ID K9SLD9_9CYAN Unreviewed; 490 AA.
AC K9SLD9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
GN ORFNames=Pse7367_2695 {ECO:0000313|EMBL:AFY70950.1};
OS Pseudanabaena sp. PCC 7367.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY70950.1, ECO:0000313|Proteomes:UP000010386};
RN [1] {ECO:0000313|EMBL:AFY70950.1, ECO:0000313|Proteomes:UP000010386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY70950.1,
RC ECO:0000313|Proteomes:UP000010386};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Pseudanabaena sp. PCC 7367.";
RL Submitted (MAY-2012) 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; CP003592; AFY70950.1; -; Genomic_DNA.
DR RefSeq; WP_015165906.1; NC_019701.1.
DR AlphaFoldDB; K9SLD9; -.
DR STRING; 82654.Pse7367_2695; -.
DR KEGG; pseu:Pse7367_2695; -.
DR PATRIC; fig|82654.3.peg.3148; -.
DR eggNOG; COG1232; Bacteria.
DR eggNOG; COG3349; Bacteria.
DR HOGENOM; CLU_022687_1_0_3; -.
DR OrthoDB; 438203at2; -.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000010386; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000010386}.
FT DOMAIN 10..451
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 457..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 54053 MW; F5A719A539E54DFC CRC64;
MRVAIAGAGL AGLSCAKYLA DCGHTPIVIE RENVLGGKVA AWQDEEGDWY ETGLHVFFGA
YPNMLQLLGE LGISDRLQWK KHAMLFNMPG QGGKLSKFDF PDGLPAPLNG IVAILSNNDM
LTWEEKIKFG IGLLPAIIKG QTYVEEMDKY SFAEWLQHQG VPERVEKEVF IAMAKALNFI
NPDQISATVV LTALNRFLQE KEGSKMAFLD GAPPERLCQP IVDYFTAKGG EVRMQTALRK
IELNADGTVK HFLVGRPGED SYALEADVYV SALPVDPLKL MLPEAWQQQA YFQQLDGLEG
VPVINLHLWF DRKLTDIDNV LFSRSPILSV YADMSNTCKE YADPDRSMLE LVLAPAAEWI
SKSEQEIVDV AIAELAKIFP EQIPHKAKLI KSKVVKTPRS VYKATPGCQS HRPAQETPIA
NFFLTGDFTM QRYLASMEGA VLSGKLTAQT IDRQISLNRS AGNTSNPTDQ APSSSFSENI
GKTTAAKNPA
//
