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2,4,6-trihydroxybenzophenone synthase (EC 2.3.1.220) (2,3',4,6-tetrahydroxybenzophenone synthase) (EC 2.3.1.151) (Benzophenone synthase) (HaBPS)

 TBSYN_HYPAN             Reviewed;         395 AA.
Q8SAS8;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
28-MAR-2018, entry version 66.
RecName: Full=2,4,6-trihydroxybenzophenone synthase;
EC=2.3.1.220 {ECO:0000269|PubMed:12795704, ECO:0000269|PubMed:19710020, ECO:0000269|PubMed:9459298};
AltName: Full=2,3',4,6-tetrahydroxybenzophenone synthase;
EC=2.3.1.151 {ECO:0000269|PubMed:12795704, ECO:0000269|PubMed:19710020, ECO:0000269|PubMed:9459298};
AltName: Full=Benzophenone synthase;
Short=HaBPS;
Name=BPS;
Hypericum androsaemum (Tutsan).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Malpighiales; Hypericaceae; Hypericeae;
Hypericum.
NCBI_TaxID=140968;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-167; ALA-260 AND
GLY-342.
PubMed=12795704; DOI=10.1046/j.1365-313X.2003.01771.x;
Liu B., Falkenstein-Paul H., Schmidt W., Beerhues L.;
"Benzophenone synthase and chalcone synthase from Hypericum
androsaemum cell cultures: cDNA cloning, functional expression, and
site-directed mutagenesis of two polyketide synthases.";
Plant J. 34:847-855(2003).
[2]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9459298; DOI=10.1016/S0014-5793(97)01507-X;
Schmidt W., Beerhues L.;
"Alternative pathways of xanthone biosynthesis in cell cultures of
Hypericum androsaemum L.";
FEBS Lett. 420:143-146(1997).
[3]
FUNCTION, CATALYTIC ACTIVITY, 3D-STRUCTURE MODELING, AND MUTAGENESIS
OF THR-135.
PubMed=19710020; DOI=10.1074/jbc.M109.038927;
Klundt T., Bocola M., Luetge M., Beuerle T., Liu B., Beerhues L.;
"A single amino acid substitution converts benzophenone synthase into
phenylpyrone synthase.";
J. Biol. Chem. 284:30957-30964(2009).
-!- FUNCTION: Type III polyketide synthase involved in the
biosynthesis of benzophenones and xanthones. The preferred
substrate is benzoyl-CoA, but can also use 3-hydroxybenzoyl-CoA
with a lower activity. {ECO:0000269|PubMed:12795704,
ECO:0000269|PubMed:19710020, ECO:0000269|PubMed:9459298}.
-!- CATALYTIC ACTIVITY: 3 malonyl-CoA + benzoyl-CoA = 4 CoA + 2,4,6-
trihydroxybenzophenone + 3 CO(2). {ECO:0000269|PubMed:12795704,
ECO:0000269|PubMed:19710020, ECO:0000269|PubMed:9459298}.
-!- CATALYTIC ACTIVITY: 3 malonyl-CoA + 3-hydroxybenzoyl-CoA = 4 CoA +
2,3',4,6-tetrahydroxybenzophenone + 3 CO(2).
{ECO:0000269|PubMed:12795704, ECO:0000269|PubMed:19710020,
ECO:0000269|PubMed:9459298}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=23.1 uM for malonyl-CoA {ECO:0000269|PubMed:12795704,
ECO:0000269|PubMed:9459298};
KM=5.7 uM for benzoyl-CoA {ECO:0000269|PubMed:12795704,
ECO:0000269|PubMed:9459298};
Note=Kcat is 9.66 min(-1) with benzoyl-CoA as substrate.;
pH dependence:
Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:12795704,
ECO:0000269|PubMed:9459298};
Temperature dependence:
Optimum temperature is 35 degrees Celsius.
{ECO:0000269|PubMed:12795704, ECO:0000269|PubMed:9459298};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12795704}.
-!- MISCELLANEOUS: The T135L mutagenesis transforms the
trihydroxybenzophenone synthase into a phenylpyrone synthase.
-!- SIMILARITY: Belongs to the chalcone/stilbene synthases family.
{ECO:0000269|PubMed:12795704}.
-----------------------------------------------------------------------
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EMBL; AF352395; AAL79808.1; -; mRNA.
PDB; 5UCO; X-ray; 2.85 A; A/B=1-395.
PDBsum; 5UCO; -.
ProteinModelPortal; Q8SAS8; -.
SMR; Q8SAS8; -.
PRIDE; Q8SAS8; -.
KEGG; ag:AAL79808; -.
KO; K21386; -.
GO; GO:0047181; F:tetrahydroxybenzophenone synthase activity; IDA:UniProtKB.
GO; GO:0016746; F:transferase activity, transferring acyl groups; IDA:UniProtKB.
GO; GO:0102735; F:trihydroxybenzophenone synthase activity; IEA:UniProtKB-EC.
GO; GO:1901787; P:benzoyl-CoA metabolic process; IDA:UniProtKB.
GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
GO; GO:2001293; P:malonyl-CoA metabolic process; IDA:UniProtKB.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR012328; Chalcone/stilbene_synth_C.
InterPro; IPR001099; Chalcone/stilbene_synthase_N.
InterPro; IPR011141; Polyketide_synthase_type-III.
InterPro; IPR016039; Thiolase-like.
PANTHER; PTHR11877; PTHR11877; 1.
Pfam; PF02797; Chal_sti_synt_C; 1.
Pfam; PF00195; Chal_sti_synt_N; 1.
PIRSF; PIRSF000451; PKS_III; 1.
SUPFAM; SSF53901; SSF53901; 2.
1: Evidence at protein level;
3D-structure; Acyltransferase; Transferase.
CHAIN 1 395 2,4,6-trihydroxybenzophenone synthase.
/FTId=PRO_0000216093.
ACT_SITE 167 167 {ECO:0000250|UniProtKB:P30074}.
MUTAGEN 135 135 T->G,A,V,I,N,Y: Loss of activity.
{ECO:0000269|PubMed:19710020}.
MUTAGEN 135 135 T->L: Changed substrate specificity and
catalytic activity.
{ECO:0000269|PubMed:19710020}.
MUTAGEN 135 135 T->S,F: No effect.
{ECO:0000269|PubMed:19710020}.
MUTAGEN 167 167 C->A: Loss of activity.
{ECO:0000269|PubMed:12795704}.
MUTAGEN 260 260 A->G: Loss of activity.
{ECO:0000269|PubMed:12795704}.
MUTAGEN 342 342 G->S: No effect.
{ECO:0000269|PubMed:12795704}.
STRAND 20 28 {ECO:0000244|PDB:5UCO}.
STRAND 33 35 {ECO:0000244|PDB:5UCO}.
HELIX 36 38 {ECO:0000244|PDB:5UCO}.
HELIX 39 45 {ECO:0000244|PDB:5UCO}.
TURN 46 48 {ECO:0000244|PDB:5UCO}.
HELIX 53 66 {ECO:0000244|PDB:5UCO}.
STRAND 70 72 {ECO:0000244|PDB:5UCO}.
HELIX 77 81 {ECO:0000244|PDB:5UCO}.
HELIX 84 87 {ECO:0000244|PDB:5UCO}.
HELIX 94 120 {ECO:0000244|PDB:5UCO}.
HELIX 124 126 {ECO:0000244|PDB:5UCO}.
STRAND 129 136 {ECO:0000244|PDB:5UCO}.
STRAND 139 141 {ECO:0000244|PDB:5UCO}.
HELIX 143 151 {ECO:0000244|PDB:5UCO}.
STRAND 158 164 {ECO:0000244|PDB:5UCO}.
HELIX 166 168 {ECO:0000244|PDB:5UCO}.
HELIX 169 183 {ECO:0000244|PDB:5UCO}.
STRAND 188 194 {ECO:0000244|PDB:5UCO}.
TURN 197 200 {ECO:0000244|PDB:5UCO}.
HELIX 210 215 {ECO:0000244|PDB:5UCO}.
STRAND 222 230 {ECO:0000244|PDB:5UCO}.
HELIX 233 235 {ECO:0000244|PDB:5UCO}.
STRAND 241 250 {ECO:0000244|PDB:5UCO}.
STRAND 257 263 {ECO:0000244|PDB:5UCO}.
STRAND 266 271 {ECO:0000244|PDB:5UCO}.
HELIX 275 280 {ECO:0000244|PDB:5UCO}.
HELIX 283 291 {ECO:0000244|PDB:5UCO}.
HELIX 292 294 {ECO:0000244|PDB:5UCO}.
STRAND 301 306 {ECO:0000244|PDB:5UCO}.
HELIX 310 321 {ECO:0000244|PDB:5UCO}.
HELIX 325 327 {ECO:0000244|PDB:5UCO}.
HELIX 329 338 {ECO:0000244|PDB:5UCO}.
HELIX 342 344 {ECO:0000244|PDB:5UCO}.
HELIX 345 359 {ECO:0000244|PDB:5UCO}.
TURN 365 368 {ECO:0000244|PDB:5UCO}.
STRAND 370 378 {ECO:0000244|PDB:5UCO}.
TURN 379 381 {ECO:0000244|PDB:5UCO}.
STRAND 382 389 {ECO:0000244|PDB:5UCO}.
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


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