ID E7CZW9_BRANA Unreviewed; 564 AA.
AC E7CZW9;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
GN Name=PDS {ECO:0000313|EMBL:ADT89706.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:ADT89706.1};
RN [1] {ECO:0000313|EMBL:ADT89706.1}
RP NUCLEOTIDE SEQUENCE.
RA Tian L.S., Niu Y.Z., Guo S.X., Yan C.X.;
RT "Cloning and sequence analysis of the phytoene desaturase cDNA from a
RT resynthesized white-flower rapeseed line (Brassica napus L.).";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADT89707.1}
RP NUCLEOTIDE SEQUENCE.
RA Tian L.S., Niu Y.Z., Guo S.X., Yan C.X.;
RT "Cloning and sequence analysis of the phytoene desaturase gene from a
RT resynthesized white-flower rapeseed line (Brassica napus L.).";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU368016}.
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:0000256|ARBA:ARBA00001534,
CC ECO:0000256|RuleBase:RU368016};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU368016};
CC -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004900, ECO:0000256|RuleBase:RU368016}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU368016}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU368016}. Plastid, chromoplast
CC {ECO:0000256|ARBA:ARBA00004260, ECO:0000256|RuleBase:RU368016}.
CC Membrane {ECO:0000256|RuleBase:RU368016}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU368016}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006046, ECO:0000256|RuleBase:RU368016}.
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DR EMBL; HM989806; ADT89706.1; -; mRNA.
DR EMBL; HM989807; ADT89707.1; -; Genomic_DNA.
DR RefSeq; NP_001303137.1; NM_001316208.1.
DR AlphaFoldDB; E7CZW9; -.
DR GeneID; 106361559; -.
DR KEGG; bna:106361559; -.
DR OrthoDB; 3597164at2759; -.
DR UniPathway; UPA00803; -.
DR ExpressionAtlas; E7CZW9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016166; F:phytoene dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR014102; Phytoene_desaturase.
DR NCBIfam; TIGR02731; phytoene_desat; 1.
DR PANTHER; PTHR42923:SF38; PHYTOENE DEHYDROGENASE; 1.
DR PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 2: Evidence at transcript level;
KW Carotenoid biosynthesis {ECO:0000256|RuleBase:RU368016};
KW Chloroplast {ECO:0000256|RuleBase:RU368016};
KW Chromoplast {ECO:0000256|ARBA:ARBA00022904};
KW Membrane {ECO:0000256|RuleBase:RU368016};
KW Oxidoreductase {ECO:0000256|RuleBase:RU368016};
KW Plastid {ECO:0000256|RuleBase:RU368016}.
FT DOMAIN 100..542
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 564 AA; 63031 MW; 4443E5C49E2B34C2 CRC64;
MVVFGNVSAA NLPYQNGFLK AISSGGCDLM GHRSFKISTS FKTTRRRRSA GPLQVVCVDI
PRPELENTVN FLEAASLSAS FRSAPRPAKP LKVVIAGAGL AGLSTAKYLA DAGHKPLLLE
ARDVLGGKIA AWKDEDGDWY ETGLHIFFGA YPNVQNLFGE LGINDRLQWK EHSMIFAMPS
KPGEFSRFDF PDVLPAPLNG IWAILRNNEM LTWPEKIKFA IGLLPAMVGG QAYVEAQDGL
SVEQWMRKQG VPDRVTDEVF IAMSKALNFI NPDELSMQCI LIALNRFLQE KHGSKMAFLD
GNPPERLCMP IVEHIRSLGG EVRLNSRIRK IELEDDGTVK SFLLTDGTTI QGDAYVFATP
VDILKLLLPD SWKEIPYFKR LEKLVGVPVI NVHIWFDKKL KNTYDHLLFS RSNLLSVYAD
MSLTCKEYYD PNRSMLELVF APAEEWISRS DSDIIDATMK ELERLFPDEI AADQSKAKIL
KYHVVKTPRS VYKTIPDCEP CRPLQRSPIK GFYLAGDYTK QKYLASMEGA VLSGKFCSQS
ILQDYELLAA SSGPQKLSET TLST
//
