PKS4_RUBID
ID PKS4_RUBID Reviewed; 383 AA.
AC B0LDU5;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Polyketide synthase 4;
DE Short=RiPKS4;
DE EC=2.3.1.212 {ECO:0000269|PubMed:12226219, ECO:0000269|PubMed:18068110};
DE EC=2.3.1.74 {ECO:0000269|PubMed:12226219, ECO:0000269|PubMed:18068110};
DE AltName: Full=Benzalacetone synthase PKS4;
DE Short=RiBAS;
DE AltName: Full=Naringenin-chalcone synthase PKS4;
GN Name=PKS4; Synonyms=BAS;
OS Rubus idaeus (Raspberry).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rubus.
OX NCBI_TaxID=32247;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Royalty; TISSUE=Leaf;
RX PubMed=18068110; DOI=10.1016/j.abb.2007.11.013;
RA Zheng D., Hrazdina G.;
RT "Molecular and biochemical characterization of benzalacetone synthase and
RT chalcone synthase genes and their proteins from raspberry (Rubus idaeus
RT L.).";
RL Arch. Biochem. Biophys. 470:139-145(2008).
RN [2]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP INDUCTION BY SUCROSE.
RX PubMed=12226219; DOI=10.1104/pp.110.3.791;
RA Borejsza-Wysocki W., Hrazdina G.;
RT "Aromatic polyketide synthases (purification, characterization, and
RT antibody development to benzalacetone synthase from raspberry fruits).";
RL Plant Physiol. 110:791-799(1996).
CC -!- FUNCTION: Bifunctional polyketide synthase producing both 4-
CC hydroxybenzalacetone and naringenin chalcone. Can use p-coumaryl-CoA
CC and ferulyl-CoA as substrates. Catalyzes the initial key reaction step
CC in the biosynthesis of phenylbutanoids. {ECO:0000269|PubMed:18068110}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-coumaroyl-CoA + H(+) + H2O + malonyl-CoA = 4-
CC hydroxybenzalacetone + 2 CO2 + 2 CoA; Xref=Rhea:RHEA:34483,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57355, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:68636; EC=2.3.1.212;
CC Evidence={ECO:0000269|PubMed:12226219, ECO:0000269|PubMed:18068110};
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:0000255|PROSITE-ProRule:PRU10023,
CC ECO:0000269|PubMed:12226219, ECO:0000269|PubMed:18068110};
CC -!- ACTIVITY REGULATION: Inhibited by glutathione.
CC {ECO:0000269|PubMed:12226219}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for malonyl-CoA {ECO:0000269|PubMed:12226219};
CC KM=3 uM for p-coumaryl CoA {ECO:0000269|PubMed:12226219};
CC pH dependence:
CC Optimum pH is approximately 8.0. {ECO:0000269|PubMed:12226219};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in fruits. {ECO:0000269|PubMed:18068110}.
CC -!- DEVELOPMENTAL STAGE: Progressively accumulates in fruits when berries
CC are white and full size until complete ripening.
CC {ECO:0000269|PubMed:18068110}.
CC -!- INDUCTION: By sucrose (at protein level).
CC {ECO:0000269|PubMed:12226219}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; EF694717; ABV54602.1; -; Genomic_DNA.
DR AlphaFoldDB; B0LDU5; -.
DR SMR; B0LDU5; -.
DR KEGG; ag:ABV54602; -.
DR BioCyc; MetaCyc:MON-15853; -.
DR BRENDA; 2.3.1.212; 5472.
DR BRENDA; 2.3.1.74; 5472.
DR UniPathway; UPA00154; -.
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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; Chromophore; Hydroxylation; Transferase.
FT CHAIN 1..383
FT /note="Polyketide synthase 4"
FT /id="PRO_0000424289"
FT ACT_SITE 164
FT /note="Nucleophile and monoketide coumarate intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
SQ SEQUENCE 383 AA; 42256 MW; D6078C3B6BD86EE7 CRC64;
MVTVEEVRKA QRAEGPATVL AIGTATPPNC VGQSTYPDYY FRITNSEHKI ELKQKFQRMC
DKSMIKKRYM YLTEEILKEN PSMCEYMAPS LDARQDMVIV EIPKLGKEAA TKAIKEWGQP
KSKITHLVFC TTSGVDMPGA DYQLIKLFGL RPSVKRLMMY QQGCFAGGTV LRLAKDLAEN
NRGARVLVVC SEITVVTFRG PSDTHLDCLV GQALFGDGVA SIIVGADPLP EIEKPLFELV
SAAQTILPDS EGAIEGHLRE VGLTFHLLEN VPALISKNIE KSLNETFKPL DIMDWNSLFW
IAHPGGPAIL DQVEAKLGLK PEKLEATGHI LSEYGNMSSA CVLFILDVVR RKSAANGVTT
RILSIGQISK SLLILAWFLF SLV
