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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//