ID   PDS_ONCHC               Reviewed;         582 AA.
AC   C3VEP9; Q52QW4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=15-cis-phytoene desaturase, chloroplastic/chromoplastic {ECO:0000305};
DE            EC=1.3.5.5 {ECO:0000250|UniProtKB:A2XDA1};
DE   AltName: Full=Phytoene dehydrogenase {ECO:0000305};
DE            Short=OgPDS {ECO:0000303|PubMed:20635095};
DE   AltName: Full=Phytoene desaturase;
DE   Flags: Precursor;
GN   Name=PDS;
OS   Oncidium hybrid cultivar (Orchid).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Cymbidieae; Oncidiinae; Oncidium.
OX   NCBI_TaxID=141207;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=20635095; DOI=10.1007/s00425-010-1222-x;
RA   Chiou C.Y., Pan H.A., Chuang Y.N., Yeh K.W.;
RT   "Differential expression of carotenoid-related genes determines diversified
RT   carotenoid coloration in floral tissues of Oncidium cultivars.";
RL   Planta 232:937-948(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 167-444, AND TISSUE SPECIFICITY.
RX   PubMed=16151849; DOI=10.1007/s00425-005-0113-z;
RA   Hieber A.D., Mudalige-Jayawickrama R.G., Kuehnle A.R.;
RT   "Color genes in the orchid Oncidium Gower Ramsey: identification,
RT   expression, and potential genetic instability in an interspecific cross.";
RL   Planta 223:521-531(2006).
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:0000250|UniProtKB:A2XDA1}.
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:0000250|UniProtKB:A2XDA1};
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   -!- TISSUE SPECIFICITY: Expressed in flower buds and lips. Lower expression
CC       in leaves and roots. {ECO:0000269|PubMed:16151849,
CC       ECO:0000269|PubMed:20635095}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during floral development.
CC       {ECO:0000269|PubMed:20635095}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; FJ859989; ACP27624.1; -; mRNA.
DR   EMBL; AY973632; AAX84687.1; -; mRNA.
DR   AlphaFoldDB; C3VEP9; -.
DR   SMR; C3VEP9; -.
DR   PRIDE; C3VEP9; -.
DR   UniPathway; UPA00803; -.
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:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0016166; F:phytoene dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0016120; P:carotene biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0051289; P:protein homotetramerization; ISS: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   2: Evidence at transcript level;
KW   Carotenoid biosynthesis; Chloroplast; Chromoplast; Membrane;
KW   Oxidoreductase; Plastid; Transit peptide.
FT   TRANSIT         1..93
FT                   /note="Chloroplast and chromoplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           94..582
FT                   /note="15-cis-phytoene desaturase,
FT                   chloroplastic/chromoplastic"
FT                   /id="PRO_0000426708"
FT   BINDING         121
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         140..141
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         148
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         165..166
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         171
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         537
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         545
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         547
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
SQ   SEQUENCE   582 AA;  65356 MW;  195109C427C11A79 CRC64;
     MNLLGSISTG FPCISLHKKS LRDENPARKR LIDMDPRWNK LRASRSSDYM GCIFEVPLLG
     FSKVKSSSAN GSMQVFCMDY PRPELENTIN FLEAAKLSAS FRDSIRPKKP LEVVIAGAGL
     AGLSTAKYLA DAGHKPILLE ARDVLGGKIA AWKDKDGDFY ETGLHIFFGA YPNVQNLFGE
     LGINDRLQWK EHSMIFAMPN KPGEFSRFDF PDVLPAPFNG IWAILRNNEM LTWSEKVKFA
     IGLLPAMVGG QSYVEAQDSL TVKEWMKRQG VPVRVNDEVF IAMSKALNFI NPDELSMQCI
     LIALNRFLQE KHGSKIAFLD GNPPERLCMP IVEHIRSLGG QVELNSRVQK IELNSDRTVK
     KFVLNNGSVI TGDAYVFATP VDILKLLLPE EWKEISCFQR LNKLAGVPVI NVHLWFDRKL
     KNTYDHLLFS RSPLLSVYAD MSVTCKEYYD PNRSMLELVF APADEWISRS DSDIVDATLK
     ELAKLFPNEI AADQSKAKLL KYHVVKTPRS VYKTVPNCEP CRPLQRTPIK GFYLAGDYTK
     QKYLASMEGA VLSGKLCAQA IVQDYDKLVS TAVGDQSAEM FV