ID   U6DT_PETCR              Reviewed;         400 AA.
AC   W0SKS3;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Umbelliferone 6-dimethylallyltransferase, chloroplastic {ECO:0000303|PubMed:24354545};
DE            EC=2.5.1.139 {ECO:0000269|PubMed:24354545};
DE   Flags: Precursor;
GN   Name=PcPT {ECO:0000303|PubMed:24354545};
OS   Petroselinum crispum (Parsley) (Petroselinum hortense).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Petroselinum.
OX   NCBI_TaxID=4043 {ECO:0000312|EMBL:BAO31627.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION
RP   BY UV, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX   PubMed=24354545; DOI=10.1111/tpj.12409;
RA   Karamat F., Olry A., Munakata R., Koeduka T., Sugiyama A., Paris C.,
RA   Hehn A., Bourgaud F., Yazaki K.;
RT   "A coumarin-specific prenyltransferase catalyzes the crucial biosynthetic
RT   reaction for furanocoumarin formation in parsley.";
RL   Plant J. 77:627-638(2014).
CC   -!- FUNCTION: Prenylates umbelliferone in the presence of dimethylallyl
CC       diphosphate (DMAPP) at the 6 position to yield demethylsuberosin (DMS)
CC       as the main product, together with a minor amount of osthenol
CC       corresponding to 8-prenylated umbelliferone. No activity with other
CC       coumarine derivatives such as psoralen, bergapten and xanthotoxin, or
CC       with geranyl diphosphate or farnesyl diphosphate as prenyl donors.
CC       {ECO:0000269|PubMed:24354545}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl diphosphate + umbelliferone = demethylsuberosin
CC         + diphosphate; Xref=Rhea:RHEA:51868, ChEBI:CHEBI:27510,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:69042;
CC         EC=2.5.1.139; Evidence={ECO:0000269|PubMed:24354545};
CC   -!- ACTIVITY REGULATION: Inhibited by psoralen, a major downstream product.
CC       {ECO:0000269|PubMed:24354545}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=21 uM for umbelliferone in the reaction producing
CC         demethylsuberosin {ECO:0000269|PubMed:24354545};
CC         KM=79 uM for dimethylallyl diphosphate in the reaction producing
CC         demethylsuberosin {ECO:0000269|PubMed:24354545};
CC         KM=25 uM for umbelliferone in the reaction producing osthenol
CC         {ECO:0000269|PubMed:24354545};
CC         KM=45 uM for dimethylallyl diphosphate in the reaction producing
CC         osthenol {ECO:0000269|PubMed:24354545};
CC       pH dependence:
CC         Optimum pH is 8.2. {ECO:0000269|PubMed:24354545};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000269|PubMed:24354545}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems.
CC       {ECO:0000269|PubMed:24354545}.
CC   -!- INDUCTION: Up-regulated upon UV-B irradiation.
CC       {ECO:0000269|PubMed:24354545}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB825956; BAO31627.1; -; mRNA.
DR   AlphaFoldDB; W0SKS3; -.
DR   SMR; W0SKS3; -.
DR   KEGG; ag:BAO31627; -.
DR   BRENDA; 2.5.1.139; 4694.
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   GO; GO:0071493; P:cellular response to UV-B; 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..48
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..400
FT                   /note="Umbelliferone 6-dimethylallyltransferase,
FT                   chloroplastic"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000440667"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   400 AA;  44221 MW;  39EF2CFFD531FFB2 CRC64;
     MSQTLMHSRF SSGFLHHQPE KGFLTLQTQR RHAKTLKGEK EFPSRVVSCH KNVDSSKNFS
     SSCEKSKTQE KILAQTLGAT SDGEAIVQPN NDFEVTWQNT LRRKWDAFSI FSRPYSAICT
     IIGISSVSLL PLTSVADFSP AYFVGLLQAL IPFLCANIYT SAINQLVDVD IDKINKPYLP
     LVSGEFSMGE GRAIVSALTF TCFAMAIMSH SVPLFVGVLV YFLIGTAYSV EHPLLRWKTK
     PAMAAFSMAG LMGLTIQPTV FYHIQNVLGK PMVFSRSVAF ATMFFSIFAA CLGAIKDIPD
     VEGDREFGNL TFSVRYGQEK VFSFCLNVLL LAYGSAVVVG ASSSSLLCKT VSVIGHTVLA
     SLLVLRAKST NPKDPESTQS FYMFLFKLLY AEYVLIHFMR