phosphoglycerate mutase family protein [Salipiger profundus]
Protein Classification
histidine phosphatase family protein( domain architecture ID 1903463)
histidine phosphatase family protein is a probable phosphatase that may catalyze the dephosphorylation of a phosphorylated substrate involving a conserved catalytic histidine residue which becomes phosphorylated during the reaction
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| PhoE super family | cl43133 | Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism]; |
29-95 | 9.86e-04 | ||
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism]; The actual alignment was detected with superfamily member COG0406: Pssm-ID: 440175 [Multi-domain] Cd Length: 195 Bit Score: 38.00 E-value: 9.86e-04
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| Name | Accession | Description | Interval | E-value | ||
| PhoE | COG0406 | Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism]; |
29-95 | 9.86e-04 | ||
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism]; Pssm-ID: 440175 [Multi-domain] Cd Length: 195 Bit Score: 38.00 E-value: 9.86e-04
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| His_Phos_1 | pfam00300 | Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ... |
30-95 | 2.12e-03 | ||
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members. Pssm-ID: 459751 [Multi-domain] Cd Length: 194 Bit Score: 36.80 E-value: 2.12e-03
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| PRK15004 | PRK15004 | adenosylcobalamin/alpha-ribazole phosphatase; |
30-96 | 8.68e-03 | ||
adenosylcobalamin/alpha-ribazole phosphatase; Pssm-ID: 184966 [Multi-domain] Cd Length: 199 Bit Score: 35.03 E-value: 8.68e-03
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| Name | Accession | Description | Interval | E-value | ||
| PhoE | COG0406 | Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism]; |
29-95 | 9.86e-04 | ||
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism]; Pssm-ID: 440175 [Multi-domain] Cd Length: 195 Bit Score: 38.00 E-value: 9.86e-04
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| His_Phos_1 | pfam00300 | Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ... |
30-95 | 2.12e-03 | ||
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members. Pssm-ID: 459751 [Multi-domain] Cd Length: 194 Bit Score: 36.80 E-value: 2.12e-03
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| PRK15004 | PRK15004 | adenosylcobalamin/alpha-ribazole phosphatase; |
30-96 | 8.68e-03 | ||
adenosylcobalamin/alpha-ribazole phosphatase; Pssm-ID: 184966 [Multi-domain] Cd Length: 199 Bit Score: 35.03 E-value: 8.68e-03
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| Blast search parameters | ||||
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