位置:首页 > 蛋白库 > PDS_CAPAN
PDS_CAPAN
ID   PDS_CAPAN               Reviewed;         582 AA.
AC   P80093;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=15-cis-phytoene desaturase, chloroplastic/chromoplastic {ECO:0000305};
DE            EC=1.3.5.5 {ECO:0000269|PubMed:1396714, ECO:0000269|PubMed:15503129};
DE   AltName: Full=Phytoene dehydrogenase {ECO:0000305};
DE   AltName: Full=Phytoene desaturase {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PDS;
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Lamuyo;
RX   PubMed=1396714; DOI=10.1111/j.1432-1033.1992.tb17302.x;
RA   Hugueney P., Roemer S., Kuntz M., Camara B.;
RT   "Characterization and molecular cloning of a flavoprotein catalyzing the
RT   synthesis of phytofluene and zeta-carotene in Capsicum chromoplasts.";
RL   Eur. J. Biochem. 209:399-407(1992).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=15503129; DOI=10.1007/s00425-004-1395-2;
RA   Breitenbach J., Sandmann G.;
RT   "zeta-Carotene cis isomers as products and substrates in the plant poly-cis
RT   carotenoid biosynthetic pathway to lycopene.";
RL   Planta 220:785-793(2005).
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:0000269|PubMed:1396714, ECO:0000269|PubMed:15503129}.
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:0000269|PubMed:1396714, ECO:0000269|PubMed:15503129};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:1396714};
CC   -!- ACTIVITY REGULATION: Inhibited by the herbicides metflurazon, difunone,
CC       fluridone and diflufenican.
CC   -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:A2XDA1}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, chromoplast
CC       {ECO:0000269|PubMed:1396714}. Membrane {ECO:0000269|PubMed:1396714};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:A2XDA1}.
CC   -!- DEVELOPMENTAL STAGE: Ripening fruit. {ECO:0000269|PubMed:1396714}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000305}.
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; X68058; CAA48195.1; -; mRNA.
DR   PIR; S29314; S29314.
DR   RefSeq; NP_001311742.1; NM_001324813.1.
DR   AlphaFoldDB; P80093; -.
DR   SMR; P80093; -.
DR   GeneID; 107861625; -.
DR   KEGG; cann:107861625; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000189700; Genome assembly.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0009509; C:chromoplast; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016166; F:phytoene dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0016120; P:carotene biosynthetic process; IDA:UniProtKB.
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; IPR014102; Phytoene_desaturase.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02731; phytoene_desat; 1.
PE   1: Evidence at protein level;
KW   Carotenoid biosynthesis; Chloroplast; Chromoplast; Herbicide resistance;
KW   Membrane; Oxidoreductase; Plastid; Transit peptide.
FT   TRANSIT         1..110
FT                   /note="Chloroplast and chromoplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           111..582
FT                   /note="15-cis-phytoene desaturase,
FT                   chloroplastic/chromoplastic"
FT                   /id="PRO_0000006323"
FT   BINDING         140..141
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         148
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         165..166
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         171
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         348
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         537
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         545
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT   BINDING         547
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A2XDA1"
SQ   SEQUENCE   582 AA;  65062 MW;  011E6E7DCAFB3DB5 CRC64;
     MPQIGLVSAV NLRVQGNSAY LWSSRSSLGT DSQDGCSQRN SLCFGGSDSM SHRLKIRNPH
     SITRRLAKDF RPLKVVCIDY PRPELDNTVN YLEAAFLSSS FRSSPRPTKP LEIVIAGAGL
     GGLSTAKYLA DAGHKPILLE ARDVLGGKVA AWKDDDGDWY ETGLHIFFGA YPNMQNLFGE
     LGINDRLQWK EHSMIFAMPN KPGEFSRFDF PEALPAPLNG ILAILKNNEM LTWPEKVKFA
     IGLLPAMLGG QSYVEAQDGI SVKDWMRKQG VPDRVTDEVF IAMSKALNFI NPDELSMQCI
     LIALNRFLQE KHGSKMAFLD GNPPERLCMP IVEHIESKGG QVRLNSRIKK IELNEDGSVK
     CFILNDGSTI EGDAFVFATP VDIFKLLLPE DWKEIPYFQK LEKLVGVPVI NVHIWFDRKL
     KNTSDNLLFS RSPLLSVYAD MSVTCKEYYD PNKSMLELVF APAEEWVSRS DSEIIDATMK
     ELAKLFPDEI SADQSKAKIL KYHVVKTPRS VYKTVPGCEP CRLLQRSPVE GFYLAGDYTK
     QKYLASMEGA VLSGKLCAQA IVQDYELLVG RSQRKLAETS VV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024