ID   N8DT2_SOPFL             Reviewed;         407 AA.
AC   B1B5P4;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Naringenin 8-dimethylallyltransferase 2, chloroplastic;
DE            Short=SfN8DT-2;
DE            EC=2.5.1.70;
DE   Flags: Precursor;
GN   Name=N8DT-2;
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, AND COFACTOR.
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB370330; BAG12673.1; -; mRNA.
DR   AlphaFoldDB; B1B5P4; -.
DR   SMR; B1B5P4; -.
DR   BioCyc; MetaCyc:MON-16838; -.
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..407
FT                   /note="Naringenin 8-dimethylallyltransferase 2,
FT                   chloroplastic"
FT                   /id="PRO_0000418450"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        383..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   407 AA;  45747 MW;  4F2FA9036BC80351 CRC64;
     MGFVLPASFP GASSITTGGS CLRSKQYAKN YYASSYVTTL WHKKGKIQKE YCAVIFSRHN
     LKQHYKVNEG GSTSKECEKK YVVNAISEQS FEYEPQARDP KNIWGSVNDA LDTFYKFCRP
     YAIFSVVLGA TFKSLVAVER LSDLSLAFFI GWLQVVVAVI CIHIFDVGLN QLCDIEIDKI
     NKPDLPLASG NLSFRNVVII TASSLILGLG FAWIVGSWPL FWTVFICCMF AAAYNVDLPL
     LRWKKYPVLT AISFIANVAV TRSLGFFLHM QTCVFKRPTT FPRPLIFCTA IVSIYAIVIA
     LFKDIPDMEG DEKFGIQSLS LRLGPKRVFW ICVSLLEMAY GVTILVGATS PILWSKIITV
     LGHAILASVL WYHAKSTDLT SNVVLQSFYM FIWKLHTAEY CLIPLFR