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Database: UniProt
Entry: B1NYI4_NICBE
LinkDB: B1NYI4_NICBE
Original site: B1NYI4_NICBE 
ID   B1NYI4_NICBE            Unreviewed;       586 AA.
AC   B1NYI4;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, 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:ABY25272.1};
GN   Synonyms=NbPDSa {ECO:0000313|EMBL:BCG50295.1};
OS   Nicotiana benthamiana.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4100 {ECO:0000313|EMBL:ABY25272.1};
RN   [1] {ECO:0000313|EMBL:ABY25272.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18211705; DOI=10.1186/1746-4811-4-5;
RA   Liu E., Page J.E.;
RT   "Optimized cDNA libraries for virus-induced gene silencing (VIGS) using
RT   tobacco rattle virus.";
RL   Plant Methods 4:5-5(2008).
RN   [2] {ECO:0000313|EMBL:BCG50295.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:BCG50295.1};
RA   Atsumi G., Matsumura T.;
RT   "Virus-mediated targeted DNA methylation illuminates the dynamics of
RT   methylation in an endogenous plant gene.";
RL   Submitted (APR-2020) 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; EU165355; ABY25272.1; -; mRNA.
DR   EMBL; LC543532; BCG50295.1; -; mRNA.
DR   AlphaFoldDB; B1NYI4; -.
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   ECO:0000313|EMBL:ABY25272.1}; Plastid {ECO:0000256|RuleBase:RU368016}.
FT   DOMAIN          120..561
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   586 AA;  65414 MW;  576695B6AFECE25E CRC64;
     MPQIGLVSAV NLRVQGNSAY LWSSRSSLGT ESQDVCLQRN LLCFGSSDSM GHKLRIRTPS
     ATTRRLTKDF NPLKVVCIDY PRPELDNTVN YLEAALLSSS FRTSSRPTKP LEIVIAGAGL
     GGLSTAKYLA DAGHKPILLE ARDVLGGKVA AWKDDDGDWY ETGLHIFFGA YPNMQNLFGE
     LGIDDRLQWK EHSMIFAMPN KPGEFSRFDF PEALPAPLNG ILAILKNNEM LTWPEKVKFA
     IGLLPAMLGG QSYVEAQDGL SVKDWMRKQG VPDRVTDEVF IAMSKALNFI NPDELSMQCI
     LIALNRFLQE KHGSKMAFLD GNPPERLCMP IVEHIESKGG QVRLNSRIKK IELNEDGSVK
     CFILNNGSTI KGDAFVFATP VDILKLLLPE DWKEIPYFQK LEKLVGVPVI NVHIWFDRKL
     KNTSDNLLFS RSPLLSVYAD MSVTCKEYYN PNQSMLELVF APAEEWINRS DSEIIDATMK
     ELAKLFPDEI SADQSKAKIL KYHVVKTPRS VYKTVPGCEP CRPLQRSPIE GFYLAGDYTK
     QKYLASMEGA VLSGKLCAEA IVQDYELLLG RSQKMLAEAS VVSIVN
//
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