MULTISPECIES: bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH [Acinetobacter]
Protein Classification
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH( domain architecture ID 10014284)
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH catalyzes both the dephosphorylation of phosphoserine (P-Ser) and phosphothreonine (P-Thr), and the transfer of a phosphoryl group to homoserine using phosphoserine as the phosphoryl group donor
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| thrH | PRK13582 | bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH; |
1-205 | 1.40e-151 | ||||
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH; : Pssm-ID: 237437 [Multi-domain] Cd Length: 205 Bit Score: 418.18 E-value: 1.40e-151
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| thrH | PRK13582 | bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH; |
1-205 | 1.40e-151 | ||||
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH; Pssm-ID: 237437 [Multi-domain] Cd Length: 205 Bit Score: 418.18 E-value: 1.40e-151
|
||||||||
| HSK-PSP | TIGR02137 | phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is ... |
1-203 | 4.33e-108 | ||||
phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is has been characterized as both a phosphoserine phosphatase and a phosphoserine:homoserine phosphotransferase. In Pseudomonas aeruginosa, where the characterization was done, a second phosphoserine phosphatase (SerB) and a second homoserine kinase (thrB) are found, but in Fibrobacter succinogenes neither are present. This enzyme is a member of the haloacid dehalogenase (HAD) superfamily, specifically part of subfamily IB by virtue of the presence of an alpha helical domain in between motifs I and II of the HAD domain. The closest homologs to this family are monofunctional phosphoserine phosphatases (TIGR00338). Pssm-ID: 162723 Cd Length: 203 Bit Score: 308.39 E-value: 4.33e-108
|
||||||||
| HAD_ThrH_like | cd02607 | bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to ... |
1-192 | 1.75e-87 | ||||
bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to Pseudomonas aeruginosa ThrH; This family includes Pseudomonas aeruginosa ThrH which is a duel activity enzyme having both phosphoserine phosphatase and phosphoserine:homoserine phosphotransferase activities, i.e. it can dephosphorylate phosphoserine, and can transfer phosphate from phosphoserine to homoserine. 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: 319793 [Multi-domain] Cd Length: 195 Bit Score: 256.05 E-value: 1.75e-87
|
||||||||
| SerB | COG0560 | Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ... |
1-171 | 8.94e-16 | ||||
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: 72.56 E-value: 8.94e-16
|
||||||||
| Hydrolase | pfam00702 | haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ... |
1-164 | 6.37e-07 | ||||
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: 47.97 E-value: 6.37e-07
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| thrH | PRK13582 | bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH; |
1-205 | 1.40e-151 | ||||
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH; Pssm-ID: 237437 [Multi-domain] Cd Length: 205 Bit Score: 418.18 E-value: 1.40e-151
|
||||||||
| HSK-PSP | TIGR02137 | phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is ... |
1-203 | 4.33e-108 | ||||
phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is has been characterized as both a phosphoserine phosphatase and a phosphoserine:homoserine phosphotransferase. In Pseudomonas aeruginosa, where the characterization was done, a second phosphoserine phosphatase (SerB) and a second homoserine kinase (thrB) are found, but in Fibrobacter succinogenes neither are present. This enzyme is a member of the haloacid dehalogenase (HAD) superfamily, specifically part of subfamily IB by virtue of the presence of an alpha helical domain in between motifs I and II of the HAD domain. The closest homologs to this family are monofunctional phosphoserine phosphatases (TIGR00338). Pssm-ID: 162723 Cd Length: 203 Bit Score: 308.39 E-value: 4.33e-108
|
||||||||
| HAD_ThrH_like | cd02607 | bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to ... |
1-192 | 1.75e-87 | ||||
bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to Pseudomonas aeruginosa ThrH; This family includes Pseudomonas aeruginosa ThrH which is a duel activity enzyme having both phosphoserine phosphatase and phosphoserine:homoserine phosphotransferase activities, i.e. it can dephosphorylate phosphoserine, and can transfer phosphate from phosphoserine to homoserine. 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: 319793 [Multi-domain] Cd Length: 195 Bit Score: 256.05 E-value: 1.75e-87
|
||||||||
| SerB | COG0560 | Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ... |
1-171 | 8.94e-16 | ||||
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: 72.56 E-value: 8.94e-16
|
||||||||
| HAD-SF-IB | TIGR01488 | Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ... |
3-160 | 7.81e-10 | ||||
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: 55.82 E-value: 7.81e-10
|
||||||||
| Hydrolase | pfam00702 | haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ... |
1-164 | 6.37e-07 | ||||
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: 47.97 E-value: 6.37e-07
|
||||||||
| HAD_PSP | cd07500 | phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ... |
38-171 | 7.89e-07 | ||||
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: 47.16 E-value: 7.89e-07
|
||||||||
| HAD | pfam12710 | haloacid dehalogenase-like hydrolase; |
57-160 | 2.78e-05 | ||||
haloacid dehalogenase-like hydrolase; Pssm-ID: 432733 [Multi-domain] Cd Length: 188 Bit Score: 42.91 E-value: 2.78e-05
|
||||||||
| HAD_Pase | cd07524 | phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ... |
71-167 | 1.12e-04 | ||||
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. 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: 319826 [Multi-domain] Cd Length: 211 Bit Score: 41.55 E-value: 1.12e-04
|
||||||||
| Cof | COG0561 | Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ... |
146-174 | 1.03e-03 | ||||
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: 38.58 E-value: 1.03e-03
|
||||||||
| HAD_like | cd01427 | Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ... |
73-163 | 1.48e-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: 1.48e-03
|
||||||||
| Cof-subfamily | TIGR00099 | Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ... |
146-177 | 1.57e-03 | ||||
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: 38.40 E-value: 1.57e-03
|
||||||||
| HAD_PGPPase | cd02612 | phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ... |
7-165 | 2.21e-03 | ||||
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: 37.67 E-value: 2.21e-03
|
||||||||
| COG4087 | COG4087 | Soluble P-type ATPase [General function prediction only]; |
64-163 | 2.67e-03 | ||||
Soluble P-type ATPase [General function prediction only]; Pssm-ID: 443263 [Multi-domain] Cd Length: 156 Bit Score: 37.06 E-value: 2.67e-03
|
||||||||
| Blast search parameters | ||||
|
