PCHP_PSEAE
ID PCHP_PSEAE Reviewed; 349 AA.
AC Q9HTR2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Phosphorylcholine phosphatase {ECO:0000303|PubMed:2116592};
DE Short=PChP {ECO:0000303|PubMed:15886911};
DE EC=3.1.3.75 {ECO:0000269|PubMed:10387109, ECO:0000269|PubMed:15886911, ECO:0000269|PubMed:17106798, ECO:0000269|PubMed:2116592};
DE AltName: Full=Phosphoethanolamine/phosphocholine phosphatase {ECO:0000305};
DE Flags: Precursor;
GN Name=pchP {ECO:0000303|PubMed:15886911};
GN OrderedLocusNames=PA5292 {ECO:0000312|EMBL:AAG08677.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=2116592; DOI=10.1007/bf00223566;
RA Garrido M.N., Lisa T.A., Albelo S., Lucchesi G.I., Domenech C.E.;
RT "Identification of the Pseudomonas aeruginosa acid phosphatase as a
RT phosphorylcholine phosphatase activity.";
RL Mol. Cell. Biochem. 94:89-95(1990).
RN [3]
RP FUNCTION IN VIRULENCE.
RX DOI=10.1007/BF01570153;
RA Lisa T.A., Lucchesi G.I., Domenech C.E.;
RT "Pathogenicity of Pseudomonas aeruginosa and its relationship to the
RT choline metabolism through the action of cholinesterase, acid phosphatase,
RT and phospholipase C.";
RL Curr. Microbiol. 29:193-199(1994).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=10387109; DOI=10.1007/pl00006819;
RA Salvano M.A., Domenech C.E.;
RT "Kinetic properties of purified Pseudomonas aeruginosa phosphorylcholine
RT phosphatase indicated that this enzyme may be utilized by the bacteria to
RT colonize in different environments.";
RL Curr. Microbiol. 39:1-8(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=15886911; DOI=10.1007/s00284-004-4499-9;
RA Massimelli M.J., Beassoni P.R., Forrellad M.A., Barra J.L., Garrido M.N.,
RA Domenech C.E., Lisa A.T.;
RT "Identification, cloning, and expression of Pseudomonas aeruginosa
RT phosphorylcholine phosphatase gene.";
RL Curr. Microbiol. 50:251-256(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, AND
RP MUTAGENESIS OF 53-ASP--THR-57; ASP-53; ASP-55; THR-57; SER-188; LYS-264;
RP GLY-283; ASP-284; ASP-287 AND ASP-289.
RX PubMed=17106798; DOI=10.1007/s00284-006-0365-2;
RA Beassoni P.R., Otero L.H., Massimelli M.J., Lisa A.T., Domenech C.E.;
RT "Critical active-site residues identified by site-directed mutagenesis in
RT Pseudomonas aeruginosa phosphorylcholine phosphatase, a new member of the
RT haloacid dehalogenases hydrolase superfamily.";
RL Curr. Microbiol. 53:534-539(2006).
RN [7]
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-53; ASP-55;
RP THR-57; SER-188; ASP-284 AND ASP-289, AND ACTIVE SITE.
RX PubMed=18801468; DOI=10.1016/j.bbapap.2008.08.014;
RA Beassoni P.R., Otero L.H., Lisa A.T., Domenech C.E.;
RT "Using a molecular model and kinetic experiments in the presence of
RT divalent cations to study the active site and catalysis of Pseudomonas
RT aeruginosa phosphorylcholine phosphatase.";
RL Biochim. Biophys. Acta 1784:2038-2044(2008).
RN [8]
RP FUNCTION IN VIRULENCE, AND INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=19103776; DOI=10.1128/iai.01008-08;
RA Wargo M.J., Ho T.C., Gross M.J., Whittaker L.A., Hogan D.A.;
RT "GbdR regulates Pseudomonas aeruginosa plcH and pchP transcription in
RT response to choline catabolites.";
RL Infect. Immun. 77:1103-1111(2009).
RN [9]
RP EXPRESSION, SUBUNIT, DISULFIDE BOND, AND PRELIMINARY CRYSTALLIZATION.
RX PubMed=20064618; DOI=10.1016/j.pep.2010.01.006;
RA Beassoni P.R., Berti F.P., Otero L.H., Risso V.A., Ferreyra R.G.,
RA Lisa A.T., Domenech C.E., Ermacora M.R.;
RT "Preparation and biophysical characterization of recombinant Pseudomonas
RT aeruginosa phosphorylcholine phosphatase.";
RL Protein Expr. Purif. 71:153-159(2010).
RN [10]
RP COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=20135339; DOI=10.1007/s10534-010-9289-1;
RA Otero L.H., Beassoni P.R., Lisa A.T., Domenech C.E.;
RT "Transition from octahedral to tetrahedral geometry causes the activation
RT or inhibition by Znf2+ of Pseudomonas aeruginosa phosphorylcholine
RT phosphatase.";
RL BioMetals 23:307-314(2010).
RN [11]
RP SUBUNIT, AND CRYSTALLIZATION.
RX PubMed=20693680; DOI=10.1107/s1744309110024061;
RA Otero L.H., Beassoni P.R., Domenech C.E., Lisa A.T., Albert A.;
RT "Crystallization and preliminary X-ray diffraction analysis of Pseudomonas
RT aeruginosa phosphorylcholine phosphatase.";
RL Acta Crystallogr. F 66:957-960(2010).
RN [12]
RP INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=20869215; DOI=10.1016/j.micres.2010.07.004;
RA Massimelli M.J., Sanchez D.G., Buchieri M.V., Olvera L., Beassoni P.R.,
RA Schweizer H.P., Morett E., Lisa A.T.;
RT "Choline catabolism, sigma54 factor and NtrC are required for the full
RT expression of the Pseudomonas aeruginosa phosphorylcholine phosphatase
RT gene.";
RL Microbiol. Res. 166:380-390(2011).
RN [13]
RP ACTIVITY REGULATION, DOMAIN, AND MUTAGENESIS OF GLU-64; GLU-65 AND
RP 104-TYR--TYR-106.
RX PubMed=21515416; DOI=10.1016/j.bbapap.2011.04.003;
RA Beassoni P.R., Otero L.H., Boetsch C., Domenech C.E., Gonzalez-Nilo F.D.,
RA Lisa A.T.;
RT "Site-directed mutations and kinetic studies show key residues involved in
RT alkylammonium interactions and reveal two sites for phosphorylcholine in
RT Pseudomonas aeruginosa phosphorylcholine phosphatase.";
RL Biochim. Biophys. Acta 1814:858-863(2011).
RN [14]
RP ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=21660097; DOI=10.4061/2011/918283;
RA Otero L.H., Beassoni P.R., Boetsch C., Lisa A.T., Domenech C.E.;
RT "Different effects of Mg and Zn on the two sites for alkylammonium
RT compounds in Pseudomonas aeruginosa phosphorylcholine phosphatase.";
RL Enzyme Res. 2011:918283-918283(2011).
RN [15]
RP REVIEW.
RX PubMed=21915373; DOI=10.4061/2011/561841;
RA Domenech C.E., Otero L.H., Beassoni P.R., Lisa A.T.;
RT "Phosphorylcholine phosphatase: a peculiar enzyme of Pseudomonas
RT aeruginosa.";
RL Enzyme Res. 2011:561841-561841(2011).
RN [16] {ECO:0007744|PDB:4AS2, ECO:0007744|PDB:4AS3}
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 23-349 IN COMPLEX WITH MAGNESIUM,
RP DISULFIDE BONDS, COFACTOR, SUBUNIT, DOMAIN, AND MUTAGENESIS OF THR-57;
RP GLU-64; GLU-65; 104-TYR--TYR-106; CYS-109; SER-188; LYS-264; GLY-283;
RP ASP-284 AND ASP-289.
RX PubMed=22922065; DOI=10.1016/j.jmb.2012.07.024;
RA Infantes L., Otero L.H., Beassoni P.R., Boetsch C., Lisa A.T.,
RA Domenech C.E., Albert A.;
RT "The structural domains of Pseudomonas aeruginosa phosphorylcholine
RT phosphatase cooperate in substrate hydrolysis: 3D structure and enzymatic
RT mechanism.";
RL J. Mol. Biol. 423:503-514(2012).
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphorylcholine (PCho) to
CC produce choline and inorganic phosphate (PubMed:2116592,
CC PubMed:10387109, PubMed:15886911, PubMed:17106798). Can also hydrolyze
CC phosphorylethanolamine and the nonphysiological substrate p-
CC nitrophenylphosphate (pNPP) (PubMed:2116592, PubMed:10387109,
CC PubMed:15886911, PubMed:17106798). Shows higher affinity and catalytic
CC efficiency with phosphorylcholine as substrate (PubMed:2116592).
CC {ECO:0000269|PubMed:10387109, ECO:0000269|PubMed:15886911,
CC ECO:0000269|PubMed:17106798, ECO:0000269|PubMed:2116592}.
CC -!- FUNCTION: Is probably involved in virulence (PubMed:19103776, Ref.3).
CC The bacteria may break down various host compounds or host cell
CC membranes through the coordinated action of phospholipase C and
CC phosphocholine phosphatase. The final consequence of the action of
CC these enzymes is an increase of the free choline concentration, which
CC may promote the pathogenicity of P.aeruginosa (Ref.3).
CC {ECO:0000269|PubMed:19103776, ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + phosphocholine = choline + phosphate;
CC Xref=Rhea:RHEA:10492, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:295975; EC=3.1.3.75;
CC Evidence={ECO:0000269|PubMed:10387109, ECO:0000269|PubMed:15886911,
CC ECO:0000269|PubMed:17106798, ECO:0000269|PubMed:2116592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + phosphoethanolamine = ethanolamine + phosphate;
CC Xref=Rhea:RHEA:16089, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:58190; EC=3.1.3.75;
CC Evidence={ECO:0000269|PubMed:10387109, ECO:0000269|PubMed:15886911,
CC ECO:0000269|PubMed:2116592};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10387109, ECO:0000269|PubMed:18801468,
CC ECO:0000269|PubMed:20135339, ECO:0000269|PubMed:22922065};
CC Note=At pH 5.0 Mg(2+), Zn(2+) or Cu(2+) is required for maximal
CC activity (PubMed:10387109, PubMed:18801468). Mg2(+) shows low affinity
CC with respect to Zn(2+) as a cofactor, but it is probably the preferred
CC cation due to its abundance and its ability to work in a broad range of
CC pH conditions (PubMed:20135339). {ECO:0000269|PubMed:10387109,
CC ECO:0000269|PubMed:18801468, ECO:0000269|PubMed:20135339};
CC -!- ACTIVITY REGULATION: Activity is inhibited by high concentrations of
CC phosphorylcholine, phosphorylethanolamine, choline or betaine
CC (PubMed:2116592, PubMed:15886911, PubMed:21515416). Displays different
CC properties depending on the substrate utilized, the pH conditions as
CC well as the presence or absence of metal ions (PubMed:10387109,
CC PubMed:21660097). At pH 5, activity is inhibited by Al(3+) ions. At pH
CC 7.4, the enzyme cannot catalyze the hydrolysis of pNPP,
CC phosphorylethanolamine is a poor substrate in either the presence or
CC absence of divalent cations, and activity measured with
CC phosphorylcholine is independent of divalent cations or is not
CC inhibited by Al(3+) ions (PubMed:10387109). Mg(2+) produces identical
CC activation at pH 5.0 and 7.4, but Zn(2+) is an activator at pH 5.0 and
CC becomes an inhibitor at pH 7.4 (PubMed:20135339). This inhibition at pH
CC 7.4 may be due to a transition from octahedral to tetrahedral
CC coordination geometry, which is produced by hydrolysis of the Zn-
CC hexacoordinated complex (PubMed:20135339).
CC {ECO:0000269|PubMed:10387109, ECO:0000269|PubMed:15886911,
CC ECO:0000269|PubMed:20135339, ECO:0000269|PubMed:2116592,
CC ECO:0000269|PubMed:21515416, ECO:0000269|PubMed:21660097}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for phosphocholine {ECO:0000269|PubMed:2116592};
CC KM=0.03 mM for phosphocholine (at pH 5.0 or 7.4, high affinity site,
CC without signal peptide) {ECO:0000269|PubMed:17106798};
CC KM=0.05 mM for phosphocholine (at pH 5.0 or 7.4, high affinity site,
CC with signal peptide) {ECO:0000269|PubMed:17106798};
CC KM=0.5 mM for phosphocholine (at pH 5.0 or 7.4, low affinity site,
CC without signal peptide) {ECO:0000269|PubMed:17106798};
CC KM=3.6 mM for phosphocholine (at pH 5.0, low affinity site, with
CC signal peptide) {ECO:0000269|PubMed:17106798};
CC KM=3.5 mM for phosphocholine (at pH 7.4, low affinity site, with
CC signal peptide) {ECO:0000269|PubMed:17106798};
CC KM=0.7 mM for phosphoethanolamine {ECO:0000269|PubMed:2116592};
CC KM=2.0 mM for pNPP {ECO:0000269|PubMed:2116592};
CC KM=2.0 mM for pNPP (at pH 5.0, with ou without signal peptide)
CC {ECO:0000269|PubMed:17106798};
CC KM=3.2 mM for pNPP (at pH 5.0, in the presence of Mg(2+))
CC {ECO:0000269|PubMed:18801468};
CC KM=3.5 mM for pNPP (at pH 5.0, in the presence of Zn(2+))
CC {ECO:0000269|PubMed:18801468};
CC KM=12.2 mM for pNPP (at pH 5.0, in the presence of Cu(2+))
CC {ECO:0000269|PubMed:18801468};
CC Vmax=1250 nmol/min/mg enzyme with phosphocholine as substrate
CC {ECO:0000269|PubMed:2116592};
CC Vmax=1390 nmol/min/mg enzyme with phosphoethanolamine as substrate
CC {ECO:0000269|PubMed:2116592};
CC Vmax=950 nmol/min/mg enzyme with pNPP as substrate
CC {ECO:0000269|PubMed:2116592};
CC Vmax=130 umol/min/mg enzyme with pNPP as substrate (at pH 5.0, in the
CC presence of Mg(2+)) {ECO:0000269|PubMed:18801468};
CC Vmax=230 umol/min/mg enzyme with pNPP as substrate (at pH 5.0, in the
CC presence of Zn(2+)) {ECO:0000269|PubMed:18801468};
CC Vmax=330 umol/min/mg enzyme with pNPP as substrate (at pH 5.0, in the
CC presence of Cu(2+)) {ECO:0000269|PubMed:18801468};
CC pH dependence:
CC Optimum pH is dependent on the substrate: optimum pH is 5-8 with
CC phosphorylcholine, 6 with phosphorylethanolamine and 5 with pNPP.
CC {ECO:0000269|PubMed:10387109};
CC -!- SUBUNIT: Monomer (PubMed:10387109, PubMed:15886911). Homodimer
CC (PubMed:20064618, PubMed:20693680, PubMed:22922065). Homotetramer
CC (PubMed:20693680). {ECO:0000269|PubMed:10387109,
CC ECO:0000269|PubMed:15886911, ECO:0000269|PubMed:20064618,
CC ECO:0000269|PubMed:20693680, ECO:0000269|PubMed:22922065}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10387109,
CC ECO:0000269|PubMed:2116592}.
CC -!- INDUCTION: Induced in the presence of choline, betaine, glycine betaine
CC or dimethylglycine (PubMed:2116592, PubMed:19103776, PubMed:20869215).
CC Induction is mediated by the transcriptional regulator GbdR
CC (PubMed:19103776, PubMed:20869215). The nitrogen regulatory protein
CC NtrC is necessary for full pchP expression (PubMed:20869215).
CC Expression is also partially dependent on the sigma-54 factor
CC (PubMed:20869215). Induced via GbdR in bovine lung surfactant and mouse
CC BALF (PubMed:19103776). {ECO:0000269|PubMed:19103776,
CC ECO:0000269|PubMed:20869215, ECO:0000269|PubMed:2116592}.
CC -!- DOMAIN: Folds into three structural domains: the first domain harbors
CC all the residues involved in catalysis, the second domain is
CC characteristic of PchP and is involved in the recognition of the
CC choline moiety of the substrate, the third domain stabilizes the
CC relative position of the other two (PubMed:22922065). Contains two
CC sites for alkylammonium compounds: one catalytic site near the metal
CC ion-phosphoester pocket and one inhibitory site (PubMed:21515416,
CC PubMed:21660097, PubMed:22922065). Sites are adjacent and share
CC residues (PubMed:21515416). Contains a high and a low affinity site for
CC phosphorylcholine (PubMed:10387109, PubMed:15886911). The signal
CC peptide is the fundamental factor responsible for decreasing the
CC affinity of the second site, and catalytic efficiency increases notably
CC after cleavage of the signal peptide (PubMed:17106798).
CC {ECO:0000269|PubMed:10387109, ECO:0000269|PubMed:15886911,
CC ECO:0000269|PubMed:17106798, ECO:0000269|PubMed:21515416,
CC ECO:0000269|PubMed:21660097, ECO:0000269|PubMed:22922065}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
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; AE004091; AAG08677.1; -; Genomic_DNA.
DR PIR; H82985; H82985.
DR RefSeq; NP_253979.1; NC_002516.2.
DR RefSeq; WP_003110458.1; NZ_QZGE01000020.1.
DR PDB; 4AS2; X-ray; 2.12 A; A/B/C/D=23-349.
DR PDB; 4AS3; X-ray; 2.40 A; A/B/C/D=23-349.
DR PDBsum; 4AS2; -.
DR PDBsum; 4AS3; -.
DR AlphaFoldDB; Q9HTR2; -.
DR SMR; Q9HTR2; -.
DR STRING; 287.DR97_2663; -.
DR PaxDb; Q9HTR2; -.
DR PRIDE; Q9HTR2; -.
DR DNASU; 877730; -.
DR EnsemblBacteria; AAG08677; AAG08677; PA5292.
DR GeneID; 877730; -.
DR KEGG; pae:PA5292; -.
DR PATRIC; fig|208964.12.peg.5546; -.
DR PseudoCAP; PA5292; -.
DR HOGENOM; CLU_062627_0_0_6; -.
DR InParanoid; Q9HTR2; -.
DR OMA; HLWINRK; -.
DR PhylomeDB; Q9HTR2; -.
DR BioCyc; PAER208964:G1FZ6-5413-MON; -.
DR BRENDA; 3.1.3.75; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Magnesium; Metal-binding;
KW Periplasm; Reference proteome; Signal; Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..349
FT /note="Phosphorylcholine phosphatase"
FT /id="PRO_5004328144"
FT ACT_SITE 53
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:18801468"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:18801468"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22922065,
FT ECO:0007744|PDB:4AS2, ECO:0007744|PDB:4AS3"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22922065,
FT ECO:0007744|PDB:4AS2, ECO:0007744|PDB:4AS3"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22922065,
FT ECO:0007744|PDB:4AS2, ECO:0007744|PDB:4AS3"
FT DISULFID 109..116
FT /evidence="ECO:0000269|PubMed:20064618,
FT ECO:0000269|PubMed:22922065, ECO:0007744|PDB:4AS2,
FT ECO:0007744|PDB:4AS3"
FT MUTAGEN 53..57
FT /note="DMDNT->AMANA: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17106798"
FT MUTAGEN 53..57
FT /note="DMDNT->EMENS: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17106798"
FT MUTAGEN 53
FT /note="D->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17106798,
FT ECO:0000269|PubMed:18801468"
FT MUTAGEN 55
FT /note="D->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17106798,
FT ECO:0000269|PubMed:18801468"
FT MUTAGEN 57
FT /note="T->S: Retains low activity with phosphorylcholine
FT and pNPP as substrates. Still activated by Mg(2+), Zn(2+)
FT or Cu(2+). Slight decrease in inhibition by
FT tetramethylammonium chloride."
FT /evidence="ECO:0000269|PubMed:17106798,
FT ECO:0000269|PubMed:18801468, ECO:0000269|PubMed:22922065"
FT MUTAGEN 64
FT /note="E->A: Shows half of the catalytic efficiency with
FT pNPP as substrate. Increases specific activity with
FT phosphorylcholine, but shows a 2-fold decrease in catalytic
FT efficiency. Decreases inhibition by high concentrations of
FT phosphorylcholine. 3-fold decrease in inhibition by
FT tetramethylammonium chloride."
FT /evidence="ECO:0000269|PubMed:21515416,
FT ECO:0000269|PubMed:22922065"
FT MUTAGEN 65
FT /note="E->A: 2.5-fold increase of the catalytic efficiency
FT with pNPP as substrate. Decreases catalytic efficiency with
FT phosphorylcholine. Insensitive to inhibition by high
FT concentrations of phosphorylcholine. 5-fold decrease in
FT inhibition by tetramethylammonium chloride."
FT /evidence="ECO:0000269|PubMed:21515416,
FT ECO:0000269|PubMed:22922065"
FT MUTAGEN 104..106
FT /note="YYY->AAA: Low catalytic efficiency with pNPP and
FT phosphorylcholine as substrates. Decreases inhibition by
FT high concentrations of phosphorylcholine. 4-fold decrease
FT in inhibition by tetramethylammonium chloride."
FT /evidence="ECO:0000269|PubMed:21515416,
FT ECO:0000269|PubMed:22922065"
FT MUTAGEN 109
FT /note="C->A: Slight decrease in inhibition by
FT tetramethylammonium chloride."
FT /evidence="ECO:0000269|PubMed:22922065"
FT MUTAGEN 188
FT /note="S->T: Strong decrease in activity with
FT phosphorylcholine and pNPP as substrates. Still activated
FT by Mg(2+), Zn(2+) or Cu(2+). Slight decrease in inhibition
FT by tetramethylammonium chloride."
FT /evidence="ECO:0000269|PubMed:17106798,
FT ECO:0000269|PubMed:18801468, ECO:0000269|PubMed:22922065"
FT MUTAGEN 264
FT /note="K->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17106798"
FT MUTAGEN 264
FT /note="K->R: Almost no change in activity. Slight decrease
FT in inhibition by tetramethylammonium chloride."
FT /evidence="ECO:0000269|PubMed:17106798,
FT ECO:0000269|PubMed:22922065"
FT MUTAGEN 283
FT /note="G->A: Decrease in activity with phosphorylcholine
FT and pNPP as substrates. Slight decrease in inhibition by
FT tetramethylammonium chloride."
FT /evidence="ECO:0000269|PubMed:17106798,
FT ECO:0000269|PubMed:22922065"
FT MUTAGEN 284
FT /note="D->E: Strong decrease in activity with
FT phosphorylcholine and pNPP as substrates. Still activated
FT by Mg(2+), Zn(2+) or Cu(2+). Slight decrease in inhibition
FT by tetramethylammonium chloride."
FT /evidence="ECO:0000269|PubMed:17106798,
FT ECO:0000269|PubMed:18801468, ECO:0000269|PubMed:22922065"
FT MUTAGEN 287
FT /note="D->E: Retains 65-70% of activity."
FT /evidence="ECO:0000269|PubMed:17106798"
FT MUTAGEN 289
FT /note="D->E: Retains 3% of activity. Still activated by
FT Mg(2+), Zn(2+) or Cu(2+). Slight decrease in inhibition by
FT tetramethylammonium chloride."
FT /evidence="ECO:0000269|PubMed:17106798,
FT ECO:0000269|PubMed:18801468, ECO:0000269|PubMed:22922065"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:4AS2"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:4AS2"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:4AS2"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:4AS2"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:4AS2"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:4AS2"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:4AS2"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:4AS2"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:4AS2"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:4AS2"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:4AS2"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:4AS2"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:4AS2"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 286..295
FT /evidence="ECO:0007829|PDB:4AS2"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 310..328
FT /evidence="ECO:0007829|PDB:4AS2"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:4AS2"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:4AS2"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:4AS2"
SQ SEQUENCE 349 AA; 39118 MW; 329D054C338F232F CRC64;
MTFAKGILAA LALAAAVGQA SATELEHWPA PAARQLNALI EANANKGAYA VFDMDNTSYR
YDLEESLLPY LEMKGVLTRD RLDPSLKLIP FKDQAGHKES LFSYYYRLCE IDDMVCYPWV
AQVFSGFTLR ELKGYVDELM AYGKPIPATY YDGDKLATLD VEPPRVFSGQ RELYNKLMEN
GIEVYVISAA HEELVRMVAA DPRYGYNAKP ENVIGVTTLL KNRKTGELTT ARKQIAEGKY
DPKANLDLEV TPYLWTPATW MAGKQAAILT YIDRWKRPIL VAGDTPDSDG YMLFNGTAEN
GVHLWVNRKA KYMEQINGMI KQHSAAQAKA GLPVTADRNW VIVTPEQIQ
