ID A8G2E9_PROM2 Unreviewed; 466 AA.
AC A8G2E9;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
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:ABV49780.1};
GN OrderedLocusNames=P9215_01611 {ECO:0000313|EMBL:ABV49780.1};
OS Prochlorococcus marinus (strain MIT 9215).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=93060 {ECO:0000313|EMBL:ABV49780.1, ECO:0000313|Proteomes:UP000002014};
RN [1] {ECO:0000313|EMBL:ABV49780.1, ECO:0000313|Proteomes:UP000002014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9215 {ECO:0000313|EMBL:ABV49780.1,
RC ECO:0000313|Proteomes:UP000002014};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000825; ABV49780.1; -; Genomic_DNA.
DR RefSeq; WP_002805422.1; NC_009840.1.
DR AlphaFoldDB; A8G2E9; -.
DR STRING; 93060.P9215_01611; -.
DR KEGG; pmh:P9215_01611; -.
DR eggNOG; COG0493; Bacteria.
DR eggNOG; COG3349; Bacteria.
DR HOGENOM; CLU_022687_1_0_3; -.
DR OrthoDB; 438203at2; -.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000002014; 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; PROTOPORPHYRINOGEN OXIDASE; 1.
DR PANTHER; PTHR42923:SF3; 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|RuleBase:RU368016};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU368016}.
FT DOMAIN 10..453
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 466 AA; 52605 MW; 3F779BBE53E7C95A CRC64;
MRVVIAGAGL AGLSCAKYLV DNGHIPIVLE ARDVLGGKVA AWKDEDGDWY ETGLHIFFGA
YPNMLQLFKE LDIEDRLQWK SHSMIFNQPS EPGTYSRFDF PDIPAPVNGV SAILSNNDML
SWNEKILFGL GLVPAMLRGQ KYLDKCDTKS WTDWLKEHNI PERVNDEVFI AMSKALNFIG
PDEISSTVLL TALNRFLQEK NGSKMAFLDG APPERLCQPM VDYITARGGE VHMNSPLRQI
NLNEDSTVKS FTIASLDKKE KKELTADAYV SAMPVDLFKL MIPKQWKGLD AFSKLDGLNG
VPVINIHLWF DKKLTDIDHL LFSRSPLLSV YADMSITCKE YEDPNRSMLE LVFAPAKDWI
NRSDQDIIDA TMEELKKLFP THFIGEDKTK LRKYKVVKTP RSVYKAVPGC QNFRPSQKSP
IKNFFLTGDY TMQKYLASME GAVLSGKLCA ESIHKENSKT LQNVSK
//
