2PS_GERHY
ID 2PS_GERHY Reviewed; 402 AA.
AC P48391;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=2-pyrone synthase;
DE Short=2-PS;
DE EC=2.3.1.-;
DE AltName: Full=G2ps1;
GN Name=2PS; Synonyms=CHS2;
OS Gerbera hybrida (Daisy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Mutisioideae; Mutisieae;
OC Gerbera.
OX NCBI_TaxID=18101;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corolla;
RX PubMed=7787187; DOI=10.1007/bf00042037;
RA Helariutta Y., Elomaa P., Kotilainen M., Griesbach R.J., Schroeder J.,
RA Teeri T.H.;
RT "Chalcone synthase-like genes active during corolla development are
RT differentially expressed and encode enzymes with different catalytic
RT properties in Gerbera hybrida (Asteraceae).";
RL Plant Mol. Biol. 28:47-60(1995).
RN [2]
RP SEQUENCE REVISION TO 259.
RA Teeri T.H.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RA Eckermann S., Schroeder G., Schmidt J., Strack D., Edrada R.A.,
RA Helariutta Y., Elomaa P., Kotilainen M., Kilpelaeinen I., Proksch P.,
RA Teeri T.H., Schroeder J.;
RT "New pathway to polyketides in plants.";
RL Nature 396:387-390(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH ACETOACETYL-COA.
RX PubMed=11137815; DOI=10.1016/s1074-5521(00)00041-7;
RA Jez J.M., Austin M.B., Ferrer J.-L., Bowman M.E., Schroeder J., Noel J.P.;
RT "Structural control of polyketide formation in plant-specific polyketide
RT synthases.";
RL Chem. Biol. 7:919-930(2000).
CC -!- FUNCTION: Polyketide synthase, which uses acetyl-CoA and two
CC condensation reactions with malonyl-CoA to form triacetic acid lactone
CC (also called methylpyrone), a precursor of phytoalexin. May participate
CC in insect and pathogen resistance. {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
CC -!- CAUTION: Ref.3 has shown that this is not a chalcone synthase, but a
CC pyrone synthase. {ECO:0000305}.
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DR EMBL; Z38097; CAA86219.2; -; mRNA.
DR PIR; S56700; S55465.
DR PDB; 1EE0; X-ray; 2.05 A; A/B=1-402.
DR PDB; 1QLV; X-ray; 2.10 A; A/B=1-402.
DR PDBsum; 1EE0; -.
DR PDBsum; 1QLV; -.
DR AlphaFoldDB; P48391; -.
DR SMR; P48391; -.
DR EvolutionaryTrace; P48391; -.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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; Transferase.
FT CHAIN 1..402
FT /note="2-pyrone synthase"
FT /id="PRO_0000216092"
FT ACT_SITE 169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1QLV"
FT HELIX 96..122
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:1EE0"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:1EE0"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 276..292
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:1EE0"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1EE0"
FT HELIX 346..360
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 370..379
FT /evidence="ECO:0007829|PDB:1EE0"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:1EE0"
FT STRAND 383..391
FT /evidence="ECO:0007829|PDB:1EE0"
SQ SEQUENCE 402 AA; 43749 MW; 593257F979EE45A8 CRC64;
MGSYSSDDVE VIREAGRAQG LATILAIGTA TPPNCVAQAD YADYYFRVTK SEHMVDLKEK
FKRICEKTAI KKRYLALTED YLQENPTMCE FMAPSLNARQ DLVVTGVPML GKEAAVKAID
EWGLPKSKIT HLIFCTTAGV DMPGADYQLV KLLGLSPSVK RYMLYQQGCA AGGTVLRLAK
DLAENNKGSR VLIVCSEITA ILFHGPNENH LDSLVAQALF GDGAAALIVG SGPHLAVERP
IFEIVSTDQT ILPDTEKAMK LHLREGGLTF QLHRDVPLMV AKNIENAAEK ALSPLGITDW
NSVFWMVHPG GRAILDQVER KLNLKEDKLR ASRHVLSEYG NLISACVLFI IDEVRKRSMA
EGKSTTGEGL DCGVLFGFGP GMTVETVVLR SVRVTAAVAN GN
