ID   PHNX_AERHH              Reviewed;         279 AA.
AC   A0KJM0;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 100.
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};
GN   OrderedLocusNames=AHA_1940;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC   KCTC 2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000462; ABK38391.1; -; Genomic_DNA.
DR   RefSeq; WP_011705810.1; NC_008570.1.
DR   RefSeq; YP_856471.1; NC_008570.1.
DR   AlphaFoldDB; A0KJM0; -.
DR   SMR; A0KJM0; -.
DR   STRING; 380703.AHA_1940; -.
DR   EnsemblBacteria; ABK38391; ABK38391; AHA_1940.
DR   KEGG; aha:AHA_1940; -.
DR   PATRIC; fig|380703.7.peg.1955; -.
DR   eggNOG; COG0637; Bacteria.
DR   HOGENOM; CLU_045011_12_0_6; -.
DR   OrthoDB; 5504491at2; -.
DR   Proteomes; UP000000756; 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; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR   NCBIfam; TIGR01422; phosphonatase; 1.
DR   PANTHER; PTHR43434; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR   PANTHER; PTHR43434:SF26; PHOSPHONOACETALDEHYDE HYDROLASE; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR   SFLD; SFLDF00038; phosphonoacetaldehyde_hydrolas; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome; Schiff base.
FT   CHAIN           1..279
FT                   /note="Phosphonoacetaldehyde hydrolase"
FT                   /id="PRO_0000284573"
FT   ACT_SITE        20
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   ACT_SITE        62
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         20
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         22
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         196
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
SQ   SEQUENCE   279 AA;  29882 MW;  5599F76509E3D2AF CRC64;
     MTDLQIAVDP TTDVEALILD WAGTVVDFGS FAPTSIFVEA FARAYDFPVT LDEARQPMGL
     GKWDHIAALG RLPSVDARWQ ARFGHPMSHA EVDHLYHTFM PLQIAAVTRF ADPIPGVLPV
     LDALRGQGMK IGSCSGYPRP VMETLVPAAA DHGYRPDHWV ATDDLKAGGR PGPWMALANV
     IELGVNAVHR CIKVDDAVPG ISEGLNAGMW TVGLSVSGNE FGATWEAFAA MSEAEIAARR
     APAEAKLRAA GAHYVIDTLA DIAPVIADIN RRLAAGERP
//