TBSYN_HYPAN
ID TBSYN_HYPAN Reviewed; 395 AA.
AC Q8SAS8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=2,4,6-trihydroxybenzophenone synthase;
DE EC=2.3.1.220 {ECO:0000269|PubMed:12795704, ECO:0000269|PubMed:19710020, ECO:0000269|PubMed:9459298};
DE AltName: Full=2,3',4,6-tetrahydroxybenzophenone synthase;
DE EC=2.3.1.151 {ECO:0000269|PubMed:12795704, ECO:0000269|PubMed:19710020, ECO:0000269|PubMed:9459298};
DE AltName: Full=Benzophenone synthase;
DE Short=HaBPS;
GN Name=BPS;
OS Hypericum androsaemum (Tutsan).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Hypericaceae; Hypericeae; Hypericum.
OX NCBI_TaxID=140968;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-167; ALA-260 AND
RP GLY-342.
RX PubMed=12795704; DOI=10.1046/j.1365-313x.2003.01771.x;
RA Liu B., Falkenstein-Paul H., Schmidt W., Beerhues L.;
RT "Benzophenone synthase and chalcone synthase from Hypericum androsaemum
RT cell cultures: cDNA cloning, functional expression, and site-directed
RT mutagenesis of two polyketide synthases.";
RL Plant J. 34:847-855(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9459298; DOI=10.1016/s0014-5793(97)01507-x;
RA Schmidt W., Beerhues L.;
RT "Alternative pathways of xanthone biosynthesis in cell cultures of
RT Hypericum androsaemum L.";
RL FEBS Lett. 420:143-146(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF
RP THR-135.
RX PubMed=19710020; DOI=10.1074/jbc.m109.038927;
RA Klundt T., Bocola M., Luetge M., Beuerle T., Liu B., Beerhues L.;
RT "A single amino acid substitution converts benzophenone synthase into
RT phenylpyrone synthase.";
RL J. Biol. Chem. 284:30957-30964(2009).
CC -!- FUNCTION: Type III polyketide synthase involved in the biosynthesis of
CC benzophenones and xanthones. The preferred substrate is benzoyl-CoA,
CC but can also use 3-hydroxybenzoyl-CoA with a lower activity.
CC {ECO:0000269|PubMed:12795704, ECO:0000269|PubMed:19710020,
CC ECO:0000269|PubMed:9459298}.
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:12795704,
CC ECO:0000269|PubMed:19710020, ECO:0000269|PubMed:9459298};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybenzoyl-CoA + 2 H(+) + 3 malonyl-CoA = 2,3',4,6-
CC tetrahydroxybenzophenone + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:19305,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57342, ChEBI:CHEBI:57384, ChEBI:CHEBI:77647;
CC EC=2.3.1.151; Evidence={ECO:0000269|PubMed:12795704,
CC ECO:0000269|PubMed:19710020, ECO:0000269|PubMed:9459298};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23.1 uM for malonyl-CoA {ECO:0000269|PubMed:12795704,
CC ECO:0000269|PubMed:9459298};
CC KM=5.7 uM for benzoyl-CoA {ECO:0000269|PubMed:12795704,
CC ECO:0000269|PubMed:9459298};
CC Note=kcat is 9.66 min(-1) with benzoyl-CoA as substrate.;
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:12795704,
CC ECO:0000269|PubMed:9459298};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:12795704, ECO:0000269|PubMed:9459298};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12795704}.
CC -!- MISCELLANEOUS: The T135L mutagenesis transforms the
CC trihydroxybenzophenone synthase into a phenylpyrone synthase.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000269|PubMed:12795704}.
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DR EMBL; AF352395; AAL79808.1; -; mRNA.
DR PDB; 5UCO; X-ray; 2.85 A; A/B=1-395.
DR PDBsum; 5UCO; -.
DR AlphaFoldDB; Q8SAS8; -.
DR SMR; Q8SAS8; -.
DR KEGG; ag:AAL79808; -.
DR BRENDA; 2.3.1.220; 2742.
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 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; Transferase.
FT CHAIN 1..395
FT /note="2,4,6-trihydroxybenzophenone synthase"
FT /id="PRO_0000216093"
FT ACT_SITE 167
FT /evidence="ECO:0000250|UniProtKB:P30074"
FT MUTAGEN 135
FT /note="T->G,A,V,I,N,Y: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19710020"
FT MUTAGEN 135
FT /note="T->L: Changed substrate specificity and catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:19710020"
FT MUTAGEN 135
FT /note="T->S,F: No effect."
FT /evidence="ECO:0000269|PubMed:19710020"
FT MUTAGEN 167
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12795704"
FT MUTAGEN 260
FT /note="A->G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12795704"
FT MUTAGEN 342
FT /note="G->S: No effect."
FT /evidence="ECO:0000269|PubMed:12795704"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:5UCO"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 94..120
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:5UCO"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:5UCO"
FT HELIX 345..359
FT /evidence="ECO:0007829|PDB:5UCO"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:5UCO"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:5UCO"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:5UCO"
SQ SEQUENCE 395 AA; 42828 MW; 3004310A4E878F1F CRC64;
MAPAMEYSTQ NGQGEGKKRA SVLAIGTTNP EHFILQEDYP DFYFRNTNSE HMTELKEKFK
RICVKSHIRK RHFYLTEEIL KENQGIATYG AGSLDARQRI LETEVPKLGQ EAALKAIAEW
GQPISKITHV VFATTSGFMM PGADYVITRL LGLNRTVRRV MLYNQGCFAG GTALRVAKDL
AENNEGARVL VVCAENTAMT FHAPNESHLD VIVGQAMFSD GAAALIIGAC PDVASGERAV
FNILSASQTI VPGSDGAITA HFYEMGMSYF LKEDVIPLFR DNIAAVMEEA FSPLGVSDWN
SLFYSIHPGG RGIIDGVAGN LGIKDENLVA TRHVLGEYGN MGSACVMFIL DELRKSSKVN
GKPTTGDGKE FGCLIGLGPG LTVEAVVLQS VPILQ
