PHP_ECOLI
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 03-AUG-2022, entry version 143.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=6.0 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 glycerol-
CC 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_SSZK01000008.1.
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 PDBsum; 1BF6; -.
DR PDBsum; 4LEF; -.
DR AlphaFoldDB; P45548; -.
DR SMR; P45548; -.
DR BioGRID; 4260764; 9.
DR DIP; DIP-10504N; -.
DR IntAct; P45548; 2.
DR STRING; 511145.b3379; -.
DR PaxDb; P45548; -.
DR PRIDE; P45548; -.
DR EnsemblBacteria; AAC76404; AAC76404; b3379.
DR EnsemblBacteria; BAE77912; BAE77912; BAE77912.
DR GeneID; 947891; -.
DR KEGG; ecj:JW3342; -.
DR KEGG; eco:b3379; -.
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 PhylomeDB; P45548; -.
DR BioCyc; EcoCyc:G7731-MON; -.
DR EvolutionaryTrace; P45548; -.
DR PRO; PR:P45548; -.
DR Proteomes; UP000000318; Chromosome.
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 GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR CDD; cd00530; PTE; 1.
DR InterPro; IPR017947; AryldialkylPase_Zn-BS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001559; Phosphotriesterase.
DR PANTHER; PTHR10819; PTHR10819; 1.
DR Pfam; PF02126; PTE; 1.
DR PIRSF; PIRSF016839; PhP; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1.
DR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
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 260..263
FT /evidence="ECO:0007829|PDB:1BF6"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:1BF6"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:1BF6"
FT HELIX 285..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
