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Annotation rule MF_01375
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General rule information [?]

Accession MF_01375
Dates 29-MAR-2007 (Created)
19-NOV-2019 (Last updated, Version 19)
Name PhnX
Scope
Bacteria; Bacteroidetes
Bacteria; Firmicutes
Bacteria; Proteobacteria
Templates O31156 (PHNX_BACCE); Q7ZAP3 (PHNX_SALTY): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
PHNX
Protein name
RecName: Full=Phosphonoacetaldehyde hydrolase;
Short=Phosphonatase;
EC 3.11.1.1;
AltName: Full=Phosphonoacetaldehyde phosphonohydrolase;
Gene name
phnX

Comments [?]

Function Involved in phosphonate degradation.
Catalytic activity RHEA:18905: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
EC 3.11.1.1
Cofactor Mg(2+)
Note: Binds 1 Mg(2+) ion per subunit.
Subunit Homodimer.
Similarity Belongs to the HAD-like hydrolase superfamily. PhnX family.

Keywords [?]

case <FT:3> or <FT:4> or <FT:5>
end case
case <FT:2>
end case

Gene Ontology [?]

GO:0050194; Molecular function: phosphonoacetaldehyde hydrolase activity.
case <FT:3> or <FT:4> or <FT:5>
GO:0000287; Molecular function: magnesium ion binding.
end case

Cross-references [?]

Pfam PF00702; Hydrolase; 1;
PRINTS PR00413; HADHALOGNASE; 1;
TIGRFAMs TIGR01549; HAD-SF-IA-v1; 1;
TIGR01422; Phosphonatase; 1;
TIGR01509; HAD-SF-IA-v3; 1;

Features [?]

From: PHNX_BACCE (O31156)
Key     From     To       Description   Tag   Condition   FTGroup
ACT_SITE     9     9       Nucleophile     D  
ACT_SITE     50     50       Schiff-base intermediate with substrate     K  
METAL     9     9       Magnesium     D  
METAL     11     11       Magnesium; via carbonyl oxygen     A  
METAL     183     183       Magnesium     D  

Additional information [?]

Size range 263-295 amino acids
Related rules None
Fusion Nter: None; Cter: MF_01376 (phnW)
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).