ID   PHNX_BACCR              Reviewed;         264 AA.
AC   Q81G82;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 112.
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=BC_1326;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP08309.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={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; AE016877; AAP08309.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_831108.1; NC_004722.1.
DR   AlphaFoldDB; Q81G82; -.
DR   SMR; Q81G82; -.
DR   STRING; 226900.BC_1326; -.
DR   EnsemblBacteria; AAP08309; AAP08309; BC_1326.
DR   KEGG; bce:BC1326; -.
DR   PATRIC; fig|226900.8.peg.1299; -.
DR   HOGENOM; CLU_045011_12_0_9; -.
DR   OMA; GRPAPWM; -.
DR   Proteomes; UP000001417; 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; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR006323; Phosphonoacetald_hydro.
DR   Pfam; PF13419; HAD_2; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR   TIGRFAMs; TIGR01422; phosphonatase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome; Schiff base.
FT   CHAIN           1..264
FT                   /note="Phosphonoacetaldehyde hydrolase"
FT                   /id="PRO_0000284577"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   ACT_SITE        50
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01375"
SQ   SEQUENCE   264 AA;  29995 MW;  116B57D980DBEF70 CRC64;
     MKIEAVIFDW AGTTVDYGCF APLEVFMKIF QKRGVEITAE EARKPMGLLK IDHVRALTEM
     PRIADEWKRV FGQLPTEADI HEMYEEFEEI LFSILPSYAT PIDGVKEVIA SLRERGIKIG
     STTGYTREMM EIVAKEAALQ GYKPDFLVTP DDVPAGRPYP WMCYKNAMEL GVYPMNHMIK
     VGDTVSDMKE GRNAGMWTVG VILGSSELGL TQYEVESMDS VELREKIEIV RNRFAENGAH
     STIETMQELE NVMEHIEKQE LIIS