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
//