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PHLD_PSEFL
ID   PHLD_PSEFL              Reviewed;         349 AA.
AC   Q51725;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Phloroglucinol synthase {ECO:0000305};
DE            EC=2.3.1.253 {ECO:0000250|UniProtKB:Q4K418};
GN   Name=phlD {ECO:0000303|PubMed:10322017};
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=Q2-87;
RX   PubMed=10322017; DOI=10.1128/jb.181.10.3155-3163.1999;
RA   Bangera M.G., Thomashow L.S.;
RT   "Identification and characterization of a gene cluster for synthesis of the
RT   polyketide antibiotic 2,4-diacetylphloroglucinol from Pseudomonas
RT   fluorescens Q2-87.";
RL   J. Bacteriol. 181:3155-3163(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Q2-1;
RA   Moynihan J.A., O'Gara F., Morrissey J.P.;
RT   "Examination of 2,4-DAPG production among phl positive isolates.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CLASSIFICATION, AND PHYLOGENETIC ANALYSIS.
RX   PubMed=11332728; DOI=10.1094/mpmi.2001.14.5.639;
RA   Ramette A., Moenne-Loccoz Y., Defago G.;
RT   "Polymorphism of the polyketide synthase gene phID in biocontrol
RT   fluorescent pseudomonads producing 2,4-diacetylphloroglucinol and
RT   comparison of PhID with plant polyketide synthases.";
RL   Mol. Plant Microbe Interact. 14:639-652(2001).
CC   -!- FUNCTION: Type III polyketide synthase that catalyzes the synthesis of
CC       phloroglucinol from three molecules of malonyl-CoA (By similarity).
CC       Required for the synthesis of the polyketide antibiotic 2,4-
CC       diacetylphloroglucinol (2,4-DAPG) (PubMed:10322017).
CC       {ECO:0000250|UniProtKB:Q4K418, ECO:0000269|PubMed:10322017}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 H(+) + 3 malonyl-CoA = 1,3,5-trihydroxybenzene + 3 CO2 + 3
CC         CoA; Xref=Rhea:RHEA:50380, ChEBI:CHEBI:15378, ChEBI:CHEBI:16204,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384;
CC         EC=2.3.1.253; Evidence={ECO:0000250|UniProtKB:Q4K418};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:10322017}.
CC   -!- DISRUPTION PHENOTYPE: Mutant cannot produce monoacetylphloroglucinol
CC       (MAPG) or 2,4-DAPG. {ECO:0000269|PubMed:10322017}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305|PubMed:11332728}.
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DR   EMBL; U41818; AAB48106.1; -; Genomic_DNA.
DR   EMBL; GU984569; ADG03656.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q51725; -.
DR   SMR; Q51725; -.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Acyltransferase; Antibiotic biosynthesis; Transferase.
FT   CHAIN           1..349
FT                   /note="Phloroglucinol synthase"
FT                   /id="PRO_0000449606"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000250|UniProtKB:Q54240"
SQ   SEQUENCE   349 AA;  38403 MW;  1266AD411E63F154 CRC64;
     MSTLCKPSLL FPHYKITQQQ MIDHLEQLHD DHPRMALAKR MIQNTQVNER YLVLPIDELA
     VHTGFTHRSI VYEREARRMS SIAARQAIEN AGLTTDDIRM VAVTSCTGFM MPSLTAHLIN
     DLGLRTSTVQ LPIAQLGCVA GAAAINRAND FASLSPDNHA LIVSLEFSSL CYQPQDTKLH
     AFISAALFGD AVSACVMRAD DKAPGFKIAK TGSYFLPDSE HYIKYDVKDS GFHFTLDKAV
     MNSIKDVAPM MEELNFETFN QHCAQNDFFI FHTGGRKILD ELVLQLDLEP GRVAQSRDSL
     SEAGNIASVV VFDVLKRQFD SGPANGATGM LAAFGPGFTA EMAVGKWVA
 
 
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