PDS_MAIZE
ID PDS_MAIZE Reviewed; 571 AA.
AC P49086; Q41849;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
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; Synonyms=PDS;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8616251; DOI=10.1007/bf00020113;
RA Li Z., Matthews P.D., Burr B., Wurtzel E.T.;
RT "Cloning and characterization of a maize cDNA encoding phytoene desaturase,
RT an enzyme of the carotenoid biosynthetic pathway.";
RL Plant Mol. Biol. 30:269-279(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Funk F; TISSUE=Leaf;
RX PubMed=7630964; DOI=10.1104/pp.108.3.1329;
RA Hable W.E., Oishi K.K.;
RT "Maize phytoene desaturase maps near the viviparous5 locus.";
RL Plant Physiol. 108:1329-1330(1995).
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; U37285; AAC12846.1; -; mRNA.
DR EMBL; L39266; AAA99519.1; -; mRNA.
DR PIR; S65060; S65060.
DR RefSeq; NP_001105381.1; NM_001111911.1.
DR AlphaFoldDB; P49086; -.
DR SMR; P49086; -.
DR STRING; 4577.GRMZM2G410515_P01; -.
DR PaxDb; P49086; -.
DR PRIDE; P49086; -.
DR MaizeGDB; 84977; -.
DR eggNOG; KOG0029; Eukaryota.
DR BRENDA; 1.3.5.5; 6752.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P49086; 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: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; Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..96
FT /note="Chloroplast and chromoplast"
FT /evidence="ECO:0000255"
FT CHAIN 97..571
FT /note="15-cis-phytoene desaturase,
FT chloroplastic/chromoplastic"
FT /id="PRO_0000006325"
FT BINDING 107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 126..127
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 134
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 151..152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 334
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 523
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 531
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 533
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT CONFLICT 61..63
FT /note="VVC -> LSA (in Ref. 2; AAA99519)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="R -> S (in Ref. 2; AAA99519)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="A -> T (in Ref. 2; AAA99519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 64116 MW; FAE119C7EFBE799A CRC64;
MDTGCLSSMN ITGASQTRSF AGQLPPQRCF ASSHYTSFAV KKLVSRNKGR RSHRRHPALQ
VVCKDFPRPP LESTINYLEA GQLSSFFRNS ERPSKPLQVV VAGAGLAGLS TAKYLADAGH
KPILLEARDV LGGKVAAWKD EDGDWYETGL HIFFGAYPNI QNLFGELRIE DRLQWKEHSM
IFAMPNKPGE FSRFDFPETL PAPINGIWAI LRNNEMLTWP EKVKFAIGLL PAMVGGQPYV
EAQDGLTVSE WMKKQGVPDR VNDEVFIAMS KALNFINPDE LSMQCILIAL NRFLQEKHGS
KMAFLDGNPP ERLCMPIVDH IRSRGGEVRL NSRIKKIELN PDGTVKHFAL SDGTQITGDA
YVCATPVDIF KLLVPQEWSE ITYFKKLEKL VGVPVINVHI WFDRKLNNTY DHLLFSRSSL
LSVYADMSVT CKEYYDPNRS MLELVFAPAD EWIGRSDTEI IDATMEELAK LFPDEIAADQ
SKAKILKYHI VKTPRSVYKT VPNCEPCRPL QRSPIEGFYL AGDYTKQKYL ASMEGAVLSG
KLCAQSIVQD YSRLALRSQK SLQSGEVPVP S
