ID   PHP_ECOLI               Reviewed;         292 AA.
AC   P45548; Q2M744;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   10-JUN-2026, entry version 156.
DE   RecName: Full=Phosphotriesterase homology protein {ECO:0000303|PubMed:30277746, ECO:0000303|PubMed:9548740};
DE            EC=3.1.-.- {ECO:0000269|PubMed:30277746};
GN   Name=php {ECO:0000303|PubMed:30277746, ECO:0000303|PubMed:9548740};
GN   Synonyms=yhfV; OrderedLocusNames=b3379, JW3342;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3] {ECO:0007744|PDB:1BF6}
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH ZINC, PARTIAL PROTEIN
RP   SEQUENCE, FUNCTION, COFACTOR, SUBUNIT, AND CIRCULAR DICHROISM ANALYSIS.
RX   PubMed=9548740; DOI=10.1021/bi971707+;
RA   Buchbinder J.L., Stephenson R.C., Dresser M.J., Pitera J.W., Scanlan T.S.,
RA   Fletterick R.J.;
RT   "Biochemical characterization and crystallographic structure of an
RT   Escherichia coli protein from the phosphotriesterase gene family.";
RL   Biochemistry 37:5096-5106(1998).
RN   [4]
RP   ERRATUM OF PUBMED:9548740.
RX   PubMed=9692977; DOI=10.1021/bi985043v;
RA   Buchbinder J.L., Stephenson R.C., Dresser M.J., Pitera J.W., Scanlan T.S.,
RA   Fletterick R.J.;
RL   Biochemistry 37:10860-10860(1998).
RN   [5] {ECO:0007744|PDB:4LEF}
RP   X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH BETA-D-GLUCOSE AND
RP   ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX   PubMed=30277746; DOI=10.1021/acs.biochem.8b00935;
RA   Nemmara V.V., Xiang D.F., Fedorov A.A., Fedorov E.V., Bonanno J.B.,
RA   Almo S.C., Raushel F.M.;
RT   "Substrate Profile of the Phosphotriesterase Homology Protein from
RT   Escherichia coli.";
RL   Biochemistry 57:6219-6227(2018).
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphorylated glyceryl acetates
CC       in which the presence of a phosphate group is required for the
CC       enzymatic hydrolysis. Hydrolyzes a dibutyl glycerol derivative
CC       suggesting it acts on phosphoglycerol substrates with a butyrate
CC       leaving group. Also active with aromatic acetates and propionates. No
CC       activity with various sugar phosphates, with various
CC       nitrophenylphosphate or nitrophenylphosphonate derivatives, or with
CC       phosphorylated or non-phosphorylated sugar lactones tested. Does not
CC       hydrolyze non-phosphorylated carboxyesters with long chain leaving
CC       groups (PubMed:30277746). No general esterase, aminopeptidase,
CC       sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and
CC       phosphotriesterase activities detected when tested with the following
CC       non-specific substrates: p-nitrophenyl acetate, L-alanine nitroanilide,
CC       p-nitrophenyl sulfate, bis(p-nitrophenyl) phosphate, paraoxon, and p-
CC       nitrophenyl phosphate (PubMed:9548740). {ECO:0000269|PubMed:30277746,
CC       ECO:0000269|PubMed:9548740}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:30277746, ECO:0000269|PubMed:9548740};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:30277746,
CC       ECO:0000269|PubMed:9548740};
CC   -!- ACTIVITY REGULATION: Activity is higher in the enzyme containing Mn(2+)
CC       than that containing Zn(2+). {ECO:0000269|PubMed:30277746}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.8 mM for 2-naphthyl acetate (in the presence of 1.0 mM MnCl(2),
CC         at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:30277746};
CC         KM=5.5 mM for (2S)-1,2-diacetyl glycerol-3-phosphate (in the presence
CC         of 1.0 mM MnCl(2), at pH 8.0 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:30277746};
CC         KM=6 mM for rac-(2R,2S)-1,2-diacetyl glycerol-3-phosphate (in the
CC         presence of 1.0 mM MnCl(2), at pH 8.0 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:30277746};
CC         Note=kcat is 2.5 sec(-1) with 2-naphthyl acetate as substrate. kcat
CC         is 27 sec(-1) with (2S)-1,2-diacetyl glycerol-3-phosphate as
CC         substrate. kcat is 28 sec(-1) with rac-(2R,2S)-1,2-diacetyl
CC         glycerol-3-phosphate as substrate. {ECO:0000269|PubMed:30277746};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9548740}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR   EMBL; U18997; AAA58176.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76404.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77912.1; -; Genomic_DNA.
DR   PIR; F65132; F65132.
DR   RefSeq; NP_417838.1; NC_000913.3.
DR   RefSeq; WP_000007010.1; NZ_CP009789.1.
DR   PDB; 1BF6; X-ray; 1.70 A; A/B=2-292.
DR   PDB; 4LEF; X-ray; 1.84 A; A/B/C/D/E/F/G/H=1-292.
DR   AlphaFoldDB; P45548; -.
DR   SMR; P45548; -.
DR   BioGRID; 4260764; 10.
DR   DIP; DIP-10504N; -.
DR   FunCoup; P45548; 218.
DR   IntAct; P45548; 2.
DR   STRING; 511145.b3379; -.
DR   PaxDb; 511145-b3379; -.
DR   EnsemblBacteria; AAC76404; AAC76404; b3379.
DR   GeneID; 75173536; -.
DR   GeneID; 947891; -.
DR   KEGG; ecj:JW3342; -.
DR   KEGG; eco:b3379; -.
DR   KEGG; ecoc:C3026_18340; -.
DR   PATRIC; fig|1411691.4.peg.3351; -.
DR   EchoBASE; EB2753; -.
DR   eggNOG; COG1735; Bacteria.
DR   HOGENOM; CLU_054760_1_1_6; -.
DR   InParanoid; P45548; -.
DR   OMA; MVKCGFI; -.
DR   OrthoDB; 9795018at2; -.
DR   PhylomeDB; P45548; -.
DR   BioCyc; EcoCyc:G7731-MONOMER; -.
DR   EvolutionaryTrace; P45548; -.
DR   PRO; PR:P45548; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR   CDD; cd00530; PTE; 1.
DR   FunFam; 3.20.20.140:FF:000063; Phosphotriesterase homology protein; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR017947; AryldialkylPase_Zn-BS.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR001559; Phosphotriesterase.
DR   NCBIfam; NF007373; PRK09875.1; 1.
DR   PANTHER; PTHR10819; PHOSPHOTRIESTERASE-RELATED; 1.
DR   PANTHER; PTHR10819:SF3; PHOSPHOTRIESTERASE-RELATED PROTEIN; 1.
DR   Pfam; PF02126; PTE; 1.
DR   PIRSF; PIRSF016839; PhP; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1.
DR   PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
DR   PDBsum; 1BF6; -.
DR   PDBsum; 4LEF; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..292
FT                   /note="Phosphotriesterase homology protein"
FT                   /id="PRO_0000205362"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         148..149
FT                   /ligand="beta-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:15903"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         176
FT                   /ligand="beta-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:15903"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         178
FT                   /ligand="beta-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:15903"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         181
FT                   /ligand="beta-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:15903"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         243
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         280
FT                   /ligand="beta-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:15903"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0007744|PDB:4LEF"
FT   BINDING         284
FT                   /ligand="beta-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:15903"
FT                   /evidence="ECO:0000269|PubMed:30277746,
FT                   ECO:0007744|PDB:4LEF"
FT   STRAND          7..13
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   STRAND          15..18
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           20..23
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           33..45
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   STRAND          48..53
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           63..73
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           92..95
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           98..110
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   STRAND          120..127
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           135..151
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   STRAND          155..158
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           165..174
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           193..201
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   STRAND          205..208
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   TURN            214..216
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           219..231
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   STRAND          238..240
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           251..253
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           261..265
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           266..271
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           276..280
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           281..285
FT                   /evidence="ECO:0007829|PDB:1BF6"
FT   HELIX           286..290
FT                   /evidence="ECO:0007829|PDB:1BF6"
SQ   SEQUENCE   292 AA;  32915 MW;  1480C6858E5E8230 CRC64;
     MSFDPTGYTL AHEHLHIDLS GFKNNVDCRL DQYAFICQEM NDLMTRGVRN VIEMTNRYMG
     RNAQFMLDVM RETGINVVAC TGYYQDAFFP EHVATRSVQE LAQEMVDEIE QGIDGTELKA
     GIIAEIGTSE GKITPLEEKV FIAAALAHNQ TGRPISTHTS FSTMGLEQLA LLQAHGVDLS
     RVTVGHCDLK DNLDNILKMI DLGAYVQFDT IGKNSYYPDE KRIAMLHALR DRGLLNRVML
     SMDITRRSHL KANGGYGYDY LLTTFIPQLR QSGFSQADVD VMLRENPSQF FQ
//