BAS_RHEPA
ID BAS_RHEPA Reviewed; 384 AA.
AC Q94FV7;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Polyketide synthase BAS;
DE EC=2.3.1.212;
DE AltName: Full=Benzalacetone synthase;
DE Short=RpBAS;
GN Name=BAS;
OS Rheum palmatum (Chinese rhubarb).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Polygonaceae; Polygonoideae; Rumiceae; Rheum.
OX NCBI_TaxID=137221;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HOMODIMER, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND CATALYTIC ACTIVITY.
RC TISSUE=Leaf;
RX PubMed=11389739; DOI=10.1046/j.1432-1327.2001.02255.x;
RA Abe I., Takahashi Y., Morita H., Noguchi H.;
RT "Benzalacetone synthase. A novel polyketide synthase that plays a crucial
RT role in the biosynthesis of phenylbutanones in Rheum palmatum.";
RL Eur. J. Biochem. 268:3354-3359(2001).
RN [2]
RP FUNCTION, MUTAGENESIS OF CYS-190; GLY-249 AND SER-331, CATALYTIC ACTIVITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17383877; DOI=10.1016/j.bmcl.2007.03.029;
RA Abe T., Morita H., Noma H., Kohno T., Noguchi H., Abe I.;
RT "Structure function analysis of benzalacetone synthase from Rheum
RT palmatum.";
RL Bioorg. Med. Chem. Lett. 17:3161-3166(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), POST-TRANSLATIONAL MODIFICATION AT
RP CYS-157, HOMODIMER, MUTAGENESIS OF 207-ILE-LEU-208, AND ACTIVE SITE.
RX PubMed=20080733; DOI=10.1073/pnas.0909982107;
RA Morita H., Shimokawa Y., Tanio M., Kato R., Noguchi H., Sugio S., Kohno T.,
RA Abe I.;
RT "A structure-based mechanism for benzalacetone synthase from Rheum
RT palmatum.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:669-673(2010).
CC -!- FUNCTION: Polyketide synthase producing 4-hydroxybenzalacetone. Can use
CC p-coumaryl-CoA as substrate but does not accept hexanoyl-CoA,
CC isobutyryl-CoA, isovaleryl-CoA, and acetyl-CoA as a substrates.
CC Catalyzes the initial key reaction step in the biosynthesis of
CC phenylbutanoids. {ECO:0000269|PubMed:11389739,
CC ECO:0000269|PubMed:17383877}.
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:11389739, ECO:0000269|PubMed:17383877};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for 4-coumaroyl-CoA (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:11389739, ECO:0000269|PubMed:17383877};
CC Note=kcat is 1.79 min(-1) with 4-coumaroyl-CoA as substrate (at pH 8
CC and 30 degrees Celsius).;
CC pH dependence:
CC Optimum pH is 8.0-8.8. {ECO:0000269|PubMed:11389739,
CC ECO:0000269|PubMed:17383877};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AF326911; AAK82824.1; -; mRNA.
DR PDB; 3A5Q; X-ray; 1.80 A; A/B=1-384.
DR PDB; 3A5R; X-ray; 1.60 A; A/B=1-384.
DR PDB; 3A5S; X-ray; 1.80 A; A/B=1-384.
DR PDBsum; 3A5Q; -.
DR PDBsum; 3A5R; -.
DR PDBsum; 3A5S; -.
DR AlphaFoldDB; Q94FV7; -.
DR SMR; Q94FV7; -.
DR DIP; DIP-58521N; -.
DR ChEMBL; CHEMBL1075247; -.
DR KEGG; ag:AAK82824; -.
DR BRENDA; 2.3.1.212; 13067.
DR UniPathway; UPA00154; -.
DR EvolutionaryTrace; Q94FV7; -.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA: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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Chromophore; Hydroxylation; Transferase.
FT CHAIN 1..384
FT /note="Polyketide synthase BAS"
FT /id="PRO_0000424291"
FT ACT_SITE 157
FT /note="Nucleophile and monoketide coumarate intermediate"
FT /evidence="ECO:0000269|PubMed:20080733"
FT MOD_RES 157
FT /note="S-(4-hydroxycinnamyl)cysteine"
FT /evidence="ECO:0000269|PubMed:20080733"
FT MUTAGEN 190
FT /note="C->G,T: Normal benzalacetone synthase activity."
FT /evidence="ECO:0000269|PubMed:17383877"
FT MUTAGEN 207..208
FT /note="IL->LF: Acquires an additional chalcone synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:20080733"
FT MUTAGEN 249
FT /note="G->L: Reduced benzalacetone synthase activity."
FT /evidence="ECO:0000269|PubMed:17383877"
FT MUTAGEN 331
FT /note="S->V: Enhanced benzalacetone synthase activity."
FT /evidence="ECO:0000269|PubMed:17383877"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:3A5R"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:3A5R"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 84..110
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:3A5R"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:3A5R"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 230..239
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 264..280
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:3A5R"
FT HELIX 334..348
FT /evidence="ECO:0007829|PDB:3A5R"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 359..367
FT /evidence="ECO:0007829|PDB:3A5R"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:3A5R"
FT STRAND 371..379
FT /evidence="ECO:0007829|PDB:3A5R"
SQ SEQUENCE 384 AA; 42225 MW; 4068107D7A3EE4B0 CRC64;
MATEEMKKLA TVMAIGTANP PNCYYQADFP DFYFRVTNSD HLINLKQKFK RLCENSRIEK
RYLHVTEEIL KENPNIAAYE ATSLNVRHKM QVKGVAELGK EAALKAIKEW GQPKSKITHL
IVCCLAGVDM PGADYQLTKL LDLDPSVKRF MFYHLGCYAG GTVLRLAKDI AENNKGARVL
IVCSEMTTTC FRGPSETHLD SMIGQAILGD GAAAVIVGAD PDLTVERPIF ELVSTAQTIV
PESHGAIEGH LLESGLSFHL YKTVPTLISN NIKTCLSDAF TPLNISDWNS LFWIAHPGGP
AILDQVTAKV GLEKEKLKVT RQVLKDYGNM SSATVFFIMD EMRKKSLENG QATTGEGLEW
GVLFGFGPGI TVETVVLRSV PVIS
