AC   MF_01375;
DC   Protein; auto
TR   HAMAP; MF_01375; -; 1; level=0
XX
Names: PhnX
XX
ID   PHNX
DE   RecName: Full=Phosphonoacetaldehyde hydrolase;
DE            Short=Phosphonatase;
DE            EC=3.11.1.1;
DE   AltName: Full=Phosphonoacetaldehyde phosphonohydrolase;
GN   Name=phnX;
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CC   -!- FUNCTION: Involved in phosphonate degradation.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PhnX family.
XX
DR   Pfam; PF00702; Hydrolase; 1; trigger=no
DR   PRINTS; PR00413; HADHALOGNASE; 1; trigger=no
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1; trigger=no
DR   NCBIfam; TIGR01422; Phosphonatase; 1; trigger=no
DR   NCBIfam; TIGR01509; HAD-SF-IA-v3; 1; trigger=no
XX
KW   Hydrolase
case <FT:3> or <FT:4> or <FT:5>
KW   Magnesium
KW   Metal-binding
end case
case <FT:2>
KW   Schiff base
end case
XX
GO   GO:0050194; F:phosphonoacetaldehyde hydrolase activity
case <FT:3> or <FT:4> or <FT:5>
GO   GO:0000287; F:magnesium ion binding
end case
XX
FT   From: PHNX_BACCE (O31156)
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT   Condition: D
FT   ACT_SITE        50
FT                   /note="Schiff-base intermediate with substrate"
FT   Condition: K
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: A
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
XX
Size: 263-295;
Related: None;
Template: O31156; Q7ZAP3;
Scope:
 Bacteria; Bacteroidota
 Bacteria; Bacillota
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: MF_01376 (phnW)
Duplicate: in SYNFM
Plasmid: None
Comments: In PHNXL_SYNFM (A0LJ16), the conserved Lys that has been shown
 to form a Schiff base with the substrate is an Arg, a mutation which
 completely inactivates the enzyme in Bacillus cereus. This entry is
 therefore annotated as atypical.
 Fused with 2-aminoethylphosphonate--pyruvate transaminase (phnW) in CLOD6.
 For a discussion of phosphonate degradation pathways see:
 PubMed=16245012; DOI=10.1007/s00239-004-0349-4;
 Huang J., Su Z., Xu Y.;
 "The evolution of microbial phosphonate degradative pathways.";
 J. Mol. Evol. 61:682-690(2005).
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# Revision 1.25 2023/06/01
//