MULTISPECIES: acid phosphatase AphA [Klebsiella]
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 ... |
1-237 | 5.98e-179 | ||||
Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction only]; : Pssm-ID: 442914 Cd Length: 237 Bit Score: 490.28 E-value: 5.98e-179
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| Name | Accession | Description | Interval | E-value | ||||
| AphA | COG3700 | Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction ... |
1-237 | 5.98e-179 | ||||
Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction only]; Pssm-ID: 442914 Cd Length: 237 Bit Score: 490.28 E-value: 5.98e-179
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| AphA | TIGR01672 | HAD superfamily (subfamily IIIB) phosphatase, TIGR01672; This family of proteins is a member ... |
1-237 | 8.69e-141 | ||||
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: 393.90 E-value: 8.69e-141
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| HAD_CBAP | cd07499 | molecular class B acid phosphatases, similar to Escherichia coli AphA; class B acid ... |
51-237 | 1.79e-124 | ||||
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: 350.57 E-value: 1.79e-124
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| Acid_phosphat_B | pfam03767 | HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ... |
51-221 | 9.42e-34 | ||||
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: 120.55 E-value: 9.42e-34
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| Name | Accession | Description | Interval | E-value | ||||
| AphA | COG3700 | Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction ... |
1-237 | 5.98e-179 | ||||
Acid phosphatase, class B [Inorganic ion transport and metabolism, General function prediction only]; Pssm-ID: 442914 Cd Length: 237 Bit Score: 490.28 E-value: 5.98e-179
|
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| AphA | TIGR01672 | HAD superfamily (subfamily IIIB) phosphatase, TIGR01672; This family of proteins is a member ... |
1-237 | 8.69e-141 | ||||
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: 393.90 E-value: 8.69e-141
|
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| HAD_CBAP | cd07499 | molecular class B acid phosphatases, similar to Escherichia coli AphA; class B acid ... |
51-237 | 1.79e-124 | ||||
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: 350.57 E-value: 1.79e-124
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| Acid_phosphat_B | pfam03767 | HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ... |
51-221 | 9.42e-34 | ||||
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: 120.55 E-value: 9.42e-34
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| HAD_like | cd01427 | Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ... |
118-210 | 1.61e-06 | ||||
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: 45.46 E-value: 1.61e-06
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| HAD_CAP | cd07534 | molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; ... |
32-200 | 4.07e-05 | ||||
molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; belongs to the haloacid dehalogenase-like hydrolase superfamily; Molecular class C acid phosphatases (CAPs) are nonspecific acid phosphatases with generally broad substrate specificity and optimum activity at neutral to acidic pH. Members include Haemophilus influenzae lipoprotein e (P4), Elizabethkingia meningosepticum OlpA, Helicobacter pylori HppA, Enterobacter sp. 4 acid phosphatase PhoI, and Streptococcus pyogenes M1 GAS LppC. Lipoprotein e (P4) exhibits phosphomonoesterase activity with aryl phosphate substrates including nicotinamide mononucleotide (NMN), tyrosine phosphate, phenyl phosphate, p-nitrophenyl phosphate, and 4-methylumbelliferyl phosphate. The role of P4 in NAD+ uptake appears to be the dephosphorylation of NMN to nicotinamide riboside, which is then taken up by the organism. Elizabethkingia meningosepticum OlpA is a broad-spectrum nucleotidase with preference for 5'-nucleotides, it efficiently hydrolyzes nucleotide monophosphates, with a strong preference for 5'-nucleotides and for 3'-AMP; OlpA can also hydrolyze sugar phosphates and beta-glycerol phosphate, although with a lower efficiency. Helicobacter pylori HppA is also a 5' nucleotidase. Members of this family belong 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: 319836 [Multi-domain] Cd Length: 196 Bit Score: 43.09 E-value: 4.07e-05
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| Hydrolase | pfam00702 | haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ... |
65-204 | 3.45e-03 | ||||
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria. Pssm-ID: 459910 [Multi-domain] Cd Length: 191 Bit Score: 37.18 E-value: 3.45e-03
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| COG2503 | COG2503 | Predicted secreted acid phosphatase [General function prediction only]; |
1-200 | 5.03e-03 | ||||
Predicted secreted acid phosphatase [General function prediction only]; Pssm-ID: 441997 [Multi-domain] Cd Length: 269 Bit Score: 37.25 E-value: 5.03e-03
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| Blast search parameters | ||||
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