ID   PHLG_PSESP              Reviewed;         294 AA.
AC   F7J5X9;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=2,4-diacetylphloroglucinol hydrolase {ECO:0000303|PubMed:22790955};
DE            Short=DAPG hydrolase {ECO:0000303|PubMed:22451400};
DE            EC=3.7.1.24 {ECO:0000269|PubMed:22790955};
GN   Name=phlG {ECO:0000303|PubMed:22451400};
OS   Pseudomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YGJ3;
RX   PubMed=22451400; DOI=10.1271/bbb.110860;
RA   Hayashi A., Saitou H., Mori T., Matano I., Sugisaki H., Maruyama K.;
RT   "Molecular and catalytic properties of monoacetylphloroglucinol
RT   acetyltransferase from Pseudomonas sp. YGJ3.";
RL   Biosci. Biotechnol. Biochem. 76:559-566(2012).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=YGJ3;
RX   PubMed=22790955; DOI=10.1271/bbb.120054;
RA   Saitou H., Watanabe M., Maruyama K.;
RT   "Molecular and catalytic properties of 2,4-diacetylphloroglucinol hydrolase
RT   (PhlG) from Pseudomonas sp. YGJ3.";
RL   Biosci. Biotechnol. Biochem. 76:1239-1241(2012).
CC   -!- FUNCTION: Hydrolase that specifically degrades the potent antimicrobial
CC       compound 2,4-diacetylphloroglucinol (DAPG) to equimolar amounts of
CC       mildly toxic monoacetylphloroglucinol (MAPG) and acetate.
CC       {ECO:0000269|PubMed:22790955}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,4-diacetylphloroglucinol + H2O = 2-acetylphloroglucinol +
CC         acetate; Xref=Rhea:RHEA:59184, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:64344, ChEBI:CHEBI:140662; EC=3.7.1.24;
CC         Evidence={ECO:0000269|PubMed:22790955};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:22790955};
CC   -!- ACTIVITY REGULATION: Specifically and significantly activated by
CC       CoCl(2). Competitively inhibited by MAPG, but not by 2-hydroxy- and 4-
CC       hydroxyacetophenone. {ECO:0000269|PubMed:22790955}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=24 uM for DAPG {ECO:0000269|PubMed:22790955};
CC         Note=kcat is 5.8 sec(-1). {ECO:0000269|PubMed:22790955};
CC       pH dependence:
CC         Optimum pH is about 6.0. {ECO:0000269|PubMed:22790955};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22790955}.
CC   -!- SIMILARITY: Belongs to the DAPG/phloretin hydrolase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB636682; BAK39611.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7J5X9; -.
DR   SMR; F7J5X9; -.
DR   KEGG; ag:BAK39611; -.
DR   BRENDA; 3.7.1.24; 5085.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR041526; DAPG_hydrolase.
DR   Pfam; PF18089; DAPG_hydrolase; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..294
FT                   /note="2,4-diacetylphloroglucinol hydrolase"
FT                   /id="PRO_0000450528"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q4K423"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q4K423"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q4K423"
FT   BINDING         274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q4K423"
SQ   SEQUENCE   294 AA;  33675 MW;  C7EAD24A47FA39F4 CRC64;
     MEARNMTPFT YFSLPMQKLF LRNQAAVRNK PYAKYFRTEM RVPLSAVRKI QQGPMALEDT
     LTPSIEDINR LLEPDFVSEE SGYALLPGPM AYVQSRKFFP GCTAQMFKWW FIWHPAESER
     YTLWFPYAHV SNPCVHHQRL CDESLSFEER LYGNTFCASE YVGDRLMHLH IDFQQPASLG
     LNTDLYREAK IDGSVSALMS LADHPEVPVS LMVHLFKEVP GGMYLTSRYW VGAHPSMARF
     PGAEKAASLL KENGFGEAEL ETLAYEFAVH DMCEFNHLAS FLPDLYREFG TPAA