PHLG_PSEF5
ID PHLG_PSEF5 Reviewed; 294 AA.
AC Q4K423;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=2,4-diacetylphloroglucinol hydrolase {ECO:0000305};
DE Short=DAPG hydrolase {ECO:0000303|PubMed:20018877};
DE EC=3.7.1.24 {ECO:0000269|PubMed:20018877};
GN Name=phlG {ECO:0000303|PubMed:20018877};
GN OrderedLocusNames=PFL_5952 {ECO:0000312|EMBL:AAY95142.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
RN [2] {ECO:0007744|PDB:3HWP}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF TYR-121; ASN-132; GLU-160; HIS-214; TYR-229;
RP HIS-270 AND GLU-274.
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=20018877; DOI=10.1074/jbc.m109.044180;
RA He Y.X., Huang L., Xue Y., Fei X., Teng Y.B., Rubin-Pitel S.B., Zhao H.,
RA Zhou C.Z.;
RT "Crystal structure and computational analyses provide insights into the
RT catalytic mechanism of 2,4-diacetylphloroglucinol hydrolase PhlG from
RT Pseudomonas fluorescens.";
RL J. Biol. Chem. 285:4603-4611(2010).
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:20018877}.
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:20018877};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20018877};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=272 uM for DAPG {ECO:0000269|PubMed:20018877};
CC Note=kcat is 4.7 sec(-1). {ECO:0000269|PubMed:20018877};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20018877}.
CC -!- DOMAIN: Contains a small N-terminal domain involved in dimerization and
CC a large C-terminal Bet v1-like fold catalytic domain.
CC {ECO:0000269|PubMed:20018877}.
CC -!- SIMILARITY: Belongs to the DAPG/phloretin hydrolase family.
CC {ECO:0000305}.
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DR EMBL; CP000076; AAY95142.1; -; Genomic_DNA.
DR RefSeq; WP_011064125.1; NC_004129.6.
DR PDB; 3HWP; X-ray; 2.00 A; A/B=1-294.
DR PDBsum; 3HWP; -.
DR AlphaFoldDB; Q4K423; -.
DR SMR; Q4K423; -.
DR STRING; 220664.PFL_5952; -.
DR EnsemblBacteria; AAY95142; AAY95142; PFL_5952.
DR KEGG; pfl:PFL_5952; -.
DR PATRIC; fig|220664.5.peg.6068; -.
DR eggNOG; ENOG502Z8Q4; Bacteria.
DR HOGENOM; CLU_055313_0_1_6; -.
DR OMA; ELRSRYW; -.
DR OrthoDB; 1551529at2; -.
DR BRENDA; 3.7.1.24; 5121.
DR EvolutionaryTrace; Q4K423; -.
DR Proteomes; UP000008540; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IDA:JCVI.
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 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..294
FT /note="2,4-diacetylphloroglucinol hydrolase"
FT /id="PRO_0000450525"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20018877,
FT ECO:0007744|PDB:3HWP"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20018877,
FT ECO:0007744|PDB:3HWP"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20018877,
FT ECO:0007744|PDB:3HWP"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20018877,
FT ECO:0007744|PDB:3HWP"
FT MUTAGEN 121
FT /note="Y->A: 81-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20018877"
FT MUTAGEN 132
FT /note="N->A: 14-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20018877"
FT MUTAGEN 160
FT /note="E->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:20018877"
FT MUTAGEN 214
FT /note="H->A: 4-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20018877"
FT MUTAGEN 214
FT /note="H->Q: 5-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20018877"
FT MUTAGEN 229
FT /note="Y->A: 15-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20018877"
FT MUTAGEN 229
FT /note="Y->F: 3-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20018877"
FT MUTAGEN 270
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20018877"
FT MUTAGEN 274
FT /note="E->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:20018877"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3HWP"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3HWP"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:3HWP"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:3HWP"
FT STRAND 90..100
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:3HWP"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:3HWP"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:3HWP"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:3HWP"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:3HWP"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3HWP"
FT STRAND 207..219
FT /evidence="ECO:0007829|PDB:3HWP"
FT STRAND 222..232
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:3HWP"
FT HELIX 257..289
FT /evidence="ECO:0007829|PDB:3HWP"
SQ SEQUENCE 294 AA; 33773 MW; DC43F525E7FCF6E4 CRC64;
MEARNMTPFT YFSLPMQKLF LRNQAAVRNK PYAKYFRSEM RVPLSAVRKI QQGPMALEDT
LTPSIEDINR LLEPDFVSEE SGYALLPGPM AYVQSRKFFP GCTAQMFKWW FIWHPAESER
YTLWFPYAHV SNPCVHHQRL RDESLSFEER LYGNTFCASE YVGDRLMHLH IDFQQPASLG
LNTDLYREAK IDGSVSALMS LADHPEVPVS LMVHLFKEVP DGMYLTSRYW VGAHPSMARF
PGAEKAASLL KENGFGEAEL ETLAYEFAVH DMCEFNHLAS FLPDLYREFG TPAA
