ID TBSYN_GARMA Reviewed; 391 AA.
AC L7NCQ3;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=2,4,6-trihydroxybenzophenone synthase;
DE Short=GmBPS;
DE EC=2.3.1.220;
GN Name=BPS;
OS Garcinia mangostana (Mangosteen).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Clusiaceae; Garcinieae; Garcinia.
OX NCBI_TaxID=58228;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, MUTAGENESIS OF THR-133; ALA-257
RP AND GLY-339, AND 3D-STRUCTURE MODELING.
RX PubMed=22390826; DOI=10.1016/j.phytochem.2012.02.002;
RA Nualkaew N., Morita H., Shimokawa Y., Kinjo K., Kushiro T., De-Eknamkul W.,
RA Ebizuka Y., Abe I.;
RT "Benzophenone synthase from Garcinia mangostana L. pericarps.";
RL Phytochemistry 77:60-69(2012).
CC -!- FUNCTION: Type III polyketide synthase involved in the biosynthesis of
CC benzophenones and xanthones. Produces mainly 2,4,6-
CC trihydroxybenzophenone together with minor amounts of tetraketide
CC lactone, triketide lactone and diketide lactone. The preferred
CC substrate is benzoyl-CoA, but can also use acetyl-CoA, phenylacetyl-
CC CoA, hexanoyl-CoA, cinnamoyl-CoA, p-coumaroyl-CoA and salicoyl-CoA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + 2 H(+) + 3 malonyl-CoA = 2,4,6-
CC trihydroxybenzophenone + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:35143,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57369, ChEBI:CHEBI:57384, ChEBI:CHEBI:77765;
CC EC=2.3.1.220; Evidence={ECO:0000269|PubMed:22390826};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.65 uM for benzoyl-CoA {ECO:0000269|PubMed:22390826};
CC KM=16.38 uM for malonyl-CoA {ECO:0000269|PubMed:22390826};
CC Note=kcat is 2.97 min(-1) with benzoyl-CoA as substrate. kcat is 3.49
CC min(-1) with malonyl-CoA as substrate.;
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:22390826};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:22390826};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22390826}.
CC -!- TISSUE SPECIFICITY: Expressed in young fruit pericarp.
CC {ECO:0000269|PubMed:22390826}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; JF907623; AEI27291.1; -; mRNA.
DR PDB; 7CBF; X-ray; 2.30 A; A/B=1-391.
DR PDBsum; 7CBF; -.
DR AlphaFoldDB; L7NCQ3; -.
DR SMR; L7NCQ3; -.
DR KEGG; ag:AEI27291; -.
DR BRENDA; 2.3.1.151; 13052.
DR BRENDA; 2.3.1.220; 13052.
DR GO; GO:0016746; F:acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047181; F:tetrahydroxybenzophenone synthase activity; IDA:UniProtKB.
DR GO; GO:0102735; F:trihydroxybenzophenone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:1901787; P:benzoyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:2001293; P:malonyl-CoA metabolic process; IDA:UniProtKB.
DR CDD; cd00831; CHS_like; 1.
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:SF108; CHALCONE SYNTHASE-LIKE; 1.
DR PANTHER; PTHR11877; HYDROXYMETHYLGLUTARYL-COA SYNTHASE; 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; Thiolase-like; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Transferase.
FT CHAIN 1..391
FT /note="2,4,6-trihydroxybenzophenone synthase"
FT /id="PRO_0000422264"
FT ACT_SITE 165
FT /evidence="ECO:0000250"
FT MUTAGEN 133
FT /note="T->L: Changed substrate specificity."
FT /evidence="ECO:0000269|PubMed:22390826"
FT MUTAGEN 257
FT /note="A->G: No effect."
FT /evidence="ECO:0000269|PubMed:22390826"
FT MUTAGEN 339
FT /note="G->S: No effect with benzoyl-CoA as substrate, but
FT loss of activity with p-coumaroyl-CoA as substrate."
FT /evidence="ECO:0000269|PubMed:22390826"
FT MUTAGEN 339
FT /note="G->V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22390826"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 92..118
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:7CBF"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 219..228
FT /evidence="ECO:0007829|PDB:7CBF"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 272..288
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 322..335
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:7CBF"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 366..375
FT /evidence="ECO:0007829|PDB:7CBF"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:7CBF"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:7CBF"
SQ SEQUENCE 391 AA; 42712 MW; D76112A2736BD4AC CRC64;
MAPAMDSAQN GHQSRGSANV LAIGTANPPN VILQEDYPDF YFKVTNSEHL TDLKEKFKRI
CVKSKTRKRH FYLTEQILKE NPGIATYGAG SLDSRQKILE TEIPKLGKEA AMVAIQEWGQ
PVSKITHVVF ATTSGFMMPG ADYSITRLLG LNPNVRRVMI YNQGCFAGGT ALRVAKDLAE
NNKGARVLVV CAENTAMTFH GPNENHLDVL VGQAMFSDGA AALIIGANPN LPEERPVYEM
VAAHQTIVPE SDGAIVAHFY EMGMSYFLKE NVIPLFGNNI EACMEAAFKE YGISDWNSLF
YSVHPGGRAI VDGIAEKLGL DEENLKATRH VLSEYGNMGS ACVIFILDEL RKKSKEEKKL
TTGDGKEWGC LIGLGPGLTV ETVVLRSVPI A
//
