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Database: UniProt
Entry: Q3B057_SYNS9
LinkDB: Q3B057_SYNS9
Original site: Q3B057_SYNS9 
ID   Q3B057_SYNS9            Unreviewed;       472 AA.
AC   Q3B057;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE            EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
GN   OrderedLocusNames=Syncc9902_0298 {ECO:0000313|EMBL:ABB25271.1};
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB25271.1, ECO:0000313|Proteomes:UP000002712};
RN   [1] {ECO:0000313|Proteomes:UP000002712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme converts phytoene into zeta-carotene via the
CC       intermediary of phytofluene by the symmetrical introduction of two
CC       double bonds at the C-11 and C-11' positions of phytoene.
CC       {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|RuleBase:RU368016};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU368016};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|RuleBase:RU368016};
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000256|RuleBase:RU368016};
CC   -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004900, ECO:0000256|RuleBase:RU368016}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU368016};
CC       Peripheral membrane protein {ECO:0000256|RuleBase:RU368016}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00006046, ECO:0000256|RuleBase:RU368016}.
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DR   EMBL; CP000097; ABB25271.1; -; Genomic_DNA.
DR   RefSeq; WP_011359129.1; NC_007513.1.
DR   AlphaFoldDB; Q3B057; -.
DR   STRING; 316279.Syncc9902_0298; -.
DR   KEGG; sye:Syncc9902_0298; -.
DR   eggNOG; COG0493; Bacteria.
DR   eggNOG; COG3349; Bacteria.
DR   HOGENOM; CLU_022687_1_0_3; -.
DR   OMA; HSMIFNQ; -.
DR   OrthoDB; 438203at2; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000002712; Chromosome.
DR   GO; GO:0005886; C:plasma 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis {ECO:0000256|ARBA:ARBA00022746,
KW   ECO:0000256|RuleBase:RU368016};
KW   Cell membrane {ECO:0000256|RuleBase:RU368016};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU368016,
KW   ECO:0000313|EMBL:ABB25271.1}.
FT   DOMAIN          10..453
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   472 AA;  52347 MW;  6EE8DD787B6A188F CRC64;
     MRVAIAGAGL AGLSCAKYLA DAGHTPILVE SRDVLGGKVA AWKDEDGDWY ETGLHIFFGA
     YPNMLQLFKE LDIEDRLQWK SHSMIFNQPE EPGTYSRFDF PDLPAPVNGV AAILGNNDML
     TWPEKISFGL GLVPAMLRGQ GYVEQCDQYS WTEWLRLHNI PERVNDEVFI AMSKALNFID
     PGEISATVLL TALNRFLQEK NGSRMAFLDG APPERLCQPV VEHIESLGGE VHLDCPLREI
     KLNDDGSVAA FQIGGVKGKE GFDLVADAYV SALPVDPFKL LLPEPWKQMD VFQKLEGLRG
     VPVINIHMWF DRKLTDIDHL LFSRSPLLSV YADMSIACKE YEDPDRSMLE LVFAPAKDWI
     SRSDEDIIEA TMGELLKLFP MHFGGDNPAK LRKSKVVKTP LSVYKTTPGC QQLRPDQTTP
     IKNFFLAGDY TMQRYLASME GAVLSGKLCA GAVDAKTDQL SKSSSVGEPV TA
//
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