ID BIPS1_SORAU Reviewed; 390 AA.
AC Q27Z07;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=3,5-dihydroxybiphenyl synthase;
DE EC=2.3.1.177;
DE AltName: Full=Biphenyl synthase 1;
DE Short=SaBIS1;
GN Name=BIS1;
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, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION BY ELICITOR.
RX PubMed=17109150; DOI=10.1007/s00425-006-0435-5;
RA Liu B., Raeth T., Beuerle T., Beerhues L.;
RT "Biphenyl synthase, a novel type III polyketide synthase.";
RL Planta 225:1495-1503(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=14595561; DOI=10.1007/s00425-003-1144-y;
RA Liu B., Beuerle T., Klundt T., Beerhues L.;
RT "Biphenyl synthase from yeast-extract-treated cell cultures of Sorbus
RT aucuparia.";
RL Planta 218:492-496(2004).
RN [3]
RP FUNCTION, AND 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).
RN [4]
RP INDUCTION BY HYDROGEN PEROXIDE.
RX PubMed=22086110; DOI=10.1007/s00425-011-1545-2;
RA Qiu X., Lei C., Huang L., Li X., Hao H., Du Z., Wang H., Ye H.,
RA Beerhues L., Liu B.;
RT "Endogenous hydrogen peroxide is a key factor in the yeast extract-induced
RT activation of biphenyl biosynthesis in cell cultures of Sorbus aucuparia.";
RL Planta 235:217-223(2012).
CC -!- FUNCTION: Type III polyketide synthase involved in the biosynthesis of
CC the phytoalexins bisphenyls and dibenzofurans. Can also use salicoyl-
CC CoA and malonyl-CoA to produce a diketide intermediate yielding 4-
CC hydroxycoumarine after cyclization and enolization. Can also use m-
CC hydroxybenzoyl-CoA as substrate, producing m-hydroxybenzoyl diacetic
CC acid lactone as a derailment product. No activity with p-
CC hydroxybenzoyl-CoA, CoA-linked cinnamic acids or acetyl-CoA.
CC {ECO:0000269|PubMed:14595561, ECO:0000269|PubMed:17109150,
CC ECO:0000269|PubMed:19757094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + 3 H(+) + 3 malonyl-CoA = biphenyl-3,5-diol + 4
CC CO2 + 4 CoA; Xref=Rhea:RHEA:22292, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:52069, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57369, ChEBI:CHEBI:57384; EC=2.3.1.177;
CC Evidence={ECO:0000269|PubMed:14595561, ECO:0000269|PubMed:17109150};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 uM for benzoyl-CoA {ECO:0000269|PubMed:17109150,
CC ECO:0000269|PubMed:19757094};
CC KM=6.2 uM for malonyl-CoA {ECO:0000269|PubMed:17109150,
CC ECO:0000269|PubMed:19757094};
CC KM=0.8 uM for salicoyl-CoA {ECO:0000269|PubMed:17109150,
CC ECO:0000269|PubMed:19757094};
CC Note=kcat is 0.43 min(-1) with benzoyl-CoA as substrate. kcat is 0.27
CC min(-1) with salicoyl-CoA as substrate.;
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:17109150,
CC ECO:0000269|PubMed:19757094};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:17109150, ECO:0000269|PubMed:19757094};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17109150}.
CC -!- INDUCTION: Up-regulated by elicitor and by endogenous H(2)O(2).
CC {ECO:0000269|PubMed:17109150, ECO:0000269|PubMed:22086110}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; DQ286036; ABB89212.1; -; mRNA.
DR AlphaFoldDB; Q27Z07; -.
DR SMR; Q27Z07; -.
DR KEGG; ag:ABB89212; -.
DR BioCyc; MetaCyc:MONOMER-17615; -.
DR BRENDA; 2.3.1.177; 5766.
DR SABIO-RK; Q27Z07; -.
DR GO; GO:0033815; F:biphenyl synthase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0052315; P:phytoalexin biosynthetic 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 Acyltransferase; Transferase.
FT CHAIN 1..390
FT /note="3,5-dihydroxybiphenyl synthase"
FT /id="PRO_0000418419"
FT ACT_SITE 161
FT /evidence="ECO:0000250"
SQ SEQUENCE 390 AA; 43014 MW; 9012DAC1BD6547F8 CRC64;
MAPLVKNHGE PQHAKILAIG TANPPNVYYQ KDYPDFLFRV TKNEHRTDLR EKFDRICEKS
RTRKRYLHLT EEILKANPSI YTYGAPSLDV RQDMLNSEVP KLGQQAALKA IKEWGQPISK
ITHLIFCTAS CVDMPGADFQ LVKLLGLNPS VTRTMIYEAG CYAGATVLRL AKDFAENNEG
ARVLVVCAEI TTVFFHGLTD THLDILVGQA LFADGASAVI VGANPEPKIE RPLFEIVACR
QTIIPNSEHG VVANIREMGF TYYLSGEVPK FVGGNVVDFL TKTFEKVDGK NKDWNSLFFS
VHPGGPAIVD QVEEQLGLKE GKLRATRHVL SEYGNMGAPS VHFILDDMRK KSIEEGKSTT
GEGLEWGVVI GIGPGLTVET AVLRSESIPC
//
