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Database: UniProt
Entry: C7DR84_BRACM
LinkDB: C7DR84_BRACM
Original site: C7DR84_BRACM 
ID   C7DR84_BRACM            Unreviewed;       563 AA.
AC   C7DR84;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 35.
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:ACT20709.1};
OS   Brassica campestris (Field mustard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3711 {ECO:0000313|EMBL:ACT20709.1};
RN   [1] {ECO:0000313|EMBL:ACT20709.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu X.M., Xue L.;
RT   "Carotenoid content and composition of the genetic analysis and the genetic
RT   identification of the related genes in B. napus.";
RL   Submitted (MAY-2009) 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; GQ200741; ACT20709.1; -; mRNA.
DR   AlphaFoldDB; C7DR84; -.
DR   UniPathway; UPA00803; -.
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:SF41; 15-CIS-PHYTOENE DESATURASE, CHLOROPLASTIC/CHROMOPLASTIC-RELATED; 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|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368016};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU368016};
KW   Plastid {ECO:0000256|RuleBase:RU368016}.
FT   DOMAIN          100..541
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   563 AA;  63089 MW;  826828DA7657F9ED CRC64;
     MVVFGNVSAA NLPYQNVFLE ALSSELMGHS SFRVPISSQA LKTRTRRRTA GPLQVVCVDI
     PRPELENTVN FLEAASLSAS FRSAPRPAKP LKVVIAGAGL AGLSTAKYLA DAGHQPLLLE
     ARDVLGGKIA AWKDEDGDWY ETGLHIFFGA YPNVQNLFGE LGINDRLQWK EHSMIFAMPS
     KPGEFSRFDF PDVLPAPLNG IWAILRNNEM LTWPEKIKFA IGLLPAMVGG QAYVEAQDGL
     SVEEWMRKQA VPDRVTDEVF IAMSKALNFI NPNELSMQCI LIALNRFLQE KHGSKMAFLD
     GNPPERLCMP IVEHIRSLGG EVRLNSRIRK IELEDDGTVK NFLLTDGTTI QGDAYVFATP
     VDILKLLLPD SWKEIPYFKK LEKLVGVPVI NVHIWFDRKL KNTYDHLLFS RSNLLSVYAD
     MSLTCKEYYD PNRSMLELVF APAEEWISRT DSDIIDATMK ELEKLFPDEI AADQSKAKIL
     KYHVVKTPRS VYKTIPDCEP CRPLQRSPIQ GFYLAGDYTK QKYLASMEGA VLSGKFCSQS
     IVQDYELLAA SGRRNLSETT VST
//
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