Members of a new molecular family of bacterial nonspecific acid phosphatases (NSAPs), indicated as class C, were found to share significant sequence similarities to bacterial class B NSAPs and to some plant acid phosphatases, representing the first example of a family of bacterial NSAPs that has a relatively close eukaryotic counterpart. Despite the lack of an overall similarity, conserved sequence motifs were also identified among the above enzyme families (class B and class C bacterial NSAPs, and related plant phosphatases) and several other families of phosphohydrolases, including bacterial phosphoglycolate phosphatases, histidinol-phosphatase domains of the bacterial bifunctional enzymes imidazole-glycerolphosphate dehydratases, and bacterial, eukaryotic, and archaeal phosphoserine phosphatases and threalose-6-phosphatases. These conserved motifs are clustered within two domains, separated by a variable spacer region, according to the pattern [FILMAVT]-D-[ILFRMVY]-D-[GSNDE]-[TV]-[ILVAM]- [ATSVILMC]-X-{YFWHKR}-X-{YFWHNQ}-X(102, 191)- {KRHNQ}-G-D-{FYWHILVMC}-{QNH}-{FWYGP}-D- {PSNQYW}. The dephosphorylating activity common to all these proteins supports the definition of this phosphatase motif and the inclusion of these enzymes into a superfamily of phosphohydrolases that we propose to indicate as "DDDD" after the presence of the four invariant aspartate residues. Database searches retrieved various hypothetical proteins of unknown function containing this or similar motifs, far which a phosphohydrolase activity could be hypothesized.

Conserved sequence motifs among bacterial, eukaryotic, and archaeal phosphatases that define a new phosphohydrolase superfamily / Maria Cristina, Thaller; Schippa, Serena; Gian Maria, Rossolini. - In: PROTEIN SCIENCE. - ISSN 0961-8368. - 7:7(1998), pp. 1647-1652. [10.1002/pro.5560070722]

Conserved sequence motifs among bacterial, eukaryotic, and archaeal phosphatases that define a new phosphohydrolase superfamily

SCHIPPA, Serena;
1998

Abstract

Members of a new molecular family of bacterial nonspecific acid phosphatases (NSAPs), indicated as class C, were found to share significant sequence similarities to bacterial class B NSAPs and to some plant acid phosphatases, representing the first example of a family of bacterial NSAPs that has a relatively close eukaryotic counterpart. Despite the lack of an overall similarity, conserved sequence motifs were also identified among the above enzyme families (class B and class C bacterial NSAPs, and related plant phosphatases) and several other families of phosphohydrolases, including bacterial phosphoglycolate phosphatases, histidinol-phosphatase domains of the bacterial bifunctional enzymes imidazole-glycerolphosphate dehydratases, and bacterial, eukaryotic, and archaeal phosphoserine phosphatases and threalose-6-phosphatases. These conserved motifs are clustered within two domains, separated by a variable spacer region, according to the pattern [FILMAVT]-D-[ILFRMVY]-D-[GSNDE]-[TV]-[ILVAM]- [ATSVILMC]-X-{YFWHKR}-X-{YFWHNQ}-X(102, 191)- {KRHNQ}-G-D-{FYWHILVMC}-{QNH}-{FWYGP}-D- {PSNQYW}. The dephosphorylating activity common to all these proteins supports the definition of this phosphatase motif and the inclusion of these enzymes into a superfamily of phosphohydrolases that we propose to indicate as "DDDD" after the presence of the four invariant aspartate residues. Database searches retrieved various hypothetical proteins of unknown function containing this or similar motifs, far which a phosphohydrolase activity could be hypothesized.
1998
acid phosphatase; homology; molecular family; molecular superfamily; phosphatase; sequence motif
01 Pubblicazione su rivista::01a Articolo in rivista
Conserved sequence motifs among bacterial, eukaryotic, and archaeal phosphatases that define a new phosphohydrolase superfamily / Maria Cristina, Thaller; Schippa, Serena; Gian Maria, Rossolini. - In: PROTEIN SCIENCE. - ISSN 0961-8368. - 7:7(1998), pp. 1647-1652. [10.1002/pro.5560070722]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/121573
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