bifunctional imidazole glycerol-phosphate dehydratase/histidinol phosphatase [Escherichia coli str. K-12 substr. MG1655]
Protein Classification
bifunctional imidazole glycerol-phosphate dehydratase/histidinol phosphatase( domain architecture ID 11481005)
bifunctional imidazole glycerol-phosphate dehydratase/histidinol phosphatase catalyzes the formation of 3-(imidazol-4-yl)-2-oxopropyl phosphate from D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate and the hydrolysis of L-histidinol phosphate to L-histidinol and phosphate
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| PRK05446 | PRK05446 | bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB; |
2-355 | 0e+00 | ||||||
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB; : Pssm-ID: 235471 [Multi-domain] Cd Length: 354 Bit Score: 777.05 E-value: 0e+00
|
||||||||||
| Name | Accession | Description | Interval | E-value | ||||||
| PRK05446 | PRK05446 | bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB; |
2-355 | 0e+00 | ||||||
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB; Pssm-ID: 235471 [Multi-domain] Cd Length: 354 Bit Score: 777.05 E-value: 0e+00
|
||||||||||
| IGPD | cd07914 | Imidazoleglycerol-phosphate dehydratase; Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2. ... |
169-355 | 7.25e-117 | ||||||
Imidazoleglycerol-phosphate dehydratase; Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2.1.19) catalyzes the dehydration of imidazole glycerol phosphate to imidazole acetol phosphate, the sixth step of histidine biosynthesis in plants and microorganisms where the histidine is synthesized de novo. There is an internal repeat in the protein domain that is related by pseudo-dyad symmetry, perhaps as a result of an ancient gene duplication. The apo-form of IGPD exists as a catalytically inactive trimer which, in the presence of specific divalent metal cations such as manganese (Mn2+), cobalt (Co2+), cadmium (Cd2+), nickel (Ni2+), iron (Fe2+) and zinc (Zn2+), assembles to form a biologically active high molecular weight metalloenzyme; a 24-mer with 4-3-2 symmetry. Each 24-mer has 24 active sites, and contains around 1.5 metal ions per monomer, each monomer contributing residues to three separate active sites. IGPD enzymes are monofunctional in fungi, plants, archaea and some eubacteria while they are encoded as bifunctional enzymes in other eubacteria, such that the enzyme is fused to histidinol-phosphate phosphatase, the penultimate enzyme of the histidine biosynthesis pathway. The histidine biosynthesis pathway is a potential target for development of herbicides, and IGPD is a target for the triazole phosphonate herbicides. Pssm-ID: 153419 Cd Length: 190 Bit Score: 336.29 E-value: 7.25e-117
|
||||||||||
| hisB_Nterm | TIGR01261 | histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ... |
3-163 | 2.58e-106 | ||||||
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: 308.56 E-value: 2.58e-106
|
||||||||||
| HisB2 | COG0131 | Imidazoleglycerol phosphate dehydratase HisB [Amino acid transport and metabolism]; ... |
177-355 | 2.16e-105 | ||||||
Imidazoleglycerol phosphate dehydratase HisB [Amino acid transport and metabolism]; Imidazoleglycerol phosphate dehydratase HisB is part of the Pathway/BioSystem: Histidine biosynthesis Pssm-ID: 439901 Cd Length: 183 Bit Score: 306.96 E-value: 2.16e-105
|
||||||||||
| IGPD | pfam00475 | Imidazoleglycerol-phosphate dehydratase; |
200-337 | 1.26e-87 | ||||||
Imidazoleglycerol-phosphate dehydratase; Pssm-ID: 459824 Cd Length: 140 Bit Score: 259.98 E-value: 1.26e-87
|
||||||||||
| Name | Accession | Description | Interval | E-value | ||||||
| PRK05446 | PRK05446 | bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB; |
2-355 | 0e+00 | ||||||
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB; Pssm-ID: 235471 [Multi-domain] Cd Length: 354 Bit Score: 777.05 E-value: 0e+00
|
||||||||||
| IGPD | cd07914 | Imidazoleglycerol-phosphate dehydratase; Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2. ... |
169-355 | 7.25e-117 | ||||||
Imidazoleglycerol-phosphate dehydratase; Imidazoleglycerol-phosphate dehydratase (IGPD; EC 4.2.1.19) catalyzes the dehydration of imidazole glycerol phosphate to imidazole acetol phosphate, the sixth step of histidine biosynthesis in plants and microorganisms where the histidine is synthesized de novo. There is an internal repeat in the protein domain that is related by pseudo-dyad symmetry, perhaps as a result of an ancient gene duplication. The apo-form of IGPD exists as a catalytically inactive trimer which, in the presence of specific divalent metal cations such as manganese (Mn2+), cobalt (Co2+), cadmium (Cd2+), nickel (Ni2+), iron (Fe2+) and zinc (Zn2+), assembles to form a biologically active high molecular weight metalloenzyme; a 24-mer with 4-3-2 symmetry. Each 24-mer has 24 active sites, and contains around 1.5 metal ions per monomer, each monomer contributing residues to three separate active sites. IGPD enzymes are monofunctional in fungi, plants, archaea and some eubacteria while they are encoded as bifunctional enzymes in other eubacteria, such that the enzyme is fused to histidinol-phosphate phosphatase, the penultimate enzyme of the histidine biosynthesis pathway. The histidine biosynthesis pathway is a potential target for development of herbicides, and IGPD is a target for the triazole phosphonate herbicides. Pssm-ID: 153419 Cd Length: 190 Bit Score: 336.29 E-value: 7.25e-117
|
||||||||||
| hisB | PRK00951 | imidazoleglycerol-phosphate dehydratase HisB; |
166-355 | 1.77e-106 | ||||||
imidazoleglycerol-phosphate dehydratase HisB; Pssm-ID: 234873 Cd Length: 195 Bit Score: 310.12 E-value: 1.77e-106
|
||||||||||
| hisB_Nterm | TIGR01261 | histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ... |
3-163 | 2.58e-106 | ||||||
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: 308.56 E-value: 2.58e-106
|
||||||||||
| HisB2 | COG0131 | Imidazoleglycerol phosphate dehydratase HisB [Amino acid transport and metabolism]; ... |
177-355 | 2.16e-105 | ||||||
Imidazoleglycerol phosphate dehydratase HisB [Amino acid transport and metabolism]; Imidazoleglycerol phosphate dehydratase HisB is part of the Pathway/BioSystem: Histidine biosynthesis Pssm-ID: 439901 Cd Length: 183 Bit Score: 306.96 E-value: 2.16e-105
|
||||||||||
| IGPD | pfam00475 | Imidazoleglycerol-phosphate dehydratase; |
200-337 | 1.26e-87 | ||||||
Imidazoleglycerol-phosphate dehydratase; Pssm-ID: 459824 Cd Length: 140 Bit Score: 259.98 E-value: 1.26e-87
|
||||||||||
| PLN02800 | PLN02800 | imidazoleglycerol-phosphate dehydratase |
167-355 | 6.57e-82 | ||||||
imidazoleglycerol-phosphate dehydratase Pssm-ID: 215430 [Multi-domain] Cd Length: 261 Bit Score: 250.14 E-value: 6.57e-82
|
||||||||||
| HisB1/GmhB | COG0241 | Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ... |
1-151 | 4.00e-70 | ||||||
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: 216.89 E-value: 4.00e-70
|
||||||||||
| HAD_HisB-N | cd07503 | histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ... |
4-148 | 5.01e-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: 192.36 E-value: 5.01e-61
|
||||||||||
| hisB | PRK13598 | imidazoleglycerol-phosphate dehydratase; Provisional |
167-355 | 1.57e-55 | ||||||
imidazoleglycerol-phosphate dehydratase; Provisional Pssm-ID: 184171 Cd Length: 193 Bit Score: 180.00 E-value: 1.57e-55
|
||||||||||
| Histidinol-ppas | TIGR01656 | histidinol-phosphate phosphatase family domain; This domain is found in authentic ... |
4-143 | 5.54e-47 | ||||||
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: 156.40 E-value: 5.54e-47
|
||||||||||
| PRK08942 | PRK08942 | D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase; |
1-144 | 5.87e-28 | ||||||
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase; Pssm-ID: 236354 [Multi-domain] Cd Length: 181 Bit Score: 107.60 E-value: 5.87e-28
|
||||||||||
| GmhB_yaeD | TIGR00213 | D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD ... |
4-140 | 1.06e-22 | ||||||
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: 93.45 E-value: 1.06e-22
|
||||||||||
| HAD-SF-IIIA | TIGR01662 | HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ... |
4-150 | 3.38e-18 | ||||||
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: 79.76 E-value: 3.38e-18
|
||||||||||
| PRK06769 | PRK06769 | HAD-IIIA family hydrolase; |
1-171 | 2.66e-17 | ||||||
HAD-IIIA family hydrolase; Pssm-ID: 180686 [Multi-domain] Cd Length: 173 Bit Score: 78.62 E-value: 2.66e-17
|
||||||||||
| HAD_like | cd01427 | Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ... |
6-148 | 5.98e-09 | ||||||
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: 53.17 E-value: 5.98e-09
|
||||||||||
| HAD_PNP | cd01625 | polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional ... |
9-143 | 2.04e-08 | ||||||
polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional enzyme polynucleotide 5'-kinase/3'-phosphatase; Polynucleotide 3'-phosphatase (PNP) domain. This domain dephosphorylates single-stranded as well as double-stranded 3'-phospho termini. It is found in bifunctional enzyme polynucleotide kinase/phosphatase (PNKP) which contain both kinase and phosphatase domains. PNKP plays a key role in both base excision repair and non-homologous end-joining DNA repair pathway. DNA strand breaks can result from DNA damage by ionizing radiation and chemical agents, such as alkylating agents or anticancer agents. Such DNA damage often results in DNA strands with 5'-hydroxyl and 3'-phosphate termini. However, the repair of DNA damage by DNA polymerases and ligases requires 5'-phosphate and 3'-hydroxyl termini. PNKP acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. 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: 319766 Cd Length: 154 Bit Score: 52.74 E-value: 2.04e-08
|
||||||||||
| Gph | COG0546 | Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]; |
22-143 | 4.00e-06 | ||||||
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]; Pssm-ID: 440312 [Multi-domain] Cd Length: 214 Bit Score: 47.23 E-value: 4.00e-06
|
||||||||||
| PNK3P | pfam08645 | Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ... |
9-143 | 7.80e-06 | ||||||
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the repair of single breaks in DNA induced by DNA-damaging agents such as gamma radiation and camptothecin. Pssm-ID: 370030 Cd Length: 161 Bit Score: 45.33 E-value: 7.80e-06
|
||||||||||
| YigB | COG1011 | FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ... |
4-156 | 1.21e-05 | ||||||
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism]; Pssm-ID: 440635 [Multi-domain] Cd Length: 220 Bit Score: 45.79 E-value: 1.21e-05
|
||||||||||
| HAD | pfam12710 | haloacid dehalogenase-like hydrolase; |
24-139 | 1.65e-04 | ||||||
haloacid dehalogenase-like hydrolase; Pssm-ID: 432733 [Multi-domain] Cd Length: 188 Bit Score: 42.13 E-value: 1.65e-04
|
||||||||||
| PNK-3'Pase | TIGR01663 | polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ... |
2-132 | 3.17e-04 | ||||||
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78 Pssm-ID: 130724 [Multi-domain] Cd Length: 526 Bit Score: 42.32 E-value: 3.17e-04
|
||||||||||
| HAD_like | cd07533 | uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ... |
34-146 | 4.05e-04 | ||||||
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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: 319835 [Multi-domain] Cd Length: 207 Bit Score: 41.23 E-value: 4.05e-04
|
||||||||||
| HAD_Pase | cd16418 | phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid ... |
36-135 | 9.45e-04 | ||||||
phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid dehalogenase-like superfamily; This family includes phosphatases with different substrate specificities. Human PHOSPHO1 is a phosphoethanolamine/phosphocholine phosphatase associated with high levels of expression at mineralizing regions of bone and cartilage and is thought to be involved in the generation of inorganic phosphate for bone mineralization. Human PHOSPHO2 is a putative phosphatase which shows high specific activity toward pyridoxal-5-phosphate; PHODPHO2 is not specific to bone but is expressed in a wide range of soft tissues. These 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 (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) 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: 319855 Cd Length: 130 Bit Score: 38.85 E-value: 9.45e-04
|
||||||||||
| Hydrolase_like | pfam13242 | HAD-hyrolase-like; |
103-146 | 2.63e-03 | ||||||
HAD-hyrolase-like; Pssm-ID: 433056 [Multi-domain] Cd Length: 75 Bit Score: 36.05 E-value: 2.63e-03
|
||||||||||
| HAD-SF-IA-v3 | TIGR01509 | haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ... |
29-144 | 3.03e-03 | ||||||
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 273662 [Multi-domain] Cd Length: 178 Bit Score: 38.17 E-value: 3.03e-03
|
||||||||||
| Blast search parameters | ||||
|
