PDS_SOLLC
ID PDS_SOLLC Reviewed; 583 AA.
AC P28554;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=15-cis-phytoene desaturase, chloroplastic/chromoplastic {ECO:0000305};
DE EC=1.3.5.5 {ECO:0000269|PubMed:1594600};
DE AltName: Full=Phytoene dehydrogenase {ECO:0000305};
DE AltName: Full=Phytoene desaturase {ECO:0000305};
DE Flags: Precursor;
GN Name=PDS;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=1594600; DOI=10.1073/pnas.89.11.4962;
RA Pecker I., Chamovitz D., Hirschberg J.;
RT "A single polypeptide catalyzing the conversion of phytoene to zeta-
RT carotene is transcriptionally regulated during tomato fruit ripening.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4962-4966(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Ailsa Craig; TISSUE=Fruit;
RX PubMed=8485401; DOI=10.2307/3869719;
RA Bartley G.E., Scolnik P.A., Giuliano G.;
RT "Regulation of carotenoid biosynthesis during tomato development.";
RL Plant Cell 5:379-387(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8123786; DOI=10.1007/bf00024111;
RA Mann V., Pecker I., Hirschberg J.;
RT "Cloning and characterization of the gene for phytoene desaturase (Pds)
RT from tomato (Lycopersicon esculentum).";
RL Plant Mol. Biol. 24:429-434(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Ailsa Craig;
RX PubMed=7991692; DOI=10.1104/pp.106.2.789;
RA Aracri B., Bartley G.E., Scolnik P.A., Giuliano G.;
RT "Sequence of the phytoene desaturase locus of tomato.";
RL Plant Physiol. 106:789-789(1994).
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:1594600}.
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:1594600};
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 -!- 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; X59948; CAA42573.1; -; mRNA.
DR EMBL; M88683; AAA68865.1; -; mRNA.
DR EMBL; X71023; CAB59726.1; -; Genomic_DNA.
DR EMBL; X78271; CAA55078.1; -; Genomic_DNA.
DR PIR; A45381; A45381.
DR RefSeq; NP_001234095.1; NM_001247166.2.
DR RefSeq; XP_010318414.1; XM_010320112.1.
DR RefSeq; XP_019068139.1; XM_019212594.1.
DR AlphaFoldDB; P28554; -.
DR SMR; P28554; -.
DR STRING; 4081.Solyc03g123760.2.1; -.
DR PaxDb; P28554; -.
DR PRIDE; P28554; -.
DR EnsemblPlants; Solyc03g123760.3.1; Solyc03g123760.3.1; Solyc03g123760.3.
DR GeneID; 544073; -.
DR Gramene; Solyc03g123760.3.1; Solyc03g123760.3.1; Solyc03g123760.3.
DR KEGG; sly:544073; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_022687_1_0_1; -.
DR InParanoid; P28554; -.
DR OMA; THCFFGA; -.
DR OrthoDB; 1151887at2759; -.
DR PhylomeDB; P28554; -.
DR BRENDA; 1.3.5.5; 3101.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000004994; Chromosome 3.
DR ExpressionAtlas; P28554; baseline and differential.
DR GO; GO:0009507; C:chloroplast; ISS:UniProtKB.
DR GO; GO:0009509; C:chromoplast; ISS:UniProtKB.
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:UniProtKB.
DR GO; GO:0016120; P:carotene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IBA:GO_Central.
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 Carotenoid biosynthesis; Chloroplast; Chromoplast; FAD; Flavoprotein;
KW Membrane; Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..111
FT /note="Chloroplast and chromoplast"
FT /evidence="ECO:0000255"
FT CHAIN 112..583
FT /note="15-cis-phytoene desaturase,
FT chloroplastic/chromoplastic"
FT /id="PRO_0000006324"
FT BINDING 118..134
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 141..142
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 149
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 166..167
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 349
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 538
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 546
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 548
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT CONFLICT 508
FT /note="T -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 64885 MW; 9EA0DF71A2FA3A44 CRC64;
MPQIGLVSAV NLRVQGSSAY LWSSRSSSLG TESRDGCLQR NSLCFAGSES MGHKLKIRTP
HATTRRLVKD LGPLKVVCID YPRPELDNTV NYLEAAFLSS TFRASPRPTK PLEIVIAGAG
LGGLSTAKYL ADAGHKPILL EARDVLGGKV AAWKDDDGDW YETGLHIFFG AYPNIQNLFG
ELGINDRLQW KEHSMIFAMP SKPGEFSRFD FSEALPAPLN GILAILKNNE MLTWPEKVKF
AIGLLPAMLG GQSYVEAQDG ISVKDWMRKQ GVPDRVTDEV FIAMSKALNF INPDELSMQC
ILIALNRFLQ EKHGSKMAFL DGNPPERLCM PIVEHIESKG GQVRLNSRIK KIELNEDGSV
KSFILSDGSA IEGDAFVFAA PVDIFKLLLP EDWKEIPYFQ KLEKLVGVPV INVHIWFDRK
LKNTYDHLLF SRSSLLSVYA DMSVTCKEYY NPNQSMLELV FAPAEEWISR SDSEIIDATM
KELATLFPDE ISADQSKAKI LKYHVVKTPR SVYKTVPGCE PCRPLQRSPI EGFYLAGDYT
KQKYLASMEG AVLSGKLCAQ AIVQDYELLV GRSQKKLSEA SVV
