RecName: Full=D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase; AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase; Short=HBP phosphatase
HAD family hydrolase( domain architecture ID 11492994)
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 | |||
Histidinol-ppas | TIGR01656 | histidinol-phosphate phosphatase family domain; This domain is found in authentic ... |
10-147 | 3.01e-68 | |||
histidinol-phosphate phosphatase family domain; This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3. : Pssm-ID: 273737 Cd Length: 147 Bit Score: 204.94 E-value: 3.01e-68
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Name | Accession | Description | Interval | E-value | ||||
Histidinol-ppas | TIGR01656 | histidinol-phosphate phosphatase family domain; This domain is found in authentic ... |
10-147 | 3.01e-68 | ||||
histidinol-phosphate phosphatase family domain; This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3. Pssm-ID: 273737 Cd Length: 147 Bit Score: 204.94 E-value: 3.01e-68
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HAD_HisB-N | cd07503 | histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ... |
10-147 | 8.75e-61 | ||||
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose 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: 319806 [Multi-domain] Cd Length: 142 Bit Score: 185.81 E-value: 8.75e-61
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HisB1/GmhB | COG0241 | Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ... |
9-179 | 7.51e-55 | ||||
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis Pssm-ID: 440011 [Multi-domain] Cd Length: 176 Bit Score: 171.82 E-value: 7.51e-55
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PRK08942 | PRK08942 | D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase; |
12-144 | 1.58e-30 | ||||
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase; Pssm-ID: 236354 [Multi-domain] Cd Length: 181 Bit Score: 109.91 E-value: 1.58e-30
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Name | Accession | Description | Interval | E-value | ||||
Histidinol-ppas | TIGR01656 | histidinol-phosphate phosphatase family domain; This domain is found in authentic ... |
10-147 | 3.01e-68 | ||||
histidinol-phosphate phosphatase family domain; This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3. Pssm-ID: 273737 Cd Length: 147 Bit Score: 204.94 E-value: 3.01e-68
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HAD_HisB-N | cd07503 | histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ... |
10-147 | 8.75e-61 | ||||
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose 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: 319806 [Multi-domain] Cd Length: 142 Bit Score: 185.81 E-value: 8.75e-61
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HisB1/GmhB | COG0241 | Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ... |
9-179 | 7.51e-55 | ||||
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis Pssm-ID: 440011 [Multi-domain] Cd Length: 176 Bit Score: 171.82 E-value: 7.51e-55
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HAD-SF-IIIA | TIGR01662 | HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ... |
10-147 | 8.98e-39 | ||||
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: 129.45 E-value: 8.98e-39
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PRK08942 | PRK08942 | D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase; |
12-144 | 1.58e-30 | ||||
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase; Pssm-ID: 236354 [Multi-domain] Cd Length: 181 Bit Score: 109.91 E-value: 1.58e-30
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GmhB_yaeD | TIGR00213 | D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD ... |
12-175 | 9.27e-25 | ||||
D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD resembles the histidinol phosphatase domain of the bifunctional protein HisB. The member from E. coli has been characterized as D,D-heptose 1,7-bisphosphate phosphatase, GmhB, involved in inner core LPS assembly (). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] Pssm-ID: 129317 [Multi-domain] Cd Length: 176 Bit Score: 94.99 E-value: 9.27e-25
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PRK05446 | PRK05446 | bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB; |
12-146 | 2.34e-18 | ||||
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB; Pssm-ID: 235471 [Multi-domain] Cd Length: 354 Bit Score: 80.99 E-value: 2.34e-18
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hisB_Nterm | TIGR01261 | histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ... |
12-147 | 5.60e-18 | ||||
histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the scope of this model are bifunctional proteins with a histidinol phosphatase domain followed by an imidazoleglycerol-phosphate dehydratase domain. These enzymatic domains catalyze the ninth and seventh steps, respectively, of histidine biosynthesis. [Amino acid biosynthesis, Histidine family] Pssm-ID: 130328 [Multi-domain] Cd Length: 161 Bit Score: 76.67 E-value: 5.60e-18
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PRK06769 | PRK06769 | HAD-IIIA family hydrolase; |
12-147 | 3.35e-12 | ||||
HAD-IIIA family hydrolase; Pssm-ID: 180686 [Multi-domain] Cd Length: 173 Bit Score: 61.67 E-value: 3.35e-12
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Blast search parameters | ||||
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