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N8DT1_SOPFL
ID   N8DT1_SOPFL             Reviewed;         410 AA.
AC   B1B3P3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Naringenin 8-dimethylallyltransferase 1, chloroplastic;
DE            Short=SfN8DT-1;
DE            EC=2.5.1.70;
DE   Flags: Precursor;
GN   Name=N8DT-1;
OS   Sophora flavescens (Ku shen).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Sophoreae; Sophora.
OX   NCBI_TaxID=49840;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP   INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=18218974; DOI=10.1104/pp.107.110544;
RA   Sasaki K., Mito K., Ohara K., Yamamoto H., Yazaki K.;
RT   "Cloning and Characterization of Naringenin 8-Prenyltransferase, a
RT   Flavonoid-Specific Prenyltransferase of Sophora flavescens.";
RL   Plant Physiol. 146:1075-1084(2008).
CC   -!- FUNCTION: Involved in the biosynthesis of sophoraflavanone G (SFG). Can
CC       use flavanones (naringenin, liquiritigenin and hesperetin) as
CC       substrates, but not flavonols or isoflavones. Shows a strict
CC       specificity for dimethylallyl diphosphate.
CC       {ECO:0000269|PubMed:18218974}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-naringenin + dimethylallyl diphosphate = diphosphate +
CC         sophoraflavanone B; Xref=Rhea:RHEA:15433, ChEBI:CHEBI:17846,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:50207, ChEBI:CHEBI:57623; EC=2.5.1.70;
CC         Evidence={ECO:0000269|PubMed:18218974};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:18218974};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:18218974};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=106 uM for dimethylallyl diphosphate
CC         {ECO:0000269|PubMed:18218974};
CC         KM=55 uM for naringenin {ECO:0000269|PubMed:18218974};
CC       Temperature dependence:
CC         Optimum temperature is 75 degrees Celsius.
CC         {ECO:0000269|PubMed:18218974};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000269|PubMed:18218974}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:18218974}.
CC   -!- TISSUE SPECIFICITY: Secifically expressed in root bark. Not detected in
CC       aerial tissues. {ECO:0000269|PubMed:18218974}.
CC   -!- INDUCTION: Up-regulated by elicitor, methyl jasmonate and salicylic
CC       acid. {ECO:0000269|PubMed:18218974}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB325579; BAG12671.1; -; mRNA.
DR   AlphaFoldDB; B1B3P3; -.
DR   SMR; B1B3P3; -.
DR   BioCyc; MetaCyc:MON-16837; -.
DR   BRENDA; 2.5.1.70; 8929.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
DR   CDD; cd13960; PT_UbiA_HPT1; 1.
DR   Gene3D; 1.10.357.140; -; 1.
DR   InterPro; IPR044502; AtHST-like.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR044878; UbiA_sf.
DR   Pfam; PF01040; UbiA; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Membrane; Plastid; Transferase; Transit peptide;
KW   Transmembrane; Transmembrane helix.
FT   TRANSIT         1..23
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..410
FT                   /note="Naringenin 8-dimethylallyltransferase 1,
FT                   chloroplastic"
FT                   /id="PRO_0000418449"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   410 AA;  46159 MW;  6DEBE3912BC82090 CRC64;
     MGSMLLASFP GASSITTGGS CLRSKQYAKN YDASSYVTTS WYKKRKIQKE HCAAIFSKHN
     LKQHYKVNEG GSTSNTSKEC EKKYVVNAIS EQSFEYEPQT RDPESIWDSV NDALDIFYKF
     CRPYAMFTIV LGATFKSLVA VEKLSDLSLA FFIGWLQVVV AVICIHIFGV GLNQLCDIEI
     DKINKPDLPL ASGKLSFRNV VIITASSLIL GLGFAWIVDS WPLFWTVFIS CMVASAYNVD
     LPLLRWKKYP VLTAINFIAD VAVTRSLGFF LHMQTCVFKR PTTFPRPLIF CTAIVSIYAI
     VIALFKDIPD MEGDEKFGIQ SLSLRLGPKR VFWICVSLLE MTYGVTILVG ATSPILWSKI
     ITVLGHAVLA SVLWYHAKSV DLTSNVVLHS FYMFIWKLHT AEYFLIPLFR
 
 
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