PT2_HUMLU
ID PT2_HUMLU Reviewed; 408 AA.
AC A0A0B4ZTQ2;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=2-acyl-4-prenylphloroglucinol 6-prenyltransferase, chloroplastic {ECO:0000305};
DE EC=2.5.1.137 {ECO:0000269|PubMed:25564559};
DE AltName: Full=Aromatic prenyltransferase PT2 {ECO:0000303|PubMed:25564559};
DE AltName: Full=Humulus lupulus prenyltransferase-2 {ECO:0000303|PubMed:25564559};
DE Short=HlPT2 {ECO:0000303|PubMed:25564559};
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], FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH
RP PT1L, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-174;
RP ASP-178; ASP-302 AND ASP-305, 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 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 two last prenylation
CC steps in the beta-bitter acid pathway (PubMed:25564559). Uses
CC dimethylallyl diphosphate (DMAPP) as the prenyl donor
CC (PubMed:25564559). {ECO:0000269|PubMed:25564559,
CC ECO:0000305|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-4-prenylphloroglucinol + dimethylallyl diphosphate =
CC a 2-acyl-4,6-diprenylphloroglucinol + diphosphate;
CC Xref=Rhea:RHEA:51756, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623,
CC ChEBI:CHEBI:134346, ChEBI:CHEBI:134371; EC=2.5.1.137;
CC Evidence={ECO:0000269|PubMed:25564559};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-4,6-diprenylphloroglucinol + dimethylallyl
CC diphosphate = a 2-acyl-4,6,6-triprenylphloroglucinol + diphosphate;
CC Xref=Rhea:RHEA:51760, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623,
CC ChEBI:CHEBI:134346, ChEBI:CHEBI:134348; EC=2.5.1.137;
CC Evidence={ECO:0000269|PubMed:25564559};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:E5RP65};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30468448}.
CC -!- SUBUNIT: Homo- and heteromer. Interacts with PT1L, forming a functional
CC metabolon. {ECO:0000269|PubMed:25564559}.
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; KM222442; AJD80255.1; -; mRNA.
DR AlphaFoldDB; A0A0B4ZTQ2; -.
DR KEGG; ag:AJD80255; -.
DR BioCyc; MetaCyc:MON-12004; -.
DR BRENDA; 2.5.1.137; 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:UniProt.
DR Gene3D; 1.10.357.140; -; 1.
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..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..408
FT /note="2-acyl-4-prenylphloroglucinol 6-prenyltransferase,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439228"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 174
FT /note="D->A: Loss of catalytic activity; when associated
FT with A-178."
FT /evidence="ECO:0000269|PubMed:25564559"
FT MUTAGEN 178
FT /note="D->A: Loss of catalytic activity; when associated
FT with A-174."
FT /evidence="ECO:0000269|PubMed:25564559"
FT MUTAGEN 302
FT /note="D->A: Loss of catalytic activity; when associated
FT with A-305."
FT /evidence="ECO:0000269|PubMed:25564559"
FT MUTAGEN 305
FT /note="D->A: Loss of catalytic activity; when associated
FT with A-302."
FT /evidence="ECO:0000269|PubMed:25564559"
SQ SEQUENCE 408 AA; 46172 MW; A752262CE043831B CRC64;
MELSSACNLS LKPNYYYYPT SLFPSNNSYN NLKASSYYQT QRPIKCCSYS PSKYCSTKKL
QTTHLLGLYA KHKCLKPFSI GHLPRPNSLT AWSHQSEFPS TIVTKGSNFG HASWKFVRPI
PFVAVSIICT SLFGAELLKN PNLFSWQLMF DAFQGLVVIL LYHIYINGLN QIYDLESDRI
NKPDLPLAAE EMSVKSAWFL TIFSAVASLL LMIKLKCGLF LTCMYCCYLV IGAMYSVPPF
RWKMNTFTST LWNFSEIGIG INFLINYASR ATLGLPFQWR PPFTFIIGFV STLSIILSIL
KDVPDVEGDK KVGMSTLPVI FGARTIVLVG SGFFLLNYVA AIGVAIMWPQ AFKGYIMIPA
HAIFASALIF KTWLLDKANY AKEASDSYYH FLWFLMIAEY ILYPFIST
