ID   PHNX_SALPB              Reviewed;         269 AA.
AC   A9MWZ8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=SPAB_03150;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX68511.1; -; Genomic_DNA.
DR   RefSeq; WP_012219071.1; NC_010102.1.
DR   AlphaFoldDB; A9MWZ8; -.
DR   SMR; A9MWZ8; -.
DR   KEGG; spq:SPAB_03150; -.
DR   PATRIC; fig|1016998.12.peg.2972; -.
DR   HOGENOM; CLU_045011_12_0_6; -.
DR   OMA; GRPAPWM; -.
DR   BioCyc; SENT1016998:SPAB_RS12860-MON; -.
DR   Proteomes; UP000008556; 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_1000144842"
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;  28718 MW;  D453B381124A3991 CRC64;
     MNRIHAVILD WAGTTVDFGS FAPTQIFVEA FRQAFDVEIT LAEARVPMGL GKWQHIEALG
     KLPAVDARWQ AKFGRSMSAA DIDAIYAAFM PLQIAKVVDF SSPIAGVIDT IAALRAEGIK
     IGSCSGYPRA VMERLVPAAA EHGYRPDHWV ATDDLAAGGR PGPWMALQNV IALGIDAVAH
     CVKVDDAAPG ISEGLNAGMW TVGLAVSGNE FGATWDAYQT MSKEDVAVRR EHAASKLYAA
     GAHYVVDSLA DLPEVIAHIN ARLAQGERP