acid phosphatase AphA [Sneathia vaginalis]
Protein Classification
AphA family protein( domain architecture ID 10007848)
AphA family protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| AphA | COG3700 | Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction ... |
16-239 | 6.91e-133 | ||||
Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction only]; : Pssm-ID: 442914 Cd Length: 237 Bit Score: 373.95 E-value: 6.91e-133
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| Name | Accession | Description | Interval | E-value | ||||
| AphA | COG3700 | Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction ... |
16-239 | 6.91e-133 | ||||
Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction only]; Pssm-ID: 442914 Cd Length: 237 Bit Score: 373.95 E-value: 6.91e-133
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| AphA | TIGR01672 | HAD superfamily (subfamily IIIB) phosphatase, TIGR01672; This family of proteins is a member ... |
16-239 | 2.02e-89 | ||||
HAD superfamily (subfamily IIIB) phosphatase, TIGR01672; This family of proteins is a member of the IIIB subfamily (pfam02767) of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of subfamily III and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. The AphA gene from E. coli has been characterized and shown to be an active phosphatase enzyme. This family has been previously described as the "class B non-specific bacterial acid phosphatase" (B-NSAP) family, where it is noted that the enzyme is secreted and has a broad substrate range. The possibility exists, however, that the enzyme is specific for an as yet undefined substrate. Supporting evidence for the inclusion in the HAD superfamily, whose phosphatase members are magnesium dependent, is the inhibition by EDTA and calcium ions, and stimulation by magnesium ion. Pssm-ID: 273747 Cd Length: 237 Bit Score: 263.70 E-value: 2.02e-89
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| HAD_CBAP | cd07499 | molecular class B acid phosphatases, similar to Escherichia coli AphA; class B acid ... |
44-239 | 5.23e-82 | ||||
molecular class B acid phosphatases, similar to Escherichia coli AphA; class B acid phosphatases (CBAPs) have been detected in a minority of bacterial species which include a number of major pathogens such as Escherichia coli, Haemophilus influenzae, and Streptococcus pyogenes. This family includes the CBAP Escherichia coli AphA. The purified enzyme is a broad-spectrum nucleotidase highly active against both 3'- and 5'-mononucleotides and monodeoxynucleotides, which can also act as a phosphotransferase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319802 Cd Length: 185 Bit Score: 243.09 E-value: 5.23e-82
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| Acid_phosphat_B | pfam03767 | HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ... |
30-213 | 1.16e-14 | ||||
HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid phosphatases and a number of vegetative storage proteins. Pssm-ID: 397712 Cd Length: 213 Bit Score: 70.47 E-value: 1.16e-14
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| Name | Accession | Description | Interval | E-value | ||||
| AphA | COG3700 | Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction ... |
16-239 | 6.91e-133 | ||||
Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction only]; Pssm-ID: 442914 Cd Length: 237 Bit Score: 373.95 E-value: 6.91e-133
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| AphA | TIGR01672 | HAD superfamily (subfamily IIIB) phosphatase, TIGR01672; This family of proteins is a member ... |
16-239 | 2.02e-89 | ||||
HAD superfamily (subfamily IIIB) phosphatase, TIGR01672; This family of proteins is a member of the IIIB subfamily (pfam02767) of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of subfamily III and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. The AphA gene from E. coli has been characterized and shown to be an active phosphatase enzyme. This family has been previously described as the "class B non-specific bacterial acid phosphatase" (B-NSAP) family, where it is noted that the enzyme is secreted and has a broad substrate range. The possibility exists, however, that the enzyme is specific for an as yet undefined substrate. Supporting evidence for the inclusion in the HAD superfamily, whose phosphatase members are magnesium dependent, is the inhibition by EDTA and calcium ions, and stimulation by magnesium ion. Pssm-ID: 273747 Cd Length: 237 Bit Score: 263.70 E-value: 2.02e-89
|
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| HAD_CBAP | cd07499 | molecular class B acid phosphatases, similar to Escherichia coli AphA; class B acid ... |
44-239 | 5.23e-82 | ||||
molecular class B acid phosphatases, similar to Escherichia coli AphA; class B acid phosphatases (CBAPs) have been detected in a minority of bacterial species which include a number of major pathogens such as Escherichia coli, Haemophilus influenzae, and Streptococcus pyogenes. This family includes the CBAP Escherichia coli AphA. The purified enzyme is a broad-spectrum nucleotidase highly active against both 3'- and 5'-mononucleotides and monodeoxynucleotides, which can also act as a phosphotransferase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319802 Cd Length: 185 Bit Score: 243.09 E-value: 5.23e-82
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| Acid_phosphat_B | pfam03767 | HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ... |
30-213 | 1.16e-14 | ||||
HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid phosphatases and a number of vegetative storage proteins. Pssm-ID: 397712 Cd Length: 213 Bit Score: 70.47 E-value: 1.16e-14
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| HAD_like | cd01427 | Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ... |
115-213 | 1.50e-07 | ||||
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319763 [Multi-domain] Cd Length: 106 Bit Score: 48.55 E-value: 1.50e-07
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| HAD-SF-IA-v1 | TIGR01549 | haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ... |
59-207 | 5.04e-05 | ||||
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 273686 [Multi-domain] Cd Length: 164 Bit Score: 42.38 E-value: 5.04e-05
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