ID A2BNT8_PROMS Unreviewed; 466 AA.
AC A2BNT8;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
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:ABM69449.1};
GN OrderedLocusNames=A9601_01611 {ECO:0000313|EMBL:ABM69449.1};
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=146891 {ECO:0000313|EMBL:ABM69449.1, ECO:0000313|Proteomes:UP000002590};
RN [1] {ECO:0000313|EMBL:ABM69449.1, ECO:0000313|Proteomes:UP000002590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601 {ECO:0000313|EMBL:ABM69449.1,
RC ECO:0000313|Proteomes:UP000002590};
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; CP000551; ABM69449.1; -; Genomic_DNA.
DR RefSeq; WP_011817636.1; NC_008816.1.
DR AlphaFoldDB; A2BNT8; -.
DR STRING; 146891.A9601_01611; -.
DR KEGG; pmb:A9601_01611; -.
DR eggNOG; COG0493; Bacteria.
DR eggNOG; COG3349; Bacteria.
DR HOGENOM; CLU_022687_1_0_3; -.
DR OrthoDB; 438203at2; -.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000002590; 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; 52498 MW; 8DD60AAE3B268160 CRC64;
MRVVIAGAGL AGLSCAKYLV DNGHIPIVLE ARDVLGGKVA AWKDEDGDWY ETGLHIFFGA
YPNMLQLFKE LDIEDRLQWK SHSMIFNQPS EPGTYSRFDF PDIPAPVNGV SAILSNNDML
SWNEKILFGL GLVPAMLRGQ KYLDKCDTKS WTDWLKEHNI PERVNDEVFI AMSKALNFIG
PDEISSTVLL TALNRFLQEK NGSKMAFLDG APPERLCQPI VDYITARGGE VHMNSPLREI
NLNEDSTVKS FTVASLDKNE KKELTADAYV SAMPVDLFKL MIPKQWKGLD AFSKLDGLNG
VPVINIHLWF DKKLTDIDHL LFSRSPLLSV YADMSITCKE YEDPNRSMLE LVFAPAKDWI
NRSEQDIVNA TMEELKKLFP THFMGDDKTN LRKYKVVKTP RSVYKAVPGC QEFRPSQKSP
IKNFFLAGDY TMQKYLASME GAVLSGKLCA ESINKEYSKI PQNVSA
//
