PT1L_HUMLU
ID PT1L_HUMLU Reviewed; 414 AA.
AC A0A0B5A051;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=2-acylphloroglucinol 4-prenyltransferase {ECO:0000305};
DE EC=2.5.1.136 {ECO:0000269|PubMed:25564559, ECO:0000269|PubMed:29760092};
DE AltName: Full=Aromatic prenyltransferase PT1L {ECO:0000303|PubMed:25564559};
DE AltName: Full=Humulus lupulus prenyltransferase-1-like {ECO:0000303|PubMed:25564559};
DE Short=HlPT1L {ECO:0000303|PubMed:25564559};
DE Flags: Precursor;
GN Name=PT1L {ECO:0000303|PubMed:25564559};
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], FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH
RP PT2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-183;
RP ASP-187; ASP-310 AND ASP-313, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=cv. Nugget; TISSUE=Lupulin gland;
RX PubMed=25564559; DOI=10.1104/pp.114.253682;
RA Li H., Ban Z., Qin H., Ma L., King A.J., Wang G.;
RT "A heteromeric membrane-bound prenyltransferase complex from hop catalyzes
RT three sequential aromatic prenylations in the bitter Acid pathway.";
RL Plant Physiol. 167:650-659(2015).
RN [2]
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, INTERACTION WITH CHIL2,
RP AND ACTIVITY REGULATION.
RX PubMed=29760092; DOI=10.1073/pnas.1802223115;
RA Ban Z., Qin H., Mitchell A.J., Liu B., Zhang F., Weng J.-K., Dixon R.A.,
RA Wang G.;
RT "Noncatalytic chalcone isomerase-fold proteins in Humulus lupulus are
RT auxiliary components in prenylated flavonoid biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E5223-E5232(2018).
RN [3]
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 (PubMed:25564559). Uses dimethylallyl
CC diphosphate (DMAPP) as the prenyl donor (PubMed:25564559).
CC {ECO:0000269|PubMed:25564559, ECO:0000305|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY: [2-acylphloroglucinol 4-prenyltransferase]:
CC Reaction=2',4,4',6'-tetrahydroxychalcone + dimethylallyl diphosphate =
CC desmethylxanthohumol + diphosphate; Xref=Rhea:RHEA:51876,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:77645,
CC ChEBI:CHEBI:134302; EC=2.5.1.136;
CC Evidence={ECO:0000269|PubMed:29760092};
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:25564559};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:E5RP65};
CC -!- ACTIVITY REGULATION: Stimulated by CHIL2 but inhibited by CHIL1.
CC {ECO:0000269|PubMed:29760092}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.74 uM for naringenin chalcone {ECO:0000269|PubMed:29760092};
CC KM=75.12 uM for dimethylallyl diphosphate
CC {ECO:0000269|PubMed:29760092};
CC KM=5.01 uM for naringenin chalcone (in the presence of CHIL2)
CC {ECO:0000269|PubMed:29760092};
CC KM=62.78 uM for dimethylallyl diphosphate (in the presence of CHIL2)
CC {ECO:0000269|PubMed:29760092};
CC KM=1.36 uM for phlorisovalerophenone {ECO:0000269|PubMed:25564559};
CC KM=5.1 uM for phlorisobutyrophenone {ECO:0000269|PubMed:25564559};
CC KM=43.52 uM for dimethylallyl diphosphate
CC {ECO:0000269|PubMed:25564559};
CC KM=5.7 uM for geranyl diphosphate {ECO:0000269|PubMed:25564559};
CC Vmax=0.1 umol/min/g enzyme with naringenin chalcone as substrate
CC {ECO:0000269|PubMed:29760092};
CC Vmax=0.13 umol/min/g enzyme with dimethylallyl diphosphate as
CC substrate {ECO:0000269|PubMed:29760092};
CC Vmax=0.12 umol/min/g enzyme with naringenin chalcone as substrate (in
CC the presence of CHIL2) {ECO:0000269|PubMed:29760092};
CC Vmax=0.23 umol/min/g enzyme with dimethylallyl diphosphate as
CC substrate (in the presence of CHIL2) {ECO:0000269|PubMed:29760092};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30468448}.
CC -!- SUBUNIT: Component an active demethylxanthohumol (DMX) biosynthetic
CC metabolon in glandular trichomes (lupulin glands) that encompasses a
CC chalcone synthase (CHS) and a membrane-bound prenyltransferase
CC (PubMed:29760092). Interacts with PT2, forming a functional metabolon
CC (PubMed:25564559). Interacts with CHIL2; this interaction promotes
CC catalytic activity (PubMed:29760092). {ECO:0000269|PubMed:25564559,
CC ECO:0000269|PubMed:29760092}.
CC -!- SUBCELLULAR LOCATION: Plastid {ECO:0000269|PubMed:25564559}. Plastid,
CC chloroplast membrane {ECO:0000255}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in trichomes.
CC {ECO:0000269|PubMed:25564559}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; KM222441; AJD80254.1; -; mRNA.
DR AlphaFoldDB; A0A0B5A051; -.
DR KEGG; ag:AJD80254; -.
DR BioCyc; MetaCyc:MON-12001; -.
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..86
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 87..414
FT /note="2-acylphloroglucinol 4-prenyltransferase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439227"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 183
FT /note="D->A: Loss of catalytic activity; when associated
FT with A-187."
FT /evidence="ECO:0000269|PubMed:25564559"
FT MUTAGEN 187
FT /note="D->A: Loss of catalytic activity; when associated
FT with A-183."
FT /evidence="ECO:0000269|PubMed:25564559"
FT MUTAGEN 310
FT /note="D->A: Loss of catalytic activity; when associated
FT with A-313."
FT /evidence="ECO:0000269|PubMed:25564559"
FT MUTAGEN 313
FT /note="D->A: Loss of catalytic activity; when associated
FT with A-310."
FT /evidence="ECO:0000269|PubMed:25564559"
SQ SEQUENCE 414 AA; 45929 MW; B2B3D1050DBE19C9 CRC64;
MELSSVSSFS LGTNPFISIP HNNNNNLKVS SYCCKSKSRV INSTNSKHCS PNNNNNNNTS
NKTTHLLGLY GQSRCLLKPL SIFSCKDQRG NSIRASAQIE DRPPESGNLS ALTNVKDFVS
VCWEYVRPYT AKGVIICSSC LFGRELLENP NLFSWPLIFR ALLGMLAILG SCFYTAGINQ
IFDMDIDRIN KPDLPLVSGR ISVESAWLLT LSPAIIGFIL ILKLNSGPLL TSLYCLAILS
GTIYSVPPFR WKKNPITAFL CILMIHAGLN FSVYYASRAA LGLAFVWSPS FSFITAFITF
MTLTLASSKD LSDINGDRKF GVETFATKLG AKNITLLGTG LLLLNYVAAI STAIIWPKAF
KSNIMLLSHA ILAFSLFFQA RELDRTNYTP EACKSFYEFI WILFSAEYVV YLFI
