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
//