HAMAP rule MF_01375
General rule information
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Accession | MF_01375 |
Dates | 29-MAR-2007 (Created) 26-JAN-2023 (Last updated, Version 24) |
Name | PhnX |
Scope | Bacteria; Bacteroidota
Bacteria; Bacillota
Bacteria; Pseudomonadota |
Templates | O31156 (PHNX_BACCE); Q7ZAP3 (PHNX_SALTY): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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Comments
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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
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case <FT:3> or <FT:4> or <FT:5>
end case
case <FT:2>
end case
Gene Ontology
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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
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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
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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 | ||||||||
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
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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). |