VPS_HUMLU
ID VPS_HUMLU Reviewed; 394 AA.
AC O80400; B3GEA6; B3GEA7; B3GEA8; B3GEA9; B3GEB0; B3GEB1; B3GEB2; B3GEB3;
AC B3GEB4; B3GEB5; B3GEB6; B9VI88;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Phloroisovalerophenone synthase {ECO:0000305|PubMed:10336650};
DE Short=3-methyl-1-(trihydroxyphenyl)butan-1-one synthase {ECO:0000305|PubMed:10336650};
DE Short=Valerophenone synthase {ECO:0000303|PubMed:11272819};
DE EC=2.3.1.156 {ECO:0000269|PubMed:10336650, ECO:0000269|PubMed:11272819, ECO:0000269|PubMed:15170123};
DE AltName: Full=Naringenin-chalcone synthase {ECO:0000303|PubMed:15170123};
DE Short=2',4,4',6'-tetrahydroxychalcone synthase {ECO:0000305|PubMed:15170123};
DE EC=2.3.1.74 {ECO:0000269|PubMed:15170123};
DE AltName: Full=Phlorisobutyrophenone synthase {ECO:0000305|PubMed:10336650};
DE Short=2-methyl-1-(2,4,6-trihydroxyphenyl)propan-1-one synthase {ECO:0000305|PubMed:10336650};
DE EC=2.3.1.156 {ECO:0000269|PubMed:10336650};
GN Name=VPS {ECO:0000303|PubMed:11272819};
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND PATHWAY.
RC STRAIN=cv. 9418R; TISSUE=Lupulin gland;
RX PubMed=11272819; DOI=10.1271/bbb.65.150;
RA Okada Y., Ito K.;
RT "Cloning and analysis of valerophenone synthase gene expressed specifically
RT in lupulin gland of hop (Humulus lupulus L.).";
RL Biosci. Biotechnol. Biochem. 65:150-155(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. 9418R;
RA Yukio O., Kazutoshi I.;
RT "gDNA of valerophenone synthase of Humulus lupulus.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLU-232 AND LEU-385.
RC STRAIN=cv. Osvals's 72; TISSUE=Lupulin gland;
RA Skopek J., Matousek J.;
RT "In vitro utilization of malonyl-3'-dephospho-CoA as an extender substrate
RT by plant type III polyketide synthases.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-394, VARIANT GLU-232, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Cascade, cv. Cluster, cv. Eastern Gold, cv. Ember, cv. Golding,
RC cv. Hallertau, cv. J78, cv. Nugget, cv. Opal, cv. Saaz X, cv. Symphony, and
RC cv. Victoria;
RX PubMed=18519445; DOI=10.1093/aob/mcn089;
RA Castro C.B., Whittock L.D., Whittock S.P., Leggett G., Koutoulis A.;
RT "DNA sequence and expression variation of hop (Humulus lupulus)
RT valerophenone synthase (VPS), a key gene in bitter acid biosynthesis.";
RL Ann. Bot. 102:265-273(2008).
RN [5]
RP PROTEIN SEQUENCE OF 285-319 AND 362-391, FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Cone, and Lupulin gland;
RX PubMed=10336650; DOI=10.1046/j.1432-1327.1999.00444.x;
RA Paniego N.B., Zuurbier K.W.M., Fung S.-Y., van der Heijden R.,
RA Scheffer J.J.C., Verpoorte R.;
RT "Phlorisovalerophenone synthase, a novel polyketide synthase from hop
RT (Humulus lupulus L.) cones.";
RL Eur. J. Biochem. 262:612-616(1999).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15170123; DOI=10.1271/bbb.68.1142;
RA Okada Y., Sano Y., Kaneko T., Abe I., Noguchi H., Ito K.;
RT "Enzymatic reactions by five chalcone synthase homologs from hop (Humulus
RT lupulus L.).";
RL Biosci. Biotechnol. Biochem. 68:1142-1145(2004).
RN [7]
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). Polyketide synthase that can use 3-
CC methylbutanoyl-CoA (isovaleryl-CoA) and 2-methylpropanoyl-CoA
CC (isobutyryl-CoA) as substrates to produce phlorisovalerophenone (PIVP)
CC and phlorisobutyrophenone (2-methyl-1-(2,4,6-trihydroxyphenyl)propan-1-
CC one), respectively, intermediates in the biosynthesis of the bitter
CC acids (alpha and beta) acids (PubMed:11272819, PubMed:10336650,
CC PubMed:15170123). Can also produce naringenin-chalcone (2',4,4',6'-
CC tetrahydroxychalcone) from 4-coumaroyl-CoA with a lower efficiency
CC (PubMed:15170123). {ECO:0000269|PubMed:10336650,
CC ECO:0000269|PubMed:11272819, ECO:0000269|PubMed:15170123,
CC ECO:0000305|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbutanoyl-CoA + 3 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA
CC + phlorisovalerophenone; Xref=Rhea:RHEA:23572, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15951, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57345, ChEBI:CHEBI:57384; EC=2.3.1.156;
CC Evidence={ECO:0000269|PubMed:10336650, ECO:0000269|PubMed:11272819,
CC ECO:0000269|PubMed:15170123};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23573;
CC Evidence={ECO:0000269|PubMed:10336650, ECO:0000269|PubMed:11272819,
CC ECO:0000269|PubMed:15170123};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-
CC tetrahydroxychalcone + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:11128,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57355, ChEBI:CHEBI:57384, ChEBI:CHEBI:77645; EC=2.3.1.74;
CC Evidence={ECO:0000269|PubMed:15170123};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11129;
CC Evidence={ECO:0000269|PubMed:15170123};
CC -!- CATALYTIC ACTIVITY: [Phloroisovalerophenone synthase]:
CC Reaction=2-methylpropanoyl-CoA + 3 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA
CC + phlorisobutanophenone; Xref=Rhea:RHEA:67000, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:133419; EC=2.3.1.156;
CC Evidence={ECO:0000269|PubMed:15170123};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67001;
CC Evidence={ECO:0000269|PubMed:15170123};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 uM for 3-methylbutanoyl-CoA {ECO:0000269|PubMed:10336650};
CC KM=10 uM for 2-methylpropanoyl-CoA {ECO:0000269|PubMed:10336650};
CC KM=33 uM for malonyl-CoA {ECO:0000269|PubMed:10336650};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:10336650};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30468448}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10336650}.
CC -!- TISSUE SPECIFICITY: Expressed in lupulin gland (PubMed:11272819,
CC PubMed:10336650). Present at low levels in leaves but accumulates in
CC cones (PubMed:18519445). {ECO:0000269|PubMed:10336650,
CC ECO:0000269|PubMed:11272819, ECO:0000269|PubMed:18519445}.
CC -!- DEVELOPMENTAL STAGE: Accumulates early in cone development and stays at
CC high levels throughout cone formation. {ECO:0000269|PubMed:18519445}.
CC -!- MISCELLANEOUS: Expression level is directly related with bitter (alpha)
CC acids content, thus influencing the bitter taste of beer, cv. Symphony
CC and cv. Ember having highest levels. {ECO:0000269|PubMed:18519445}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AB015430; BAA29039.1; -; mRNA.
DR EMBL; AB047593; BAB12102.1; -; Genomic_DNA.
DR EMBL; FJ554588; ACM17227.1; -; mRNA.
DR EMBL; EU685789; ACD69648.1; -; Genomic_DNA.
DR EMBL; EU685790; ACD69649.1; -; Genomic_DNA.
DR EMBL; EU685791; ACD69650.1; -; Genomic_DNA.
DR EMBL; EU685792; ACD69651.1; -; Genomic_DNA.
DR EMBL; EU685793; ACD69652.1; -; Genomic_DNA.
DR EMBL; EU685794; ACD69653.1; -; Genomic_DNA.
DR EMBL; EU685795; ACD69654.1; -; Genomic_DNA.
DR EMBL; EU685796; ACD69655.1; -; Genomic_DNA.
DR EMBL; EU685797; ACD69656.1; -; Genomic_DNA.
DR EMBL; EU685798; ACD69657.1; -; Genomic_DNA.
DR EMBL; EU685799; ACD69658.1; -; Genomic_DNA.
DR EMBL; EU685800; ACD69659.1; -; Genomic_DNA.
DR PIR; JC7639; JC7639.
DR AlphaFoldDB; O80400; -.
DR SMR; O80400; -.
DR BioCyc; MetaCyc:MON-11999; -.
DR BRENDA; 2.3.1.156; 2716.
DR GO; GO:0102128; F:chalcone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016210; F:naringenin-chalcone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050634; F:phloroisovalerophenone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR012328; Chalcone/stilbene_synt_C.
DR InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR InterPro; IPR018088; Chalcone/stilbene_synthase_AS.
DR InterPro; IPR011141; Polyketide_synthase_type-III.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11877; PTHR11877; 1.
DR Pfam; PF02797; Chal_sti_synt_C; 1.
DR Pfam; PF00195; Chal_sti_synt_N; 1.
DR PIRSF; PIRSF000451; PKS_III; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR PROSITE; PS00441; CHALCONE_SYNTH; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Transferase.
FT CHAIN 1..394
FT /note="Phloroisovalerophenone synthase"
FT /id="PRO_0000216085"
FT ACT_SITE 166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT VARIANT 232
FT /note="A -> E (in strain: cv. Osvals's 72, cv. Cluster and
FT cv. Nugget)"
FT /evidence="ECO:0000269|PubMed:18519445, ECO:0000269|Ref.3"
FT VARIANT 385
FT /note="V -> L (in strain: cv. Osvals's 72)"
FT /evidence="ECO:0000269|Ref.3"
SQ SEQUENCE 394 AA; 43080 MW; 4C06DC3064AC4981 CRC64;
MASVTVEQIR KAQRAEGPAT ILAIGTAVPA NCFNQADFPD YYFRVTKSEH MTDLKKKFQR
MCEKSTIKKR YLHLTEEHLK QNPHLCEYNA PSLNTRQDML VVEVPKLGKE AAINAIKEWG
QPKSKITHLI FCTGSSIDMP GADYQCAKLL GLRPSVKRVM LYQLGCYAGG KVLRIAKDIA
ENNKGARVLI VCSEITACIF RGPSEKHLDC LVGQSLFGDG ASSVIVGADP DASVGERPIF
ELVSAAQTIL PNSDGAIAGH VTEAGLTFHL LRDVPGLISQ NIEKSLIEAF TPIGINDWNN
IFWIAHPGGP AILDEIEAKL ELKKEKMKAS REMLSEYGNM SCASVFFIVD EMRKQSSKEG
KSTTGDGLEW GALFGFGPGL TVETVVLHSV PTNV
