PDS_SOYBN
ID PDS_SOYBN Reviewed; 570 AA.
AC P28553;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 AltName: Full=Phytoene desaturase {ECO:0000305};
DE Flags: Precursor;
GN Name=PDS1;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=1862081; DOI=10.1073/pnas.88.15.6532;
RA Bartley G.E., Viitanen P.V., Pecker I., Chamovitz D., Hirschberg J.,
RA Scolnik P.A.;
RT "Molecular cloning and expression in photosynthetic bacteria of a soybean
RT cDNA coding for phytoene desaturase, an enzyme of the carotenoid
RT biosynthesis pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6532-6536(1991).
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 -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; M64704; AAA34001.1; -; mRNA.
DR PIR; A39597; A39597.
DR RefSeq; NP_001236769.1; NM_001249840.1.
DR AlphaFoldDB; P28553; -.
DR SMR; P28553; -.
DR STRING; 3847.GLYMA18G00720.1; -.
DR PRIDE; P28553; -.
DR GeneID; 547970; -.
DR KEGG; gmx:547970; -.
DR eggNOG; KOG0029; Eukaryota.
DR InParanoid; P28553; -.
DR OrthoDB; 1151887at2759; -.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000008827; Unplaced.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR014102; Phytoene_desaturase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02731; phytoene_desat; 1.
PE 2: Evidence at transcript level;
KW Carotenoid biosynthesis; Chloroplast; Chromoplast; FAD; Flavoprotein;
KW Membrane; NAD; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..98
FT /note="Chloroplast and chromoplast"
FT /evidence="ECO:0000255"
FT CHAIN 99..570
FT /note="15-cis-phytoene desaturase,
FT chloroplastic/chromoplastic"
FT /id="PRO_0000006328"
FT BINDING 105..121
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 109
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 128..129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 153..154
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 336
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 525
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 533
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 535
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
SQ SEQUENCE 570 AA; 63595 MW; E4CF0B43B76AE845 CRC64;
MAACGYISAA NFNYLVGARN ISKFASSDAT ISFSFGGSDS MGLTLRPAPI RAPKRNHFSP
LRVVCVDYPR PELENTVNFV EAAYLSSTFR ASPRPLKPLN IVIAGAGLAG LSTAKYLADA
GHKPILLEAR DVLGGKVAAW KDKDGDWYET GLHIFFGAYP YVQNLFGELG INDRLQWKEH
SMIFAMPNKP GEFSRFDFPE VLPSPLNGIW AILRNNEMLT WPEKVKFAIG LLPAMLGGQP
YVEAQDGLSV QEWMKKQGVP ERVADEVFIA MSKALNFINP DELSMQCILI ALNRFLQEKH
GSKMAFLDGN PPERLCMPIV DYIQSLGGEV HLNSRIQKIE LNDDGTVKSF LLNNGKVMEG
DAYVFATPVD ILKLLLPDNW KGIPYFQRLD KLVGVPVINV HIWFDRKLKN TYDHLLFSRS
PLLSVYADMS VTCKEYYSPN QSMLELVFAP AEEWISRSDD DIIQATMTEL AKLFPDEISA
DQSKAKILKY HVVKTPRSVY KTVPNCEPCR PIQRSPIEGF YLAGDYTKQK YLASMEGAVL
SGKLCAQAIV QDSELLATRG QKRMAKASVV
