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Database: UniProt
Entry: A0A2Z5T7S6_9CYAN
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Original site: A0A2Z5T7S6_9CYAN 
ID   A0A2Z5T7S6_9CYAN        Unreviewed;       464 AA.
AC   A0A2Z5T7S6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE            EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
GN   ORFNames=RGRSB_0674 {ECO:0000313|EMBL:BBA79224.1};
OS   cyanobacterium endosymbiont of Rhopalodia gibberula.
OC   Bacteria; Cyanobacteriota.
OX   NCBI_TaxID=1763363 {ECO:0000313|EMBL:BBA79224.1, ECO:0000313|Proteomes:UP000264686};
RN   [1] {ECO:0000313|EMBL:BBA79224.1, ECO:0000313|Proteomes:UP000264686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RgSB {ECO:0000313|EMBL:BBA79224.1};
RX   PubMed=29026213; DOI=10.1038/s41598-017-13578-8;
RA   Nakayama T., Inagaki Y.;
RT   "Genomic divergence within non-photosynthetic cyanobacterial endosymbionts
RT   in rhopalodiacean diatoms.";
RL   Sci. Rep. 7:13075-13075(2017).
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; AP018341; BBA79224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z5T7S6; -.
DR   KEGG; cer:RGRSB_0674; -.
DR   OrthoDB; 438203at2; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000264686; 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:UP000264686}.
FT   DOMAIN          10..454
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   464 AA;  52621 MW;  26639EA29AC1DF1F CRC64;
     MRVAIAGAGL AGLSCGKYLV DAGHTPIILE RRDVLGGKVA AWKDDDGDWY ETGLHIFFGA
     YPNMLQLFKE LGIEERLQWK EHSMIFNQPE KPGTYSRFDF PNIPAPFNGI IAILCNDDML
     TWEEKVKFGL GLIPAIIHGQ NYVEKMDRYS WSEWIRRQNI PPRVEKEIFI AMSKALNFIN
     PNEISATVLL TALNRFLQEK NGSKMAFLDG PPTERLCKPI IDYITERGGE VRLNTPLKEI
     ILDEDNTVKG FLLRGLNGEP DEMFKAHLYL SAIPVDLLKL LLPKPWKTLN FARQLEGLEG
     VPVINLHLWF DRKLTDVDHL LFSRSDLLSV YADMSNTCKE YVNQDRSMLE LVLAPAKDWI
     SQSDEDIIAA TMEELCKLFP QHFTGENPTK LLKFHVVKTP RSVYKATPGR QAFRPSQKTP
     IANFYLAGDY TMQQYLGSME GAVLSGKLAA QAIIRDYPTN IVVP
//
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