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Annotation rule MF_01375 |
General rule information
[?]
Accession |
MF_01375 |
Dates |
29-MAR-2007 (Created) 19-NOV-2019 (Last updated, Version 19) |
Scope |
Bacteria; Bacteroidetes
Bacteria; Firmicutes
Bacteria; Proteobacteria |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Protein name |
RecName:
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Full=Phosphonoacetaldehyde hydrolase;
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Short=Phosphonatase;
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EC 3.11.1.1;
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AltName:
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Full=Phosphonoacetaldehyde phosphonohydrolase;
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Function |
Involved in phosphonate degradation. |
Catalytic activity |
RHEA:18905: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
EC 3.11.1.1
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Cofactor |
Mg(2+) Note: Binds 1 Mg(2+) ion per subunit. |
Subunit |
Homodimer. |
Similarity |
Belongs to the HAD-like hydrolase superfamily. PhnX family. |
case <FT:3> or <FT:4> or <FT:5>
end case
case <FT:2>
end case
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
From: PHNX_BACCE (O31156) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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ACT_SITE
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9
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9
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Nucleophile
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D
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ACT_SITE
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50
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50
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Schiff-base intermediate with substrate
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K
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METAL
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9
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9
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Magnesium
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D
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METAL
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11
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11
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Magnesium; via carbonyl oxygen
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A
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METAL
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183
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183
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Magnesium
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D
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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). |