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Database: UniProt
Entry: Q1KMK7_NICBE
LinkDB: Q1KMK7_NICBE
Original site: Q1KMK7_NICBE 
ID   Q1KMK7_NICBE            Unreviewed;       586 AA.
AC   Q1KMK7;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE            EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
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:ABE99707.1};
RN   [1] {ECO:0000313|EMBL:ABE99707.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Muthappa S.-K., Anand A., Makarla U., Mysore K.S.;
RT   "Assessing the efficiency of silencing of heterologous PDS gene probes in
RT   Nicotiana benthamiana by virus induced gene silencing (VIGS).";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABE99707.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17997764; DOI=10.1111/j.1469-8137.2007.02225.x;
RA   Senthil-Kumar M., Hema R., Anand A., Kang L., Udayakumar M., Mysore K.S.;
RT   "A systematic study to determine the extent of gene silencing in Nicotiana
RT   benthamiana and other Solanaceae species when heterologous gene sequences
RT   are used for virus-induced gene silencing.";
RL   New Phytol. 176:782-791(2007).
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; DQ469932; ABE99707.1; -; mRNA.
DR   AlphaFoldDB; Q1KMK7; -.
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          120..561
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   586 AA;  65413 MW;  576695A3EEB8E25E 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 VLSGKLCAQA IVQDYELLLG RSQKMLAEAS VVSIVN
//
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