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beta-lactamase hydrolase domain-containing protein
This domain, once called DUF442, is found as the N-terminal region, a sulfur transferase domain, of the bifunctional protein Blh (from the former name beta-lactamase-like hydrolase). The longer C-terminal domain of Blh is a sulfur dioxygenase domain. An earlier study on the uncharacterized protein NMA1982 showed a structure similar to protein tyrosine phosphatases, and reportedly some activity was detected on the test substrate p-nitrophenyl phosphate. Consequently, proteins annotated by this HMM and the related HMM TIGR01244 have been annotated as phosphatases.
MBL fold metallo-hydrolase
bifunctional sulfur transferase/dioxygenase Blh
TIGR01244 family sulfur transferase
Members of this family include NMA1982 from Neisseria meningitidis, which originally was called a phosphatase based on a fold similar to protein-tyrosine phosphatases and reportedly some activity on the phosphatase test substrate p-nitrophenyl phosphate. However, more recent work on the protein Blh from the plant pathogen Xylella fastidiosa showed that the N-terminal domain, covered by this HMM and by PF04273 (previously DUF442), acts as a sulfur transferase. The C-terminal domain of Blh (beta-lactamase-like hydrolase), with a metallo-beta-lactamase fold, was shown to act as a sulfur dioxygenase. The more recent work makes it seem likely that previous annotations of suggesting classification of member proteins as phosphatases were incorrect.
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