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Database: UniProt
Entry: Q063L3_9SYNE
LinkDB: Q063L3_9SYNE
Original site: Q063L3_9SYNE 
ID   Q063L3_9SYNE            Unreviewed;       472 AA.
AC   Q063L3;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE            EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
GN   ORFNames=BL107_05149 {ECO:0000313|EMBL:EAU70889.1};
OS   Synechococcus sp. BL107.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=313625 {ECO:0000313|EMBL:EAU70889.1, ECO:0000313|Proteomes:UP000004390};
RN   [1] {ECO:0000313|EMBL:EAU70889.1, ECO:0000313|Proteomes:UP000004390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL107 {ECO:0000313|EMBL:EAU70889.1,
RC   ECO:0000313|Proteomes:UP000004390};
RA   Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (OCT-2006) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAU70889.1}.
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DR   EMBL; AATZ01000002; EAU70889.1; -; Genomic_DNA.
DR   RefSeq; WP_009788257.1; NZ_DS022298.1.
DR   AlphaFoldDB; Q063L3; -.
DR   STRING; 313625.BL107_05149; -.
DR   eggNOG; COG0493; Bacteria.
DR   eggNOG; COG3349; Bacteria.
DR   HOGENOM; CLU_022687_1_0_3; -.
DR   OrthoDB; 438203at2; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000004390; Unassembled WGS sequence.
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}.
FT   DOMAIN          10..453
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   472 AA;  52432 MW;  F452337F071D453F CRC64;
     MRVAIAGAGL AGLSCAKYLA DAGHTPILVE SRDVLGGKVA AWKDEDGDWY ETGLHIFFGA
     YPNMLQLFKE LNIEDRLQWK SHSMIFNQPE EPGTYSRFDF PDLPAPVNGV AAILGNNDML
     TWPEKISFGL GLVPAMLRGQ GYVEQCDQYS WTEWLRLHNI PERVNDEVFI AMSKALNFID
     PGEISATVLL TALNRFLQEK NGSRMAFLDG APPERLCQPV VEHIESLGGE VHLDCPLREI
     KLNDDGSVAA FQIGGVKGKE GFDLVADAYV SALPVDPFKL LLPEPWKQME VFRKLDGLRG
     VPVINIHMWF DRKLTDIDHL LFSRSPLLSV YADMSIACKE YEDPDRSMLE LVFAPAKDWI
     SRSDEDIIEA TMGELLKLFP MHFSGDNPAK LRKSKVVKTP LSVYKTTPGC QQLRPDQTTP
     IKNFFLAGDY TMQRYLASME GAVLSGKLCA GAVDAKTDQL SQSSSVGEPV TV
//
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