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Database: UniProt
Entry: K9PKU1_9CYAN
LinkDB: K9PKU1_9CYAN
Original site: K9PKU1_9CYAN 
ID   K9PKU1_9CYAN            Unreviewed;       479 AA.
AC   K9PKU1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Phytoene dehydrogenase {ECO:0000256|RuleBase:RU368016};
DE            EC=1.3.5.5 {ECO:0000256|RuleBase:RU368016};
GN   ORFNames=Cal7507_3633 {ECO:0000313|EMBL:AFY34025.1};
OS   Calothrix sp. PCC 7507.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY34025.1, ECO:0000313|Proteomes:UP000010390};
RN   [1] {ECO:0000313|EMBL:AFY34025.1, ECO:0000313|Proteomes:UP000010390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY34025.1,
RC   ECO:0000313|Proteomes:UP000010390};
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., Teshima H., Chen A.,
RA   Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA   Woyke T., Kerfeld C.;
RT   "Finished genome of Calothrix sp. PCC 7507.";
RL   Submitted (APR-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; CP003943; AFY34025.1; -; Genomic_DNA.
DR   RefSeq; WP_015129832.1; NC_019682.1.
DR   AlphaFoldDB; K9PKU1; -.
DR   STRING; 99598.Cal7507_3633; -.
DR   KEGG; calo:Cal7507_3633; -.
DR   PATRIC; fig|99598.3.peg.4118; -.
DR   eggNOG; COG0493; Bacteria.
DR   eggNOG; COG3349; Bacteria.
DR   HOGENOM; CLU_022687_1_0_3; -.
DR   OrthoDB; 438203at2; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000010390; 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:UP000010390}.
FT   DOMAIN          10..453
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   479 AA;  53461 MW;  E7030BD082E0ECAA CRC64;
     MRVAIAGAGL AGLSCAKYLT DAGHTPIVLE RRDVLGGKVA AWQDSDGDWY ETGLHIFFGA
     YPNMLQLFKE LDIEDRLQWK EHSMIFNQPD DPGTYSRFDF PDLPAPLNGV IAILRNNDML
     TWPEKIKFGL GLIPAMIQGQ KYVEEMDKYS WTEWLRKQNI PERVNDEVFI AMCKSLNFIG
     PDEISATILL TALNRFLQEK KGSTMAFLDG PPTERLCQPI VDHITAGGGE VRLNAPLKEI
     LLNPDGTVKG FLLRGLDGAE DEVFTADLYV SAMPVDPLKV ILPKPWQQME FFQKLEGLEG
     VPVINLHLWF DRKLTEIDHL LFSRSPLLSV YADMSNTCRG YANPDRSMLE LVLAPAKDWI
     AKSDEEIVAA TIAELEKLFP NHFGVDNPAK LLKYHVVKTP RSVYKATPGR QQHRPSQVTP
     ISNFYLTGDF TMQRYLASME GAVLSGKLTA QAIREALPVA NASNLQTLSR SPATNAATA
//
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