ID   BIPS3_SORAU             Reviewed;         388 AA.
AC   D2DRC5;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=4-hydroxycoumarin synthase 2;
DE            EC=2.3.1.208;
DE   AltName: Full=Biphenyl synthase 3;
DE            Short=SaBIS3;
GN   Name=BIS3;
OS   Sorbus aucuparia (European mountain ash) (Rowan).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Sorbus.
OX   NCBI_TaxID=36599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY ELICITOR, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19757094; DOI=10.1007/s11103-009-9548-0;
RA   Liu B., Raeth T., Beuerle T., Beerhues L.;
RT   "A novel 4-hydroxycoumarin biosynthetic pathway.";
RL   Plant Mol. Biol. 72:17-25(2010).
CC   -!- FUNCTION: Type III polyketide synthase involved preferentially in the
CC       biosynthesis of 4-hydroxycoumarin from salicoyl-CoA. Can also use
CC       benzoyl-CoA and malonyl-CoA to produce 3,5-dihydroxybiphenyl as a major
CC       product and benzoyldiacetic acid lactone as a minor side product. Can
CC       also use m-hydroxybenzoyl-CoA as substrate, producing m-hydroxybenzoyl
CC       diacetic acid lactone as a derailment product. No activity with p-
CC       hydroxybenzoyl-CoA, CoA-linked cinnamic acids or acetyl-CoA.
CC       {ECO:0000269|PubMed:19757094}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxybenzoyl-CoA + malonyl-CoA = 4-hydroxycoumarin + CO2 +
CC         2 CoA; Xref=Rhea:RHEA:34175, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:67148, ChEBI:CHEBI:77858;
CC         EC=2.3.1.208;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.6 uM for benzoyl-CoA {ECO:0000269|PubMed:19757094};
CC         KM=10.1 uM for malonyl-CoA {ECO:0000269|PubMed:19757094};
CC         KM=3.2 uM for salicoyl-CoA {ECO:0000269|PubMed:19757094};
CC         Note=kcat is 1.02 min(-1) with benzoyl-CoA as substrate. kcat is 2.22
CC         min(-1) with salicoyl-CoA as substrate.;
CC       pH dependence:
CC         Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:19757094};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius.
CC         {ECO:0000269|PubMed:19757094};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by elicitor. {ECO:0000269|PubMed:19757094}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; FJ706069; ACW82505.1; -; mRNA.
DR   AlphaFoldDB; D2DRC5; -.
DR   SMR; D2DRC5; -.
DR   KEGG; ag:ACW82505; -.
DR   SABIO-RK; D2DRC5; -.
DR   GO; GO:0033815; F:biphenyl synthase activity; IDA:UniProtKB.
DR   GO; GO:1901886; P:2-hydroxybenzoyl-CoA catabolic process; IDA:UniProtKB.
DR   GO; GO:1901884; P:4-hydroxycoumarin biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0009805; P:coumarin biosynthetic 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   Acyltransferase; Transferase.
FT   CHAIN           1..388
FT                   /note="4-hydroxycoumarin synthase 2"
FT                   /id="PRO_0000421869"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  43030 MW;  4DDF75646DD765C2 CRC64;
     MAPVVKNEPQ HAKILAIGTA NPPNVFHQKD YPDFLFRVTK NEHRTDLREK FDRICEKSRT
     KKRYLHLTEE MLKANPNIYT YGAPSLNVRQ DICNIEVPKL GQEASLKAIK EWGQPISKIT
     HLIFCTASCV DMPGCDFQLI KLLGLDPSVT RTMIYEAGCY AGATVLRMAK DFAENNKGAR
     VLVVCAEITT VFFHGLTDTH LDILVGQALF ADGASAVIVG ANPEPEIERP LFEIVACRQT
     ILPNSEHGVV ANIREMGFNY YLSGDVPKFV GGNVVDFMTK TFEKVDGKNK DWNSLFFSVH
     PGGPAIVDQV EEKLGLKEGK LRATRHVLSE YGNMGAPTVH FILDEMRNKS IEEGKTTTGE
     GLEWGVVIGI GPGLTVETAV LRSEFITY