ID   BIPS2_SORAU             Reviewed;         390 AA.
AC   D2DRC4;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=4-hydroxycoumarin synthase 1;
DE            EC=2.3.1.208;
DE   AltName: Full=Biphenyl synthase 2;
DE            Short=SaBIS2;
GN   Name=BIS2;
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=1.4 uM for benzoyl-CoA {ECO:0000269|PubMed:19757094};
CC         KM=10.0 uM for malonyl-CoA {ECO:0000269|PubMed:19757094};
CC         KM=2.3 uM for salicoyl-CoA {ECO:0000269|PubMed:19757094};
CC         Note=kcat is 0.89 min(-1) with benzoyl-CoA as substrate. kcat is 1.76
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: Not 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; FJ706068; ACW82504.1; -; mRNA.
DR   AlphaFoldDB; D2DRC4; -.
DR   SMR; D2DRC4; -.
DR   PRIDE; D2DRC4; -.
DR   KEGG; ag:ACW82504; -.
DR   SABIO-RK; D2DRC4; -.
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..390
FT                   /note="4-hydroxycoumarin synthase 1"
FT                   /id="PRO_0000421868"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  43083 MW;  E3A5CC4C1D2D4168 CRC64;
     MAPSVKDQVE PQHAKILAIG TANPPNVYYQ EDYPDFLFRV TKNEHRTDLR EKFDRICEKS
     RTRKRYLYLT EEILKANPCI YTYGAPSLDV RQDMLNPEVP KLGQEAALKA IKEWGQPISK
     ITHLIFCTAS CVDMPGADFQ LVKLLGLNPS VTRTMIYEAG CYAGATVLRL AKDFAENNEG
     ARVLVVCAEI TTVFFHGLTD THLDILVGQA LFADGASAVI VGANPEPEIE SPLFEIVACR
     QTIIPNSEHG VVANIREMGF NYYLSGEVPK FVGGNVVDFL TKTFEKVDGK NKDWNSLFFS
     VHPGGPAIVD QVEEQLGLKE GKLRATRHVL SEYGNMGAPS VHFILDEMRK KSIEEGKATT
     GEGLEWGVVI GIGPGLTVET AVLRSEFITC