CRTI_SYNY3
ID CRTI_SYNY3 Reviewed; 472 AA.
AC P29273;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phytoene dehydrogenase;
DE EC=1.3.99.-;
DE AltName: Full=Phytoene desaturase;
GN Name=pds; Synonyms=crtD; OrderedLocusNames=slr1254;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1581575; DOI=10.1007/bf00019213;
RA Martinez-Ferez I.M., Vioque A.;
RT "Nucleotide sequence of the phytoene desaturase gene from Synechocystis sp.
RT PCC 6803 and characterization of a new mutation which confers resistance to
RT the herbicide norflurazon.";
RL Plant Mol. Biol. 18:981-983(1992).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Vioque A.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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 -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000305};
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000305};
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by the herbicide norflurazon in a non-
CC competitive way.
CC -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; X62574; CAA44452.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17847.1; -; Genomic_DNA.
DR PIR; S74886; S74886.
DR AlphaFoldDB; P29273; -.
DR SMR; P29273; -.
DR IntAct; P29273; 3.
DR STRING; 1148.1652929; -.
DR PaxDb; P29273; -.
DR EnsemblBacteria; BAA17847; BAA17847; BAA17847.
DR KEGG; syn:slr1254; -.
DR eggNOG; COG0654; Bacteria.
DR eggNOG; COG3349; Bacteria.
DR InParanoid; P29273; -.
DR OMA; HSMIFNQ; -.
DR PhylomeDB; P29273; -.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016166; F:phytoene dehydrogenase activity; IEA:InterPro.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR InterPro; IPR014102; Phytoene_desaturase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02731; phytoene_desat; 1.
PE 3: Inferred from homology;
KW Carotenoid biosynthesis; Cell membrane; FAD; Flavoprotein;
KW Herbicide resistance; Membrane; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..472
FT /note="Phytoene dehydrogenase"
FT /id="PRO_0000067698"
FT BINDING 7..23
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT VARIANT 195
FT /note="R -> C (confers resistance to the herbicide
FT norflurazon)"
SQ SEQUENCE 472 AA; 52921 MW; 81D089A6DAA28758 CRC64;
MRVVIAGAGL AGLACAKYLA DAGFTPVVLE RRDVLGGKIA AWKDEDGDWY ETGLHIFFGA
YPNMLQLFKE LDIEDRLQWK EHSMIFNQPE KPGTYSRFDF PDIPAPINGL VAILRNNDML
TWPEKIRFGL GLLPAIVQGQ SYVEEMDKYT WSEWMAKQNI PPRIEKEVFI AMSKALNFID
PDEISATILL TALNRFLQEK NGSKMAFLDG APPERLCQPL VDYITERGGE VHINKPLKEI
LLNEDGSVKG YLIRGLDGAP DEVITADLYV SAMPVDPLKT MVPAPWREYP EFKQIQGLEG
VPVINLHLWF DRKLTDIDHL LFSRSPLLSV YADMSNTCRE YSDPDKSMLE LVLAPAQDWI
GKSDEEIVAA TMAEIKQLFP QHFNGDNPAR LLKSHVVKTP RSVYKATPGR QACRPDQRTS
VPNFYLAGDF TMQKYLGSME GAVLSGKQCA QAIAADFNPQ TVPPTREIVT VG