ID   PHNX_SALPA              Reviewed;         269 AA.
AC   Q5PFR1;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=SPA2291;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78176.1; -; Genomic_DNA.
DR   RefSeq; WP_011233114.1; NC_006511.1.
DR   AlphaFoldDB; Q5PFR1; -.
DR   SMR; Q5PFR1; -.
DR   EnsemblBacteria; AAV78176; AAV78176; SPA2291.
DR   KEGG; spt:SPA2291; -.
DR   HOGENOM; CLU_045011_12_0_6; -.
DR   OMA; GRPAPWM; -.
DR   Proteomes; UP000008185; Chromosome.
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..269
FT                   /note="Phosphonoacetaldehyde hydrolase"
FT                   /id="PRO_0000284599"
FT   ACT_SITE        10
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   ACT_SITE        52
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
SQ   SEQUENCE   269 AA;  28535 MW;  7EFD158967B903B2 CRC64;
     MNRIHAVILD WAGTTVDFGS FAPTQIFVEA FRQAFDVEIT LAEARVPMGL GKWQHIEALG
     KLPAVDARWQ AKFGRAMSAA DIDAIYAAFM PLQIAKVVDF SSPIAGVIDT IATLRAEGIK
     IGSCSGYPRA VMERLVPAAA GHGYCPDHWV ATDDLAAGGR PGPWMALQNV IALGIDAVAH
     CVKVDDAAPG ISEGLNAGMW TVGLAVSGNE FGATWDAYQT MSKEDVAVRR EHAASKLYAA
     GAHYVVDSLA DLPGVIAHIN ARLAQGERP