PHLG_PSEPH
ID PHLG_PSEPH Reviewed; 307 AA.
AC A0A2C9EVE6; Q9RF01;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=2,4-diacetylphloroglucinol hydrolase {ECO:0000305};
DE Short=DAPG hydrolase {ECO:0000303|PubMed:16391073};
DE EC=3.7.1.24 {ECO:0000269|PubMed:16391073};
GN Name=phlG {ECO:0000303|PubMed:10671440};
GN ORFNames=PFLCHA0_c59060 {ECO:0000312|EMBL:AGL87634.1};
OS Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1124983;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=10671440; DOI=10.1128/jb.182.5.1215-1225.2000;
RA Schnider-Keel U., Seematter A., Maurhofer M., Blumer C., Duffy B.,
RA Gigot-Bonnefoy C., Reimmann C., Notz R., Defago G., Haas D., Keel C.;
RT "Autoinduction of 2,4-diacetylphloroglucinol biosynthesis in the biocontrol
RT agent Pseudomonas fluorescens CHA0 and repression by the bacterial
RT metabolites salicylate and pyoluteorin.";
RL J. Bacteriol. 182:1215-1225(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=24762936; DOI=10.1128/genomea.00322-14;
RA Jousset A., Schuldes J., Keel C., Maurhofer M., Daniel R., Scheu S.,
RA Thuermer A.;
RT "Full-genome sequence of the plant growth-promoting bacterium Pseudomonas
RT protegens CHA0.";
RL Genome Announc. 2:E00322-E00322(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=16391073; DOI=10.1128/aem.72.1.418-427.2006;
RA Bottiglieri M., Keel C.;
RT "Characterization of PhlG, a hydrolase that specifically degrades the
RT antifungal compound 2,4-diacetylphloroglucinol in the biocontrol agent
RT Pseudomonas fluorescens CHA0.";
RL Appl. Environ. Microbiol. 72:418-427(2006).
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. Does not
CC degrade other compounds with structures similar to DAPG, such as MAPG
CC and triacetylphloroglucinol, suggesting strict substrate specificity
CC (PubMed:16391073). Degradation of DAPG to MAPG may provide an
CC additional means of fine-tuning levels of this antibiotic or may help
CC avoid accumulation of a metabolite that at high levels may become toxic
CC to the producing bacterium (PubMed:16391073).
CC {ECO:0000269|PubMed:16391073}.
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:16391073};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q4K423};
CC -!- ACTIVITY REGULATION: Activity is strongly reduced by pyoluteorin, an
CC antifungal compound produced by the bacterium.
CC {ECO:0000269|PubMed:16391073}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 uM for DAPG {ECO:0000269|PubMed:16391073};
CC Note=kcat is 33 sec(-1). {ECO:0000269|PubMed:16391073};
CC pH dependence:
CC Activity is slightly enhanced at pH 6.6 and pH 6.0. Retains only 10%
CC of its maximal activity at pH 7.6 and is inactive at pH 8.0.
CC {ECO:0000269|PubMed:16391073};
CC -!- INDUCTION: Expression is induced by the GacS/GacA two-component system
CC and repressed by the pathway-specific regulators PhlF and PhlH.
CC Expression is not influenced by the substrate DAPG or the degradation
CC product MAPG. {ECO:0000269|PubMed:16391073}.
CC -!- DISRUPTION PHENOTYPE: The phlA-phlG double mutant cannot degrade DAPG.
CC {ECO:0000269|PubMed:16391073}.
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; AF207529; AAF20929.2; -; Genomic_DNA.
DR EMBL; CP003190; AGL87634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9EVE6; -.
DR SMR; A0A2C9EVE6; -.
DR STRING; 1124983.PFLCHA0_c59060; -.
DR EnsemblBacteria; AGL87634; AGL87634; PFLCHA0_c59060.
DR KEGG; pprc:PFLCHA0_c59060; -.
DR eggNOG; ENOG502Z8Q4; Bacteria.
DR HOGENOM; CLU_055313_0_1_6; -.
DR BRENDA; 3.7.1.24; 5121.
DR Proteomes; UP000013940; Chromosome.
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..307
FT /note="2,4-diacetylphloroglucinol hydrolase"
FT /id="PRO_0000450527"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4K423"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4K423"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4K423"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4K423"
SQ SEQUENCE 307 AA; 35126 MW; 50EC314235F5ED22 CRC64;
MAAICQFTPK DISMEARNMT PFTYFSLPMQ KLFLRNQAAV RNKPYAKYFR SEMRVPLSAV
RKIQQGPMAL EDTLTPSIED INRLLEPDFV SEESGYALLP GPMAYVQSRK FFPGCTAQMF
KWWFIWHPAE SERYTLWFPY AHVSNPCVHH QRLCDESLSF EERLYGNTFC ASEYVGDRLM
HLHIDFQQPA SLGLNTDLYR EAKIDGSVSA LMSLADHPEV PVSLMVHLFK EVPDGMYLTS
RYWVGAHPSM ARFPGAEKAA SLLKENGFGE AELETLAYEF AVHDMCEFNH LASFLPDLYR
EFGTPAA
