MULTISPECIES: pyridoxal phosphatase [Yersinia pseudotuberculosis complex]
Protein Classification
HAD family hydrolase( domain architecture ID 11484771)
The HAD (haloacid dehalogenase) family of hydrolase includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PRK10530 | PRK10530 | pyridoxal phosphate (PLP) phosphatase; Provisional |
1-272 | 0e+00 | |||||
pyridoxal phosphate (PLP) phosphatase; Provisional : Pssm-ID: 182523 [Multi-domain] Cd Length: 272 Bit Score: 590.07 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| PRK10530 | PRK10530 | pyridoxal phosphate (PLP) phosphatase; Provisional |
1-272 | 0e+00 | |||||
pyridoxal phosphate (PLP) phosphatase; Provisional Pssm-ID: 182523 [Multi-domain] Cd Length: 272 Bit Score: 590.07 E-value: 0e+00
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| HAD_Pase | cd07516 | phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ... |
5-269 | 1.30e-79 | |||||
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. 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: 319818 [Multi-domain] Cd Length: 253 Bit Score: 240.57 E-value: 1.30e-79
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| Cof-subfamily | TIGR00099 | Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ... |
5-267 | 2.64e-74 | |||||
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 272905 [Multi-domain] Cd Length: 256 Bit Score: 227.54 E-value: 2.64e-74
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| Hydrolase_3 | pfam08282 | haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ... |
6-267 | 8.08e-74 | |||||
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes. Pssm-ID: 429897 [Multi-domain] Cd Length: 255 Bit Score: 225.97 E-value: 8.08e-74
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| Cof | COG0561 | Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ... |
2-270 | 9.67e-69 | |||||
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only]; Pssm-ID: 440327 [Multi-domain] Cd Length: 192 Bit Score: 210.76 E-value: 9.67e-69
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| Name | Accession | Description | Interval | E-value | |||||
| PRK10530 | PRK10530 | pyridoxal phosphate (PLP) phosphatase; Provisional |
1-272 | 0e+00 | |||||
pyridoxal phosphate (PLP) phosphatase; Provisional Pssm-ID: 182523 [Multi-domain] Cd Length: 272 Bit Score: 590.07 E-value: 0e+00
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| HAD_Pase | cd07516 | phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ... |
5-269 | 1.30e-79 | |||||
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. 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: 319818 [Multi-domain] Cd Length: 253 Bit Score: 240.57 E-value: 1.30e-79
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| Cof-subfamily | TIGR00099 | Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ... |
5-267 | 2.64e-74 | |||||
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 272905 [Multi-domain] Cd Length: 256 Bit Score: 227.54 E-value: 2.64e-74
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| Hydrolase_3 | pfam08282 | haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ... |
6-267 | 8.08e-74 | |||||
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes. Pssm-ID: 429897 [Multi-domain] Cd Length: 255 Bit Score: 225.97 E-value: 8.08e-74
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| Cof | COG0561 | Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ... |
2-270 | 9.67e-69 | |||||
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only]; Pssm-ID: 440327 [Multi-domain] Cd Length: 192 Bit Score: 210.76 E-value: 9.67e-69
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| HAD_HPP | cd07517 | phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ... |
4-264 | 7.99e-40 | |||||
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. 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: 319819 [Multi-domain] Cd Length: 213 Bit Score: 137.35 E-value: 7.99e-40
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| PRK10513 | PRK10513 | sugar phosphate phosphatase; Provisional |
1-272 | 9.01e-31 | |||||
sugar phosphate phosphatase; Provisional Pssm-ID: 182509 [Multi-domain] Cd Length: 270 Bit Score: 115.56 E-value: 9.01e-31
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| PRK15126 | PRK15126 | HMP-PP phosphatase; |
3-264 | 1.88e-25 | |||||
HMP-PP phosphatase; Pssm-ID: 185080 [Multi-domain] Cd Length: 272 Bit Score: 101.31 E-value: 1.88e-25
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| PRK01158 | PRK01158 | phosphoglycolate phosphatase; Provisional |
1-268 | 2.33e-22 | |||||
phosphoglycolate phosphatase; Provisional Pssm-ID: 234910 [Multi-domain] Cd Length: 230 Bit Score: 92.34 E-value: 2.33e-22
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| HAD_YbiV-Like | cd07518 | Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ... |
4-268 | 1.12e-19 | |||||
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. 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: 319820 [Multi-domain] Cd Length: 184 Bit Score: 83.79 E-value: 1.12e-19
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| HAD-SF-IIB | TIGR01484 | HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ... |
5-240 | 1.24e-18 | |||||
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 273651 [Multi-domain] Cd Length: 207 Bit Score: 81.66 E-value: 1.24e-18
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| Pglycolate_arch | TIGR01487 | phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ... |
4-267 | 1.03e-17 | |||||
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. Pssm-ID: 273652 [Multi-domain] Cd Length: 215 Bit Score: 79.40 E-value: 1.03e-17
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| PRK10976 | PRK10976 | putative hydrolase; Provisional |
3-248 | 2.07e-17 | |||||
putative hydrolase; Provisional Pssm-ID: 182878 [Multi-domain] Cd Length: 266 Bit Score: 79.71 E-value: 2.07e-17
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| PLN02887 | PLN02887 | hydrolase family protein |
3-267 | 1.25e-16 | |||||
hydrolase family protein Pssm-ID: 215479 [Multi-domain] Cd Length: 580 Bit Score: 79.15 E-value: 1.25e-16
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| SPP-subfamily | TIGR01482 | sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ... |
6-259 | 1.61e-14 | |||||
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP. Pssm-ID: 273650 [Multi-domain] Cd Length: 225 Bit Score: 70.95 E-value: 1.61e-14
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| HAD_Pase | cd07514 | phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ... |
197-268 | 7.41e-13 | |||||
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain] Cd Length: 139 Bit Score: 64.15 E-value: 7.41e-13
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| HAD-SF-IIB-MPGP | TIGR01486 | mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ... |
5-248 | 1.03e-12 | |||||
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. Several members of this family from thermophiles (and from Dehalococcoides ethenogenes) are now known to act as mannosyl-3-phosphoglycerate (MPG) phosphatase. In these cases, the enzyme acts after MPG synthase to make the compatible solute mannosylglycerate. We propose that other mesophilic members of this family do not act as mannosyl-3-phosphoglycerate phosphatase. A member of this family is found in Escherichia coli, which appears to lack MPG synthase. Mannosylglycerate is imported in E. coli by phosphoenolpyruvate-dependent transporter (), but it appears the phosphorylation is not on the glycerate moiety, that the phosphorylated import is degraded by an alpha-mannosidase from an adjacent gene, and that E. coli would have no pathway to obtain MPG. Pssm-ID: 130550 [Multi-domain] Cd Length: 256 Bit Score: 66.27 E-value: 1.03e-12
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| SerB | COG0560 | Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ... |
197-252 | 1.30e-12 | |||||
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis Pssm-ID: 440326 [Multi-domain] Cd Length: 221 Bit Score: 65.24 E-value: 1.30e-12
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| HAD_SPP | cd02605 | sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ... |
5-254 | 2.67e-12 | |||||
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. 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: 319792 [Multi-domain] Cd Length: 245 Bit Score: 65.06 E-value: 2.67e-12
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| S6PP | pfam05116 | Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ... |
4-244 | 7.95e-12 | |||||
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis. Pssm-ID: 428314 [Multi-domain] Cd Length: 246 Bit Score: 63.44 E-value: 7.95e-12
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| PRK00192 | PRK00192 | mannosyl-3-phosphoglycerate phosphatase; Reviewed |
1-262 | 1.80e-11 | |||||
mannosyl-3-phosphoglycerate phosphatase; Reviewed Pssm-ID: 234684 [Multi-domain] Cd Length: 273 Bit Score: 62.65 E-value: 1.80e-11
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| HAD_PSP | cd07500 | phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ... |
197-239 | 1.04e-09 | |||||
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain] Cd Length: 180 Bit Score: 56.40 E-value: 1.04e-09
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| HAD_Pase | cd07507 | haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ... |
5-262 | 1.06e-08 | |||||
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii mannosyl-3-phosphoglycerate phosphatase and Persephonella marina glucosyl-3-phosphoglycerate phosphatase; This family includes Pyrococcus horikoshii and Thermus thermophilus HB27 mannosyl-3-phosphoglycerate phosphatases (MpgPs) which catalyze the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG), and Persephonella marina glucosyl-3-phosphoglycerate phosphatase (GpgP) which catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to produce glucosylglycerate (GG). It also includes Methanococcoides burtonii MpgP protein which is able to dephosphorylate GPG to GG, and MPG to MG. Similar flexibilities in substrate specificity have been confirmed in vitro for the MpgPs from Thermus thermophiles and Pyrococcus horikoshii. Screens with natural substrates have not yet detected activity for another member Escherichia Coli YedP. 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: 319810 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 1.06e-08
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| YedP | COG3769 | Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ... |
5-238 | 2.68e-08 | |||||
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 442983 [Multi-domain] Cd Length: 268 Bit Score: 53.68 E-value: 2.68e-08
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| Hydrolase | pfam00702 | haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ... |
3-235 | 5.91e-08 | |||||
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: 51.82 E-value: 5.91e-08
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| HAD_KDO-like | cd01630 | haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ... |
192-254 | 2.12e-06 | |||||
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. 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: 319769 [Multi-domain] Cd Length: 146 Bit Score: 46.36 E-value: 2.12e-06
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| COG4087 | COG4087 | Soluble P-type ATPase [General function prediction only]; |
175-257 | 1.35e-05 | |||||
Soluble P-type ATPase [General function prediction only]; Pssm-ID: 443263 [Multi-domain] Cd Length: 156 Bit Score: 44.00 E-value: 1.35e-05
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| Hydrolase_6 | pfam13344 | Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily. |
6-80 | 1.66e-05 | |||||
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily. Pssm-ID: 433132 Cd Length: 101 Bit Score: 42.84 E-value: 1.66e-05
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| HAD_like | cd01427 | Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ... |
6-91 | 3.01e-05 | |||||
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: 42.00 E-value: 3.01e-05
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| OtsB | COG1877 | Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism]; |
4-45 | 8.67e-05 | |||||
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism]; Pssm-ID: 441481 [Multi-domain] Cd Length: 242 Bit Score: 42.87 E-value: 8.67e-05
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| HAD_PGPPase | cd02612 | phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ... |
197-235 | 9.33e-05 | |||||
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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: 319796 [Multi-domain] Cd Length: 195 Bit Score: 42.29 E-value: 9.33e-05
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| P-type_ATPase-Cd_Zn_Co_like | cd07548 | P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to ... |
216-268 | 1.19e-04 | |||||
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis CadA which appears to transport cadmium, zinc and cobalt but not copper out of the cell; Bacillus subtilis CadA/YvgW appears to transport cadmium, zinc and cobalt but not copper, out of the cell. Functions in metal ion resistance and cellular metal ion homeostasis. CadA/YvgW is also important for sporulation in B. subtilis, the significant specific expression of the cadA/yvgW gene during the late stage of sporulation, is controlled by forespore-specific sigma factor, sigma G, and mother cell-specific sigma factor, sigma E. This subfamily also includes Helicobacter pylori CadA an essential resistance pump with ion specificity towards Cd(2+), Zn(2+) and Co(2+), and Zn-transporting ATPase, ZiaA(N) in Synechocystis PCC 6803. Transcription of ziaA is induced by Zn under the control of the Zn responsive repressor ZiaR. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. Pssm-ID: 319847 [Multi-domain] Cd Length: 604 Bit Score: 42.99 E-value: 1.19e-04
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| HAD-SF-IB-hyp1 | TIGR01490 | HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ... |
197-235 | 5.94e-04 | |||||
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 273654 [Multi-domain] Cd Length: 202 Bit Score: 40.02 E-value: 5.94e-04
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| NagD | COG0647 | Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism]; |
1-43 | 7.29e-04 | |||||
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism]; Pssm-ID: 440412 [Multi-domain] Cd Length: 259 Bit Score: 40.09 E-value: 7.29e-04
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| HAD-SF-IIIA | TIGR01662 | HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ... |
4-44 | 8.31e-04 | |||||
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 273742 [Multi-domain] Cd Length: 135 Bit Score: 38.54 E-value: 8.31e-04
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| serB | PRK11133 | phosphoserine phosphatase; Provisional |
200-239 | 9.06e-04 | |||||
phosphoserine phosphatase; Provisional Pssm-ID: 182988 [Multi-domain] Cd Length: 322 Bit Score: 39.93 E-value: 9.06e-04
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| P-type_ATPases | cd01431 | ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ... |
217-268 | 1.29e-03 | |||||
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine. Pssm-ID: 319764 [Multi-domain] Cd Length: 319 Bit Score: 39.74 E-value: 1.29e-03
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| HAD | pfam12710 | haloacid dehalogenase-like hydrolase; |
17-60 | 1.67e-03 | |||||
haloacid dehalogenase-like hydrolase; Pssm-ID: 432733 [Multi-domain] Cd Length: 188 Bit Score: 38.67 E-value: 1.67e-03
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| P-type_ATPase | cd02609 | uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ... |
222-258 | 1.83e-03 | |||||
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized Streptococcus pneumoniae exported protein 7, Exp7; This subfamily contains P-type ATPase transporters of unknown function, similar to Streptococcus pneumoniae Exp7. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine. Pssm-ID: 319795 [Multi-domain] Cd Length: 661 Bit Score: 39.57 E-value: 1.83e-03
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| P-type_ATPase_Pb_Zn_Cd2-like | cd07546 | P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ... |
200-268 | 1.88e-03 | |||||
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+); Escherichia coli ZntA mediates resistance to toxic levels of selected divalent metal ions. ZntA has the highest selectivity for Pb(2+), followed by Zn(2+) and Cd(2+); it also shows low levels of activity with Cu(2+), Ni(2+), and Co(2+). It is upregulated by the transcription factor ZntR at high zinc concentrations. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. Pssm-ID: 319846 [Multi-domain] Cd Length: 597 Bit Score: 39.31 E-value: 1.88e-03
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| P-type_ATPase_cation | cd02080 | P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ... |
203-269 | 2.30e-03 | |||||
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, and Synechocystis sp. PCC 6803 PMA1, a putative Ca(2+)-ATPase; This subfamily includes the P-type Na(+)-ATPase of an alkaliphilic bacterium Exiguobacterium aurantiacum Mna and cyanobacterium Synechocystis sp. PCC 6803 PMA1, a cation-transporting ATPase which may translocate calcium. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. Pssm-ID: 319775 [Multi-domain] Cd Length: 819 Bit Score: 39.17 E-value: 2.30e-03
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| P-type_ATPase_Na_ENA | cd02086 | fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ... |
222-269 | 2.63e-03 | |||||
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces cerevisiae Ena1p, Ena2p and Ustilago maydis Ena1, and the endoplasmic reticulum sodium transporter Ustilago maydis Ena2; Fungal-type Na(+)-ATPase (also called ENA ATPases). This subfamily includes the Saccharomyces cerevisiae plasma membrane transporters: Na(+)/Li(+)-exporting ATPase Ena1p which may also extrudes K(+), and Na(+)-exporting P-type ATPase Ena2p. It also includes Ustilago maydis plasma membrane Ena1, an K(+)/Na(+)-ATPase whose chief role is to pump Na(+) and K(+) out of the cytoplasm, especially at high pH values, and endoplasmic reticulum Ena2 ATPase which mediates Na(+) or K(+) fluxes in the ER or in other endomembranes. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. Pssm-ID: 319780 [Multi-domain] Cd Length: 920 Bit Score: 38.98 E-value: 2.63e-03
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| P-type_ATPase | cd07538 | uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ... |
217-268 | 3.36e-03 | |||||
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase transporters of unknown function. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine. Pssm-ID: 319839 [Multi-domain] Cd Length: 653 Bit Score: 38.58 E-value: 3.36e-03
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| PTZ00174 | PTZ00174 | phosphomannomutase; Provisional |
1-72 | 5.25e-03 | |||||
phosphomannomutase; Provisional Pssm-ID: 240305 Cd Length: 247 Bit Score: 37.62 E-value: 5.25e-03
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| HAD_like | cd01427 | Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ... |
200-240 | 5.62e-03 | |||||
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: 35.83 E-value: 5.62e-03
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| ATPase_P-type | TIGR01494 | ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ... |
216-268 | 5.80e-03 | |||||
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily. Pssm-ID: 273656 [Multi-domain] Cd Length: 545 Bit Score: 37.68 E-value: 5.80e-03
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| HAD-SF-IB | TIGR01488 | Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ... |
184-234 | 9.03e-03 | |||||
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 273653 [Multi-domain] Cd Length: 177 Bit Score: 36.18 E-value: 9.03e-03
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