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}.
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; 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