Due to maintenance work, this service will be unavailable from
Mon Nov 11 17:30 until
Tue Nov 12 09:00
CET.
Apologies for the inconvenience.
HAMAP rule MF_01375
General rule information
[?]
| Accession | MF_01375 |
| Dates | 29-MAR-2007 (Created)
1-JUN-2023 (Last updated, Version 25) |
| Name | PhnX |
| Scope(s) |
Bacteria Bacteroidota Bacillota Pseudomonadota |
| Template(s) | O31156 (PHNX_BACCE); Q7ZAP3 (PHNX_SALTY); [ Recover all ] |
| Triggered by |
HAMAP; MF_01375 (Get profile general information and statistics) |
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 | Name=phnX; |
Comments
[?]
| FUNCTION | Involved in phosphonate degradation. |
| CATALYTIC ACTIVITY | Reaction=H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate; Xref=Rhea:RHEA:18905, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58383; EC=3.11.1.1; |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; |
| SUBUNIT | Homodimer. |
| SIMILARITY | Belongs to the HAD-like hydrolase superfamily. PhnX family. |
Keywords
[?]
| Hydrolase | |
| case <FT:3> or <FT:4> or <FT:5> | |
| Magnesium | |
| Metal-binding | |
| end case | |
| case <FT:2> | |
| Schiff base | |
| 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; |
| NCBIfam | TIGR01549; HAD-SF-IA-v1; 1; |
| NCBIfam | TIGR01422; Phosphonatase; 1; |
| NCBIfam | TIGR01509; HAD-SF-IA-v3; 1; |
Features
[?]
| From: PHNX_BACCE (O31156) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 9 | 9 | /note="Nucleophile" | D | ||||||||
| ACT_SITE | 50 | 50 | /note="Schiff-base intermediate with substrate" | K | ||||||||
| BINDING | 9 | 9 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
D | ||||||||
| BINDING | 11 | 11 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
A | ||||||||
| BINDING | 183 | 183 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
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). |