PT1_HUMLU
ID PT1_HUMLU Reviewed; 411 AA.
AC E5RP65;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=2-acylphloroglucinol 4-prenyltransferase, chloroplastic {ECO:0000305};
DE EC=2.5.1.136 {ECO:0000269|PubMed:22166201};
DE AltName: Full=Aromatic prenyltransferase PT1 {ECO:0000303|Ref.1};
DE AltName: Full=Humulus lupulus prenyltransferase-1 {ECO:0000303|Ref.1};
DE Short=HlPT-1 {ECO:0000303|Ref.1};
DE Flags: Precursor;
OS Humulus lupulus (European hop).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Humulus.
OX NCBI_TaxID=3486;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Kirin II; TISSUE=Lupulin gland;
RX DOI=10.5511/plantbiotechnology.27.199;
RA Tsurumaru Y., Sasaki K., Miyawaki T., Momma T., Umemoto N., Yazaki K.;
RT "An aromatic prenyltransferase-like gene HlPT-1 preferentially expressed in
RT lupulin glands of hop.";
RL Plant Biotechnol. (Sheffield) 27:199-204(2010).
RN [2]
RP FUNCTION.
RA Page J., Liu E., Nagel J.;
RT "Aromatic prenyltransferase from hop.";
RL Patent number WO2009114939, 24-SEP-2009.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND PATHWAY.
RX PubMed=22166201; DOI=10.1016/j.bbrc.2011.11.125;
RA Tsurumaru Y., Sasaki K., Miyawaki T., Uto Y., Momma T., Umemoto N.,
RA Momose M., Yazaki K.;
RT "HlPT-1, a membrane-bound prenyltransferase responsible for the
RT biosynthesis of bitter acids in hops.";
RL Biochem. Biophys. Res. Commun. 417:393-398(2012).
RN [4]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Involved in the biosynthesis of prenylated phenolics natural
CC products which contribute to the bitter taste of beer and display broad
CC biological activities (Probable). Catalyzes the first prenylation step
CC in the beta-bitter acid pathway (Ref.2, PubMed:22166201). Abble to
CC transfer dimethylallyl diphosphate (DMAPP) or geranyl diphosphate (GPP)
CC to phlorisovalerophenone (PIVP), phlorisobutrylphenone (PIMP) and
CC naringenin chalcone (Ref.2). Can also use phlorisobutyrophenone (PIBP)
CC and phlormethylbutanophenone (PMBP) as substrates, but not 6'-O-
CC methylated chalcone or naringenin (PubMed:22166201).
CC {ECO:0000269|PubMed:22166201, ECO:0000269|Ref.2,
CC ECO:0000305|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acylphloroglucinol + dimethylallyl diphosphate = a 2-acyl-
CC 4-prenylphloroglucinol + diphosphate; Xref=Rhea:RHEA:51752,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:134371,
CC ChEBI:CHEBI:134386; EC=2.5.1.136;
CC Evidence={ECO:0000269|PubMed:22166201};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22166201};
CC Note=Cannot be substituted by Mn(2+) or Zn(2+).;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=59.5 uM for phlorisovalerophenone {ECO:0000269|PubMed:22166201};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:22166201};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30468448}.
CC -!- SUBCELLULAR LOCATION: Plastid {ECO:0000269|Ref.1}. Plastid, chloroplast
CC membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in glandular trichomes called lupulin
CC glands, and in early stage and mature cones. Detected in leaves, but
CC not in root, stem and first stage of flowers. No expression in male
CC flowers. {ECO:0000269|Ref.1}.
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; AB543053; BAJ61049.1; -; mRNA.
DR AlphaFoldDB; E5RP65; -.
DR SMR; E5RP65; -.
DR KEGG; ag:BAJ61049; -.
DR BRENDA; 2.5.1.136; 2716.
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; IEA:InterPro.
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..91
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 92..411
FT /note="2-acylphloroglucinol 4-prenyltransferase,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439226"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 411 AA; 45481 MW; 4AC55DDAD6619464 CRC64;
MELSSVSSFS LGTNPFISIP HNNNNLKVSS YCCKSKSRVI NSTNSKHCSP NNNNNTSNKT
THLLGLYGQS RCLLKPLSFI SCNDQRGNSI RASAQIEDRP PESGNLSALT NVKDFVSVCW
EYVRPYTAKG VIICSSCLFG RELLENPNLF SRPLIFRALL GMLAILGSCF YTAGINQIFD
MDIDRINKPD LPLVSGRISV ESAWLLTLSP AIIGFILILK LNSGPLLTSL YCLAILSGTI
YSVPPFRWKK NPITAFLCIL MIHAGLNFSV YYASRAALGL AFAWSPSFSF ITAFITFMTL
TLASSKDLSD INGDRKFGVE TFATKLGAKN ITLLGTGLLL LNYVAAISTA IIWPKAFKSN
IMLLSHAILA FSLIFQAREL DRTNYTPEAC KSFYEFIWIL FSAEYVVYLF I
