PDS_NARPS
ID PDS_NARPS Reviewed; 570 AA.
AC Q40406;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=15-cis-phytoene desaturase, chloroplastic/chromoplastic {ECO:0000305};
DE EC=1.3.5.5 {ECO:0000269|PubMed:29176862, ECO:0000269|PubMed:8653112};
DE AltName: Full=Phytoene dehydrogenase {ECO:0000305};
DE AltName: Full=Phytoene desaturase {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=PDS1; Synonyms=PDS;
OS Narcissus pseudonarcissus (Daffodil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC Amaryllidoideae; Narcissus.
OX NCBI_TaxID=39639;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Paracorolla;
RA Al-Babili S., Beyer P.;
RT "A cDNA encoding phytoene desaturase from daffodil.";
RL (er) Plant Gene Register PGR95-131(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Paracorolla;
RX PubMed=8653112; DOI=10.1046/j.1365-313x.1996.9050601.x;
RA Al-Babili S., von Lintig J., Haubruck H., Beyer P.;
RT "A novel, soluble form of phytoene desaturase from Narcissus
RT pseudonarcissus chromoplasts is Hsp70-complexed and competent for
RT flavinylation, membrane association and enzymatic activation.";
RL Plant J. 9:601-612(1996).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=9288918; DOI=10.1111/j.1432-1033.1997.00942.x;
RA Bonk M., Hoffmann B., von Lintig J., Schledz M., Al-Babili S., Hobeika E.,
RA Kleinig H., Beyer P.;
RT "Chloroplast import of four carotenoid biosynthetic enzymes in vitro
RT reveals differential fates prior to membrane binding and oligomeric
RT assembly.";
RL Eur. J. Biochem. 247:942-950(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=29176862; DOI=10.1371/journal.pone.0187628;
RA Koschmieder J., Fehling-Kaschek M., Schaub P., Ghisla S., Brausemann A.,
RA Timmer J., Beyer P.;
RT "Plant-type phytoene desaturase: Functional evaluation of structural
RT implications.";
RL PLoS ONE 12:E0187628-E0187628(2017).
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:29176862, ECO:0000269|PubMed:8653112}.
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:29176862, ECO:0000269|PubMed:8653112};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:8653112};
CC -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:A2XDA1}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:9288918}. Plastid, chromoplast
CC {ECO:0000269|PubMed:29176862, ECO:0000269|PubMed:8653112,
CC ECO:0000269|PubMed:9288918}. Membrane {ECO:0000269|PubMed:8653112,
CC ECO:0000269|PubMed:9288918}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:A2XDA1}. Note=Exists as an inactive soluble form
CC and an active membrane-bound form. {ECO:0000269|PubMed:8653112}.
CC -!- TISSUE SPECIFICITY: Expressed more strongly in flowers than in leaves.
CC {ECO:0000269|PubMed:8653112}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during flower development.
CC {ECO:0000269|PubMed:8653112}.
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; X78815; CAA55392.1; -; mRNA.
DR PIR; S54134; S54134.
DR AlphaFoldDB; Q40406; -.
DR SMR; Q40406; -.
DR UniPathway; UPA00803; -.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009509; C:chromoplast; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016166; F:phytoene dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR InterPro; IPR014102; Phytoene_desaturase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02731; phytoene_desat; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Chloroplast; Chromoplast; FAD; Flavoprotein;
KW Membrane; Oxidoreductase; Plastid; Transit peptide.
FT TRANSIT 1..91
FT /note="Chloroplast and chromoplast"
FT /evidence="ECO:0000255"
FT CHAIN 92..570
FT /note="15-cis-phytoene desaturase,
FT chloroplastic/chromoplastic"
FT /id="PRO_0000006326"
FT BINDING 104..120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 127..128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 152..153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 158
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 524
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 532
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 534
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
SQ SEQUENCE 570 AA; 63791 MW; 654F569F5B83BE77 CRC64;
MSIVGLVSVV CPSGGIKKRY FSKGLDNFQG FRSSECLGIQ LQVPVPFYSG IRQSPRATSL
QVVCKDCPRP ELEGAVNFLE AAQLSASFRS SPRPEKGLEV VVVGAGLAGL STAKYLADAG
HKPILLESRD VLGGKIAAWK DKDGDWYETG LHIFFGAYPN VQNLFGELGI NDRLQWKEHS
MIFAMPNKPG EFSRFDFPEV LPAPLNGIWA ILRNNEMLTW PEKVRFAIGL LPAMVGGQAY
VEAQDGLTVT EWMRRQGVPD RVNDEVFIAM SKALNFINPD ELSMQCILIA LNRFLQEKHG
SKMAFLDGNP PERLCMPIVD HIQSLGGRAQ LNSRLQKIEL NPDGTVKHFV LGNGNIITGD
AYVVAAPVDI LKLLLPQEWR EIPYFQKLDK LVGVPVINVH IWFDRKLKNT YDHLLFTRSP
LLSVYADMSV TCKEYYDPNR SMLELVFAPA EEWISRSDSE IIERTMKELA KLFPDEIAAD
QSKAKILKYH VVKTPRSVYK TIPDCEPCRP LQRSPIEGFY LAGDYTNQKY LASMEGAVLS
GKLCAQSIVQ DYELLVRRSK KASTAEMTVV
