sugar-phosphatase [Morganella morganii]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PRK10513 super family | cl32525 | sugar phosphate phosphatase; Provisional |
1-268 | 3.48e-131 | |||||
sugar phosphate phosphatase; Provisional The actual alignment was detected with superfamily member PRK10513: Pssm-ID: 182509 [Multi-domain] Cd Length: 270 Bit Score: 372.10 E-value: 3.48e-131
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| Name | Accession | Description | Interval | E-value | |||||
| PRK10513 | PRK10513 | sugar phosphate phosphatase; Provisional |
1-268 | 3.48e-131 | |||||
sugar phosphate phosphatase; Provisional Pssm-ID: 182509 [Multi-domain] Cd Length: 270 Bit Score: 372.10 E-value: 3.48e-131
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| HAD_Pase | cd07516 | phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ... |
5-266 | 4.90e-93 | |||||
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: 274.86 E-value: 4.90e-93
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| Cof-subfamily | TIGR00099 | Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ... |
5-264 | 2.81e-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: 227.15 E-value: 2.81e-74
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| Cof | COG0561 | Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ... |
2-267 | 8.29e-68 | |||||
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: 208.45 E-value: 8.29e-68
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| Hydrolase_3 | pfam08282 | haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ... |
6-264 | 4.79e-67 | |||||
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes. Pssm-ID: 429897 [Multi-domain] Cd Length: 255 Bit Score: 208.63 E-value: 4.79e-67
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| Name | Accession | Description | Interval | E-value | |||||
| PRK10513 | PRK10513 | sugar phosphate phosphatase; Provisional |
1-268 | 3.48e-131 | |||||
sugar phosphate phosphatase; Provisional Pssm-ID: 182509 [Multi-domain] Cd Length: 270 Bit Score: 372.10 E-value: 3.48e-131
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| HAD_Pase | cd07516 | phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ... |
5-266 | 4.90e-93 | |||||
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: 274.86 E-value: 4.90e-93
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| Cof-subfamily | TIGR00099 | Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ... |
5-264 | 2.81e-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: 227.15 E-value: 2.81e-74
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| Cof | COG0561 | Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ... |
2-267 | 8.29e-68 | |||||
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: 208.45 E-value: 8.29e-68
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| Hydrolase_3 | pfam08282 | haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ... |
6-264 | 4.79e-67 | |||||
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes. Pssm-ID: 429897 [Multi-domain] Cd Length: 255 Bit Score: 208.63 E-value: 4.79e-67
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| HAD_HPP | cd07517 | phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ... |
4-267 | 1.56e-39 | |||||
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: 136.58 E-value: 1.56e-39
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| PRK10530 | PRK10530 | pyridoxal phosphate (PLP) phosphatase; Provisional |
1-268 | 1.39e-31 | |||||
pyridoxal phosphate (PLP) phosphatase; Provisional Pssm-ID: 182523 [Multi-domain] Cd Length: 272 Bit Score: 117.43 E-value: 1.39e-31
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| PRK01158 | PRK01158 | phosphoglycolate phosphatase; Provisional |
1-268 | 1.80e-30 | |||||
phosphoglycolate phosphatase; Provisional Pssm-ID: 234910 [Multi-domain] Cd Length: 230 Bit Score: 113.53 E-value: 1.80e-30
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| PLN02887 | PLN02887 | hydrolase family protein |
4-267 | 1.37e-24 | |||||
hydrolase family protein Pssm-ID: 215479 [Multi-domain] Cd Length: 580 Bit Score: 102.65 E-value: 1.37e-24
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| HAD_YbiV-Like | cd07518 | Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ... |
4-265 | 2.12e-24 | |||||
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: 96.50 E-value: 2.12e-24
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| HAD-SF-IIB | TIGR01484 | HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ... |
5-237 | 3.12e-23 | |||||
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: 93.98 E-value: 3.12e-23
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| HAD_Pase | cd07514 | phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ... |
173-267 | 2.62e-19 | |||||
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: 81.48 E-value: 2.62e-19
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| Pglycolate_arch | TIGR01487 | phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ... |
3-264 | 9.69e-19 | |||||
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: 82.10 E-value: 9.69e-19
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| PRK15126 | PRK15126 | HMP-PP phosphatase; |
4-246 | 1.12e-17 | |||||
HMP-PP phosphatase; Pssm-ID: 185080 [Multi-domain] Cd Length: 272 Bit Score: 80.12 E-value: 1.12e-17
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| SPP-subfamily | TIGR01482 | sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ... |
6-267 | 1.66e-17 | |||||
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: 79.04 E-value: 1.66e-17
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| YedP | COG3769 | Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ... |
5-268 | 3.64e-12 | |||||
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 442983 [Multi-domain] Cd Length: 268 Bit Score: 64.85 E-value: 3.64e-12
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| HAD-SF-IIB-MPGP | TIGR01486 | mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ... |
5-229 | 3.19e-11 | |||||
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: 62.03 E-value: 3.19e-11
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| PRK10976 | PRK10976 | putative hydrolase; Provisional |
5-260 | 9.06e-11 | |||||
putative hydrolase; Provisional Pssm-ID: 182878 [Multi-domain] Cd Length: 266 Bit Score: 60.83 E-value: 9.06e-11
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| HAD_KDO-like | cd01630 | haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ... |
197-255 | 6.62e-09 | |||||
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: 53.29 E-value: 6.62e-09
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| HAD_SPP | cd02605 | sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ... |
187-267 | 8.44e-09 | |||||
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: 54.66 E-value: 8.44e-09
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| PRK00192 | PRK00192 | mannosyl-3-phosphoglycerate phosphatase; Reviewed |
1-240 | 1.10e-08 | |||||
mannosyl-3-phosphoglycerate phosphatase; Reviewed Pssm-ID: 234684 [Multi-domain] Cd Length: 273 Bit Score: 54.56 E-value: 1.10e-08
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| PRK03669 | PRK03669 | mannosyl-3-phosphoglycerate phosphatase-related protein; |
5-233 | 4.31e-08 | |||||
mannosyl-3-phosphoglycerate phosphatase-related protein; Pssm-ID: 179628 [Multi-domain] Cd Length: 271 Bit Score: 52.71 E-value: 4.31e-08
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| HAD_Pase | cd07507 | haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ... |
5-229 | 5.67e-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: 52.37 E-value: 5.67e-08
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| KdsC | COG1778 | 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ... |
197-255 | 3.09e-07 | |||||
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only]; Pssm-ID: 441384 [Multi-domain] Cd Length: 170 Bit Score: 49.28 E-value: 3.09e-07
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| S6PP | pfam05116 | Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ... |
4-240 | 1.62e-06 | |||||
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: 48.03 E-value: 1.62e-06
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| HAD_PSP | cd07500 | phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ... |
195-236 | 9.16e-06 | |||||
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: 44.85 E-value: 9.16e-06
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| HAD_like | cd01427 | Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ... |
5-74 | 2.06e-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: 42.77 E-value: 2.06e-05
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| SerB | COG0560 | Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ... |
195-236 | 3.64e-05 | |||||
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: 43.67 E-value: 3.64e-05
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| Hydrolase | pfam00702 | haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ... |
3-232 | 5.37e-05 | |||||
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: 42.96 E-value: 5.37e-05
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| Hydrolase_6 | pfam13344 | Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily. |
6-60 | 5.88e-05 | |||||
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily. Pssm-ID: 433132 Cd Length: 101 Bit Score: 41.30 E-value: 5.88e-05
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| PRK13222 | PRK13222 | N-acetylmuramic acid 6-phosphate phosphatase MupP; |
1-30 | 2.11e-04 | |||||
N-acetylmuramic acid 6-phosphate phosphatase MupP; Pssm-ID: 237310 [Multi-domain] Cd Length: 226 Bit Score: 41.33 E-value: 2.11e-04
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| HAD_PMM | cd02585 | phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis ... |
5-75 | 3.54e-04 | |||||
phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis thaliana PMM; PMM catalyzes the interconversion of mannose-6-phosphate (M6P) to mannose-1-phosphate (M1P); the conversion of M6P to M1P is an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes. M1P is the substrate for the synthesis of GDP-mannose, which is an intermediate for protein glycosylation, protein sorting and secretion, and maintaining a functional endomembrane system in eukaryotic cells. Proteins in this family contains a conserved phosphorylated motif DxDx(T/V) shared with some other phosphotransferases. This family contains two human homologs, PMM1 and PMM2; PMM2 deficiency causes congenital disorder of glycosylation type I-a, also known as Jaeken syndrome. PMM1 can also act as glucose-1,6-bisphosphatase in the brain after stimulation with inosine monophosphate; PMM2 on the other hand, is insensitive to IMP and demonstrates low glucose-1,6-bisphosphatase activity. Arabidopsis thaliana PMM converted M1P into M6P and glucose-1-phosphate into glucose-6-phosphate, with the latter reaction being less efficient. Arabidopsis thaliana and Nicotiana benthamian PPMs are involved in ascorbic acid biosynthesis. 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: 319784 Cd Length: 238 Bit Score: 40.72 E-value: 3.54e-04
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| PTZ00174 | PTZ00174 | phosphomannomutase; Provisional |
1-75 | 5.14e-04 | |||||
phosphomannomutase; Provisional Pssm-ID: 240305 Cd Length: 247 Bit Score: 40.32 E-value: 5.14e-04
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| ATPase-IB_hvy | TIGR01525 | heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the ... |
214-266 | 5.88e-04 | |||||
heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the copper and cadmium-type heavy metal transporting P-type ATPases (TIGR01511 and TIGR01512) as well as those species which score ambiguously between both models. For more comments and references, see the files on TIGR01511 and 01512. Pssm-ID: 273669 [Multi-domain] Cd Length: 558 Bit Score: 41.08 E-value: 5.88e-04
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| P-type_ATPase_APLT_Neo1-like | cd07541 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ... |
197-248 | 7.46e-04 | |||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human putative APLT, ATP9B; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as a flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. The yeast Neo1 gene is an essential gene; Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Also included in this sub family is human putative ATPase phospholipid transporting 9B, ATP9B, which localizes to the trans-golgi network in a CDC50 protein-independent manner. Levels of ATP9B, along with levels of other ATPase genes, may contribute to expressivity of and atypical presentations of Hailey-Hailey disease (HHD), and the ATP9B gene has recently been identified as a putative Alzheimer's disease loci. 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: 319841 [Multi-domain] Cd Length: 792 Bit Score: 40.86 E-value: 7.46e-04
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| HAD_TPP | cd01627 | trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ... |
5-241 | 8.13e-04 | |||||
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. 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: 319767 [Multi-domain] Cd Length: 228 Bit Score: 39.58 E-value: 8.13e-04
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| COG4087 | COG4087 | Soluble P-type ATPase [General function prediction only]; |
210-236 | 1.18e-03 | |||||
Soluble P-type ATPase [General function prediction only]; Pssm-ID: 443263 [Multi-domain] Cd Length: 156 Bit Score: 38.60 E-value: 1.18e-03
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| serB | TIGR00338 | phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ... |
197-247 | 1.38e-03 | |||||
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family] Pssm-ID: 273022 [Multi-domain] Cd Length: 219 Bit Score: 38.88 E-value: 1.38e-03
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| KdsC-phosphatas | TIGR01670 | 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ... |
204-264 | 1.62e-03 | |||||
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) 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. One member of this family, the YrbI protein from H. influenzae has been cloned, expressed, purified and found to be an active 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase. Furthermore, its crystal structure has been determined. This family consists of sequences from beta, gamma and epsilon proteobacteria, Aquifex, Fusobacterium, Porphyromonas and Methanosarcina. The Methanosarcina sequence is distinctive in that it is linked to an N-terminal cytidylyltransferase domain (pfam02348) and is annotated as acylneuraminate cytidylyltransferase. This may give some clue as the function of these phosphatases. Several eukaryotic sequences scoring between trusted and noise are also closely related to this function such as the CMP-N-acetylneuraminic acid synthetase from mouse, but in these cases the phosphatase domain is clearly inactive as many of the active site residues are not conserved. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] Pssm-ID: 130731 [Multi-domain] Cd Length: 154 Bit Score: 38.27 E-value: 1.62e-03
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| NagD | COG0647 | Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism]; |
1-60 | 1.87e-03 | |||||
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism]; Pssm-ID: 440412 [Multi-domain] Cd Length: 259 Bit Score: 38.94 E-value: 1.87e-03
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| HAD_like | cd01427 | Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ... |
192-237 | 1.96e-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: 36.99 E-value: 1.96e-03
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| P-type_ATPase_HM | cd07550 | P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ... |
213-265 | 3.64e-03 | |||||
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. 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: 319848 [Multi-domain] Cd Length: 592 Bit Score: 38.41 E-value: 3.64e-03
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| P-type_ATPase_HM | cd02079 | P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ... |
213-266 | 3.77e-03 | |||||
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family 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: 319774 [Multi-domain] Cd Length: 617 Bit Score: 38.35 E-value: 3.77e-03
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| ATPase-Plipid | TIGR01652 | phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ... |
197-235 | 7.92e-03 | |||||
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes. Pssm-ID: 273734 [Multi-domain] Cd Length: 1057 Bit Score: 37.75 E-value: 7.92e-03
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