ID   PHNX_PSEA8              Reviewed;         275 AA.
AC   B7UVR5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Phosphonoacetaldehyde hydrolase {ECO:0000255|HAMAP-Rule:MF_01375};
DE            Short=Phosphonatase {ECO:0000255|HAMAP-Rule:MF_01375};
DE            EC=3.11.1.1 {ECO:0000255|HAMAP-Rule:MF_01375};
DE   AltName: Full=Phosphonoacetaldehyde phosphonohydrolase {ECO:0000255|HAMAP-Rule:MF_01375};
GN   Name=phnX {ECO:0000255|HAMAP-Rule:MF_01375}; OrderedLocusNames=PLES_38711;
OS   Pseudomonas aeruginosa (strain LESB58).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=557722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LESB58;
RX   PubMed=19047519; DOI=10.1101/gr.086082.108;
RA   Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA   Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA   Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA   Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT   "Newly introduced genomic prophage islands are critical determinants of in
RT   vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT   aeruginosa.";
RL   Genome Res. 19:12-23(2009).
CC   -!- FUNCTION: Involved in phosphonate degradation. {ECO:0000255|HAMAP-
CC       Rule:MF_01375}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate;
CC         Xref=Rhea:RHEA:18905, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58383; EC=3.11.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01375};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01375};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01375};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01375}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PhnX family.
CC       {ECO:0000255|HAMAP-Rule:MF_01375}.
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DR   EMBL; FM209186; CAW28598.1; -; Genomic_DNA.
DR   RefSeq; WP_012614330.1; NC_011770.1.
DR   AlphaFoldDB; B7UVR5; -.
DR   SMR; B7UVR5; -.
DR   KEGG; pag:PLES_38711; -.
DR   HOGENOM; CLU_045011_12_0_6; -.
DR   OMA; TWPGILE; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050194; F:phosphonoacetaldehyde hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019700; P:organic phosphonate catabolic process; IEA:InterPro.
DR   CDD; cd02586; HAD_PHN; 1.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_01375; PhnX; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR006323; Phosphonoacetald_hydro.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR   TIGRFAMs; TIGR01422; phosphonatase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Schiff base.
FT   CHAIN           1..275
FT                   /note="Phosphonoacetaldehyde hydrolase"
FT                   /id="PRO_1000144834"
FT   ACT_SITE        15
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   ACT_SITE        56
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         15
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         189
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
SQ   SEQUENCE   275 AA;  29915 MW;  17043EE9E4A3EE9D CRC64;
     MNYNQPATLQ AAILDWAGTV VDFGSFAPTQ IFVEAFAEFG VQVSLEEARG PMGMGKWDHI
     RTLCDIPAIA ERYRAVFGRL PSDDDVTAIY ERFMPLQIEK IAEHSAVIPG ALQAIAELRG
     MGLKIGSCSG YPAVVMEKVV ALAETNGYVA DHVVATDEVP NGRPWPAQAL ANVIALGIDD
     VAACVKVDDT WPGILEGRRA GMWTVALTCS GNALGLTYEQ YKALPAAELE RERTRIEQMF
     EGSRPHYLIE TIAELPAVVR DINARLARGE MPQGN