ID A0A1J1LH79_9CYAN Unreviewed; 478 AA.
AC A0A1J1LH79;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:CUR31574.1};
GN ORFNames=PL9214291165 {ECO:0000313|EMBL:CUR31574.1};
OS Planktothrix tepida PCC 9214.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=671072 {ECO:0000313|EMBL:CUR31574.1, ECO:0000313|Proteomes:UP000184315};
RN [1] {ECO:0000313|Proteomes:UP000184315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Regsiter A., william w.;
RL Submitted (OCT-2015) 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; CZDF01000132; CUR31574.1; -; Genomic_DNA.
DR RefSeq; WP_072718397.1; NZ_LN889782.1.
DR AlphaFoldDB; A0A1J1LH79; -.
DR STRING; 671072.PL9214291165; -.
DR OrthoDB; 438203at2; -.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000184315; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184315}.
FT DOMAIN 10..451
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 478 AA; 53688 MW; 683253274233D5A9 CRC64;
MRVAIAGAGL AGLACAKYLT DLGHTPIVLE RRDVLGGKVA AWKDEDGDWY ETGLHIFFGA
YPNMLQLFKE LDIEDRLQWK EHSMIFNQPE KPGTYSRFDF PNLPAPFNGV VAILRNNDML
TWPEKIRFGL GLIPAMLQGQ KYVEEMDKYS FSEWLKLHNV PPRVEKEVFI AMSKALNFIN
PDEISSTVIL TALNRFLQEK NGSKMAFLDG SPTERLCQPL VDYITERGGE VRLNAPIKEF
LLNADGTVKG FLIRGLNDTP DQVLTADLYV SAMPVDPLKV MLPQPWQEMD YFKQLEGLEG
VPVINVHLWF DRKLTNVDHL LFSRSPLLSV YADMSNTCKE YSNPDRSMLE LVLAPAKDWI
SKSDEDIVAA TMAELEKLFP EEIPHPAKLL KSHVVKTPRS VYKATPGRQA HRPSQKTPIP
NFYLTGDYTM QRYLASMEGA VLSGKLTAQA IQEDLTSDRF LALSAPSANV ASPSPIPS
//
