DPSS_PINSY
ID DPSS_PINSY Reviewed; 393 AA.
AC Q02323;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Pinosylvin synthase {ECO:0000303|PubMed:1426272};
DE EC=2.3.1.146 {ECO:0000269|PubMed:1426272};
DE AltName: Full=Dihydropinosylvin synthase {ECO:0000303|PubMed:1426272};
DE AltName: Full=Pinosylvin-forming stilbene synthase;
DE AltName: Full=Stilbene synthase;
DE Short=STS;
OS Pinus sylvestris (Scotch pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3349;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1536925; DOI=10.1007/bf00040665;
RA Fliegmann J., Schroeder G., Schanz S., Britsch L., Schroeder J.;
RT "Molecular analysis of chalcone and dihydropinosylvin synthase from Scots
RT pine (Pinus sylvestris), and differential regulation of these and related
RT enzyme activities in stressed plants.";
RL Plant Mol. Biol. 18:489-503(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1451785; DOI=10.1016/0014-5793(92)80206-v;
RA Schwekendiek A., Pfeffer G., Kindl H.;
RT "Pine stilbene synthase cDNA, a tool for probing environmental stress.";
RL FEBS Lett. 301:41-44(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-172, FUNCTION, AND MUTAGENESIS.
RX PubMed=1400374; DOI=10.1016/s0021-9258(19)36721-3;
RA Schroeder G., Schroeder J.;
RT "A single change of histidine to glutamine alters the substrate preference
RT of a stilbene synthase.";
RL J. Biol. Chem. 267:20558-20560(1992).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1426272; DOI=10.1016/0014-5793(92)81187-q;
RA Schanz S., Schroeder G., Schroeder J.;
RT "Stilbene synthase from Scots pine (Pinus sylvestris).";
RL FEBS Lett. 313:71-74(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS), AND REACTION MECHANISM.
RX PubMed=15380179; DOI=10.1016/j.chembiol.2004.05.024;
RA Austin M.B., Bowman M.E., Ferrer J.-L., Schroeder J., Noel J.P.;
RT "An aldol switch discovered in stilbene synthases mediates cyclization
RT specificity of type III polyketide synthases.";
RL Chem. Biol. 11:1179-1194(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH METHYLMALONYL COA.
RA Ng S.H., Chirgadze D., Spiteller D., Li T.L., Spencer J.B., Blundell T.L.;
RT "Crystal structure of stilbene synthase from Pinus sylvestris, complexed
RT with methylmalonyl CoA.";
RL Submitted (SEP-2004) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the production of pinosylvin from cinnamoyl-CoA and
CC malonyl-CoA, and dihydropinosylvin from dihydrocinnamoyl-CoA.
CC {ECO:0000269|PubMed:1426272}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamoyl-CoA + 3 H(+) + 3 malonyl-CoA = (E)-pinosylvin +
CC 4 CO2 + 4 CoA; Xref=Rhea:RHEA:12552, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17323, ChEBI:CHEBI:57252,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384; EC=2.3.1.146;
CC Evidence={ECO:0000269|PubMed:1426272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpropanoyl-CoA + 3 H(+) + 3 malonyl-CoA = 4 CO2 + 4 CoA
CC + dihydropinosylvin; Xref=Rhea:RHEA:46096, ChEBI:CHEBI:4579,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:85676;
CC Evidence={ECO:0000269|PubMed:1426272};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for cinnamoyl-CoA {ECO:0000269|PubMed:1426272};
CC KM=5 uM for dihydrocinnamoyl-CoA {ECO:0000269|PubMed:1426272};
CC Vmax=0.12 nmol/sec/mg enzyme with cinnamoyl-CoA as substrate
CC {ECO:0000269|PubMed:1426272};
CC Vmax=0.15 nmol/sec/mg enzyme with dihydrocinnamoyl-CoA as substrate
CC {ECO:0000269|PubMed:1426272};
CC -!- PATHWAY: Phytoalexin biosynthesis; hydropinosylvin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By stress.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; X60753; CAA43165.1; -; Genomic_DNA.
DR EMBL; S50350; AAB24341.2; -; mRNA.
DR EMBL; L00659; AAA50524.1; -; Genomic_DNA.
DR EMBL; L00660; AAA50525.1; -; Genomic_DNA.
DR PIR; S20514; S20514.
DR PIR; S21123; S21123.
DR PDB; 1U0U; X-ray; 2.11 A; A/B/C/D/E/F=1-393.
DR PDB; 1XES; X-ray; 1.70 A; A/B/C/D=1-393.
DR PDB; 1XET; X-ray; 2.00 A; A/B/C/D=1-393.
DR PDBsum; 1U0U; -.
DR PDBsum; 1XES; -.
DR PDBsum; 1XET; -.
DR AlphaFoldDB; Q02323; -.
DR SMR; Q02323; -.
DR BRENDA; 2.3.1.146; 4856.
DR SABIO-RK; Q02323; -.
DR UniPathway; UPA00374; -.
DR EvolutionaryTrace; Q02323; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050198; F:pinosylvin 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 3D-structure; Acyltransferase; Cytoplasm; Stress response; Transferase.
FT CHAIN 1..393
FT /note="Pinosylvin synthase"
FT /id="PRO_0000216078"
FT ACT_SITE 167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT BINDING 57..60
FT /ligand="substrate"
FT BINDING 270
FT /ligand="substrate"
FT BINDING 308..310
FT /ligand="substrate"
FT MUTAGEN 165
FT /note="H->Q: Reduced activity."
FT /evidence="ECO:0000269|PubMed:1400374"
FT CONFLICT 306
FT /note="H -> N (in Ref. 2; AAB24341)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="R -> P (in Ref. 2; AAB24341)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="V -> F (in Ref. 2; AAB24341)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="Q -> E (in Ref. 2; AAB24341)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="C -> F (in Ref. 2; AAB24341)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="Missing (in Ref. 2; AAB24341)"
FT /evidence="ECO:0000305"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 94..120
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:1XES"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:1XES"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 239..249
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:1XES"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:1XES"
FT HELIX 344..358
FT /evidence="ECO:0007829|PDB:1XES"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 369..377
FT /evidence="ECO:0007829|PDB:1XES"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:1XES"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:1XES"
SQ SEQUENCE 393 AA; 42735 MW; D4A00036D3E72641 CRC64;
MGGVDFEGFR KLQRADGFAS ILAIGTANPP NAVDQSTYPD FYFRITGNEH NTELKDKFKR
ICERSAIKQR YMYLTEEILK KNPDVCAFVE VPSLDARQAM LAMEVPRLAK EAAEKAIQEW
GQSKSGITHL IFCSTTTPDL PGADFEVAKL LGLHPSVKRV GVFQHGCFAG GTVLRMAKDL
AENNRGARVL VICSETTAVT FRGPSETHLD SLVGQALFGD GASALIVGAD PIPQVEKACF
EIVWTAQTVV PNSEGAIGGK VREVGLTFQL KGAVPDLISA NIENCMVEAF SQFKISDWNK
LFWVVHPGGR AILDRVEAKL NLDPTKLIPT RHVMSEYGNM SSACVHFILD QTRKASLQNG
CSTTGEGLEM GVLFGFGPGL TIETVVLKSV PIQ
