0016166; F:phytoene dehydrogenase activity; IDA:TAIR.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IDA:TAIR.
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; IPR014102; Phytoene_desaturase.
DR   NCBIfam; TIGR02731; phytoene_desat; 1.
DR   PANTHER; PTHR42923:SF41; 15-CIS-PHYTOENE DESATURASE, CHLOROPLASTIC/CHROMOPLASTIC-RELATED; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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
//
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