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PDS_ORYSJ
ID   PDS_ORYSJ               Reviewed;         578 AA.
AC   Q0DUI8; A0A0P0VTZ9; Q10QT5; Q93Y74; Q9ZTN9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=15-cis-phytoene desaturase, chloroplastic/chromoplastic {ECO:0000305};
DE            EC=1.3.5.5 {ECO:0000250|UniProtKB:A2XDA1};
DE   AltName: Full=Phytoene dehydrogenase {ECO:0000305};
DE   AltName: Full=Phytoene desaturase {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PDS; Synonyms=PDS1; OrderedLocusNames=Os03g0184000, LOC_Os03g08570;
GN   ORFNames=OSJNBa0032G08.5;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
CC   -!- FUNCTION: Converts phytoene into zeta-carotene via the intermediary of
CC       phytofluene by the symmetrical introduction of two double bonds at the
CC       C-11 and C-11' positions of phytoene with a concomitant isomerization
CC       of two neighboring double bonds at the C9 and C9' positions from trans
CC       to cis. {ECO:0000250|UniProtKB:A2XDA1}.
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:0000250|UniProtKB:A2XDA1};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:A2XDA1};
CC   -!- ACTIVITY REGULATION: Inhibited by the herbicide norflurazon (NFZ).
CC       {ECO:0000250|UniProtKB:A2XDA1}.
CC   -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC   -!- SUBUNIT: Homotetramer. Homotetramer is the active form of the enzyme.
CC       {ECO:0000250|UniProtKB:A2XDA1}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000250|UniProtKB:Q40406}. Plastid, chromoplast
CC       {ECO:0000250|UniProtKB:Q40406}. Membrane
CC       {ECO:0000250|UniProtKB:A2XDA1}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:A2XDA1}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF11100.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC079633; AAK92625.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF94340.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF11100.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP014959; BAS82656.1; -; Genomic_DNA.
DR   RefSeq; XP_015633101.1; XM_015777615.1.
DR   AlphaFoldDB; Q0DUI8; -.
DR   SMR; Q0DUI8; -.
DR   STRING; 4530.OS03T0184000-00; -.
DR   PaxDb; Q0DUI8; -.
DR   PRIDE; Q0DUI8; -.
DR   EnsemblPlants; Os03t0184000-00; Os03t0184000-00; Os03g0184000.
DR   GeneID; 4331854; -.
DR   Gramene; Os03t0184000-00; Os03t0184000-00; Os03g0184000.
DR   KEGG; osa:4331854; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   HOGENOM; CLU_022687_1_0_1; -.
DR   InParanoid; Q0DUI8; -.
DR   OMA; THCFFGA; -.
DR   OrthoDB; 1151887at2759; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   GO; GO:0009507; C:chloroplast; ISS:UniProtKB.
DR   GO; GO:0009509; C:chromoplast; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016166; F:phytoene dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0016120; P:carotene biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR014102; Phytoene_desaturase.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02731; phytoene_desat; 1.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis; Chloroplast; Chromoplast; FAD; Flavoprotein;
KW   Membrane; Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..87
FT                   /note="Chloroplast and chromoplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           88..578
FT                   /note="15-cis-phytoene desaturase,
FT                   chloroplastic/chromoplastic"
FT                   /id="PRO_0000006327"
FT   BINDING         115
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         134..135
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         142
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         159..160
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         165
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         342
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         531
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         539
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         541
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
SQ   SEQUENCE   578 AA;  64770 MW;  6561B0DE071282EF CRC64;
     MDTGCLSSMN ITGTSQARSF AGQLPTHRCF ASSSIQALKS SQHVSFGVKS LVLRNKGKRF
     RRRLGALQVV CQDFPRPPLE NTINFLEAGQ LSSFFRNSEQ PTKPLQVVIA GAGLAGLSTA
     KYLADAGHKP ILLEARDVLG GKIAAWKDED GDWYETGLHI FFGAYPNIQN LFGELGINDR
     LQWKEHSMIF AMPNKPGEFS RFDFPETLPA PLNGIWAILR NNEMLTWPEK VKFALGLLPA
     MVGGQAYVEA QDGFTVSEWM KKQGVPDRVN DEVFIAMSKA LNFINPDELS MQCILIALNR
     FLQEKHGSKM AFLDGNPPER LCMPIVDHVR SLGGEVRLNS RIQKIELNPD GTVKHFALTD
     GTQITGDAYV FATPVDILKL LVPQEWKEIS YFKKLEKLVG VPVINVHIWF DRKLKNTYDH
     LLFSRSSLLS VYADMSVTCK EYYDPNRSML ELVFAPAEEW VGRSDTEIIE ATMQELAKLF
     PDEIAADQSK AKILKYHVVK TPRSVYKTIP DCEPCRPLQR SPIEGFYLAG DYTKQKYLAS
     MEGAVLSGKL CAQSVVEDYK MLSRRSLKSL QSEVPVAS
 
 
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