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Conserved domains on  [gi|15609556|ref|NP_216935|]
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glucosyl-3-phosphoglycerate phosphatase [Mycobacterium tuberculosis H37Rv]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10001383)

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

CATH:  3.40.50.1240
Gene Ontology:  GO:0016791
PubMed:  18092946
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
4-213 3.32e-49

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


:

Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 159.34  E-value: 3.32e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   4 RRLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKRQPLLIVSSDLRRAYDTAVKLGERTGLVVRVDTRLR 83
Cdd:COG0406   2 TRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPRLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556  84 ETHLGDWQGLTHAQIDADAPGARLAWRED-ATWAPHGGESRVDVAARSRPLVAELVASepewggadEPDRPVVLVAHGGL 162
Cdd:COG0406  82 EIDFGDWEGLTFAELEARYPEALAAWLADpAEFRPPGGESLADVQARVRAALEELLAR--------HPGGTVLVVTHGGV 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15609556 163 IAALSAALLKLPVANWPALgGMGNASWTQLsghwapgsDFESIRWRLDVWN 213
Cdd:COG0406 154 IRALLAHLLGLPLEAFWRL-RIDNASVTVL--------EFDDGRWRLVALN 195
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
4-213 3.32e-49

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 159.34  E-value: 3.32e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   4 RRLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKRQPLLIVSSDLRRAYDTAVKLGERTGLVVRVDTRLR 83
Cdd:COG0406   2 TRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPRLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556  84 ETHLGDWQGLTHAQIDADAPGARLAWRED-ATWAPHGGESRVDVAARSRPLVAELVASepewggadEPDRPVVLVAHGGL 162
Cdd:COG0406  82 EIDFGDWEGLTFAELEARYPEALAAWLADpAEFRPPGGESLADVQARVRAALEELLAR--------HPGGTVLVVTHGGV 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15609556 163 IAALSAALLKLPVANWPALgGMGNASWTQLsghwapgsDFESIRWRLDVWN 213
Cdd:COG0406 154 IRALLAHLLGLPLEAFWRL-RIDNASVTVL--------EFDDGRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-213 4.17e-49

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: 158.91  E-value: 4.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556     6 LVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKRQPLLIVSSDLRRAYDTAVKLGERTGLVVRVDTRLRET 85
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRLREI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    86 HLGDWQGLTHAQIDADAPGARLAWRED-ATWAPHGGESRVDVAARSRPLVAELVasepewggADEPDRPVVLVAHGGLIA 164
Cdd:pfam00300  81 DFGDWEGLTFEEIAERYPEEYDAWLADpADYRPPGGESLADVRARVRAALEELA--------ARHPGKTVLVVSHGGVIR 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 15609556   165 ALSAALLKLPVANWPALgGMGNASWTQLsghwapgsDFESIRWRLDVWN 213
Cdd:pfam00300 153 ALLAHLLGLPLEALRRF-PLDNASLSIL--------EFDGGGWVLVLLN 192
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 5-161 5.04e-34

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 119.10  E-value: 5.04e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556      5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVL---GKRQPLLIVSSDLRRAYDTAVKLGERTGLvvrvdTR 81
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLaslLLPRFDVVYSSPLKRARQTAEALAIALGL-----PG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556     82 LRETHLGDWQGLTHAQIDADAPGARLA-WREDATW---APHGGESRVDVAARSRPLVAELVASepewggADEPDRPVVLV 157
Cdd:smart00855  76 LRERDFGAWEGLTWDEIAAKYPEEYLAaWRDPYDPappAPPGGESLADLVERVEPALDELIAT------ADASGQNVLIV 149


                   ....
gi 15609556    158 AHGG 161
Cdd:smart00855 150 SHGG 153
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 5-159 2.99e-33

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 122.78  E-value: 2.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKRQPL-LIVSSDLRRAYDTAVKLGERTGLVVRVDTRLR 83
Cdd:PRK07238 173 RLLLLRHGQTELSVQRRYSGRGNPELTEVGRRQAAAAARYLAARGGIdAVVSSPLQRARDTAAAAAKALGLDVTVDDDLI 252

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15609556   84 ETHLGDWQGLTHAQIDADAPGARLAWREDATWAPHGGESRVDVAARSRPLVAELVAsepEWGGADepdrpVVLVAH 159
Cdd:PRK07238 253 ETDFGAWEGLTFAEAAERDPELHRAWLADTSVAPPGGESFDAVARRVRRARDRLIA---EYPGAT-----VLVVSH 320
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 6-161 5.28e-31

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 111.95  E-value: 5.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556     6 LVMLRHGQTDYNVGSRMqGQLDTELSELGRTQAVAAAEVLGKRQPLLIVSSDLRRAYDTAVKLGERTGLVVRVDTRLRET 85
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCY-GQTDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAERRGLPIIKDDRLREM 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15609556    86 HLGDWQGLTHAQIDADAPGARlAWRED-ATWAPHGGESRVDVAARSRPLVAELVASepewggadEPDRPVVLVAHGG 161
Cdd:TIGR03162  80 DFGDWEGRSWDEIPEAYPELD-AWAADwQHARPPGGESFADFYQRVSEFLEELLKA--------HEGDNVLIVTHGG 147
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 5-84 8.17e-21

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 84.68  E-value: 8.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKR--QPLLIVSSDLRRAYDTAVKLGE-RTGLVVRVDTR 81
Cdd:cd07067   1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELgiKFDRIYSSPLKRAIQTAEIILEeLPGLPVEVDPR 80


                ...
gi 15609556  82 LRE 84
Cdd:cd07067  81 LRE 83
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
4-213 3.32e-49

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 159.34  E-value: 3.32e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   4 RRLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKRQPLLIVSSDLRRAYDTAVKLGERTGLVVRVDTRLR 83
Cdd:COG0406   2 TRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPRLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556  84 ETHLGDWQGLTHAQIDADAPGARLAWRED-ATWAPHGGESRVDVAARSRPLVAELVASepewggadEPDRPVVLVAHGGL 162
Cdd:COG0406  82 EIDFGDWEGLTFAELEARYPEALAAWLADpAEFRPPGGESLADVQARVRAALEELLAR--------HPGGTVLVVTHGGV 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15609556 163 IAALSAALLKLPVANWPALgGMGNASWTQLsghwapgsDFESIRWRLDVWN 213
Cdd:COG0406 154 IRALLAHLLGLPLEAFWRL-RIDNASVTVL--------EFDDGRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-213 4.17e-49

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: 158.91  E-value: 4.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556     6 LVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKRQPLLIVSSDLRRAYDTAVKLGERTGLVVRVDTRLRET 85
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRLREI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    86 HLGDWQGLTHAQIDADAPGARLAWRED-ATWAPHGGESRVDVAARSRPLVAELVasepewggADEPDRPVVLVAHGGLIA 164
Cdd:pfam00300  81 DFGDWEGLTFEEIAERYPEEYDAWLADpADYRPPGGESLADVRARVRAALEELA--------ARHPGKTVLVVSHGGVIR 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 15609556   165 ALSAALLKLPVANWPALgGMGNASWTQLsghwapgsDFESIRWRLDVWN 213
Cdd:pfam00300 153 ALLAHLLGLPLEALRRF-PLDNASLSIL--------EFDGGGWVLVLLN 192
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 5-161 5.04e-34

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 119.10  E-value: 5.04e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556      5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVL---GKRQPLLIVSSDLRRAYDTAVKLGERTGLvvrvdTR 81
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLaslLLPRFDVVYSSPLKRARQTAEALAIALGL-----PG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556     82 LRETHLGDWQGLTHAQIDADAPGARLA-WREDATW---APHGGESRVDVAARSRPLVAELVASepewggADEPDRPVVLV 157
Cdd:smart00855  76 LRERDFGAWEGLTWDEIAAKYPEEYLAaWRDPYDPappAPPGGESLADLVERVEPALDELIAT------ADASGQNVLIV 149


                   ....
gi 15609556    158 AHGG 161
Cdd:smart00855 150 SHGG 153
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 5-159 2.99e-33

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 122.78  E-value: 2.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKRQPL-LIVSSDLRRAYDTAVKLGERTGLVVRVDTRLR 83
Cdd:PRK07238 173 RLLLLRHGQTELSVQRRYSGRGNPELTEVGRRQAAAAARYLAARGGIdAVVSSPLQRARDTAAAAAKALGLDVTVDDDLI 252

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15609556   84 ETHLGDWQGLTHAQIDADAPGARLAWREDATWAPHGGESRVDVAARSRPLVAELVAsepEWGGADepdrpVVLVAH 159
Cdd:PRK07238 253 ETDFGAWEGLTFAEAAERDPELHRAWLADTSVAPPGGESFDAVARRVRRARDRLIA---EYPGAT-----VLVVSH 320
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 6-161 5.28e-31

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 111.95  E-value: 5.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556     6 LVMLRHGQTDYNVGSRMqGQLDTELSELGRTQAVAAAEVLGKRQPLLIVSSDLRRAYDTAVKLGERTGLVVRVDTRLRET 85
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCY-GQTDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAERRGLPIIKDDRLREM 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15609556    86 HLGDWQGLTHAQIDADAPGARlAWRED-ATWAPHGGESRVDVAARSRPLVAELVASepewggadEPDRPVVLVAHGG 161
Cdd:TIGR03162  80 DFGDWEGRSWDEIPEAYPELD-AWAADwQHARPPGGESFADFYQRVSEFLEELLKA--------HEGDNVLIVTHGG 147
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 5-84 8.17e-21

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 84.68  E-value: 8.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKR--QPLLIVSSDLRRAYDTAVKLGE-RTGLVVRVDTR 81
Cdd:cd07067   1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELgiKFDRIYSSPLKRAIQTAEIILEeLPGLPVEVDPR 80


                ...
gi 15609556  82 LRE 84
Cdd:cd07067  81 LRE 83
PRK13462 PRK13462
acid phosphatase; Provisional
 5-160 1.31e-17

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 77.56  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGK---RQPlLIVSSDLRRAYDTAvklgERTGLVV-RVDT 80
Cdd:PRK13462   7 RLLLLRHGETEWSKSGRHTGRTELELTETGRTQAELAGQALGElelDDP-LVISSPRRRALDTA----KLAGLTVdEVSG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   81 RLRETHLGDWQGLTHAQIDADAPGArLAWredaTWAPHGGESRVDVAARSRPLVAeLVASEPEwggadepDRPVVLVAHG 160
Cdd:PRK13462  82 LLAEWDYGSYEGLTTPQIRESEPDW-LVW----THGCPGGESVAQVNERADRAVA-LALEHME-------SRDVVFVSHG 148
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 5-83 1.90e-16

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


Pssm-ID: 132716 [Multi-domain]  Cd Length: 153  Bit Score: 73.22  E-value: 1.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKR--QPLLIVSSDLRRAYDTAVKLGE--RTGLVVRVDT 80
Cdd:cd07040   1 VLYLVRHGEREPNAEGRFTGWGDGPLTEKGRQQARELGKALRERyiKFDRIYSSPLKRAIQTAEIILEglFEGLPVEVDP 80


                ...
gi 15609556  81 RLR 83
Cdd:cd07040  81 RAR 83
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
5-161 1.75e-15

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 72.01  E-value: 1.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKRQPLLIVSSDLRRAYDTAVKLGERTGLVVRVDTRLRE 84
Cdd:PRK15004   2 RLWLVRHGETQANVDGLYSGHAPTPLTARGIEQAQNLHTLLRDVPFDLVLCSELERAQHTARLVLSDRQLPVHIIPELNE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   85 THLGDWQGLTHAQIDADAPGARLAWREDatW---APHGGESRVDVAARSRPLVAELVASEPEwggadepdRPVVLVAHGG 161
Cdd:PRK15004  82 MFFGDWEMRHHRDLMQEDAENYAAWCND--WqhaIPTNGEGFQAFSQRVERFIARLSAFQHY--------QNLLIVSHQG 151
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-160 1.83e-11

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 61.59  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    1 MRARRLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKRQ--PLLIVSSDLRRAYDTA---VKLGERTGLV 75
Cdd:PRK14120   2 MMTYTLVLLRHGESEWNAKNLFTGWVDVDLTEKGEAEAKRGGELLAEAGvlPDVVYTSLLRRAIRTAnlaLDAADRLWIP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   76 VRVDTRLRETHLGDWQGLTHAQIDAD-APGARLAWR----------EDATWAPHGGESR---VDVAARSRPLVAELVASE 141
Cdd:PRK14120  82 VRRSWRLNERHYGALQGKDKAETKAEyGEEQFMLWRrsydtppppiEDGSEYSQDNDPRyadLGVGPRTECLKDVVARFL 161

                        170       180
                 ....*....|....*....|...
gi 15609556  142 PEWGGADEPD----RPVVLVAHG 160
Cdd:PRK14120 162 PYWEDDIVPDlkagKTVLIAAHG 184
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 4-132 6.46e-11

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 59.70  E-value: 6.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    4 RRLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLgKRQPL---LIVSSDLRRAYDTA-VKLGE--RTGLVVR 77
Cdd:PRK01295   3 RTLVLVRHGQSEWNLKNLFTGWRDPDLTEQGVAEAKAAGRKL-KAAGLkfdIAFTSALSRAQHTCqLILEElgQPGLETI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15609556   78 VDTRLRETHLGDWQGLTHAqiDADAPGAR---LAWREDATWAPHGGESRVDVAARSRP 132
Cdd:PRK01295  82 RDQALNERDYGDLSGLNKD--DARAKWGEeqvHIWRRSYDVPPPGGESLKDTGARVLP 137
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
8-88 6.65e-11

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 59.74  E-value: 6.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    8 MLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKRQPLLIVSSDLRRAYDTAVKLGERTGLVVRVDTRLRETHL 87
Cdd:PRK03482   6 LVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAEIIAQACGCDIIFDPRLRELNM 85


                 .
gi 15609556   88 G 88
Cdd:PRK03482  86 G 86
PRK13463 PRK13463
phosphoserine phosphatase 1;
10-129 2.55e-10

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 57.75  E-value: 2.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   10 RHGQTDYNVGSRMQGQLDTELSELGRTQavaaAEVLGKRQPLL----IVSSDLRRAYDTAVKL-GERTgLVVRVDTRLRE 84
Cdd:PRK13463   9 RHGETEWNVAKRMQGRKNSALTENGILQ----AKQLGERMKDLsihaIYSSPSERTLHTAELIkGERD-IPIIADEHFYE 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15609556   85 THLGDWQGLTHAQIDADAP-GARLAWREDATWAPHGGESRVDVAAR 129
Cdd:PRK13463  84 INMGIWEGQTIDDIERQYPdDIQLFWNEPHLFQSTSGENFEAVHKR 129
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
4-93 5.99e-08

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 51.40  E-value: 5.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    4 RRLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKR--QPLLIVSSDLRRAYDT---AVKLGERTGLVVRV 78
Cdd:PRK14115   1 TKLVLIRHGESQWNKENRFTGWTDVDLSEKGVSEAKAAGKLLKEEgyTFDVAYTSVLKRAIRTlwiVLDELDQMWLPVEK 80

                         90
                 ....*....|....*
gi 15609556   79 DTRLRETHLGDWQGL 93
Cdd:PRK14115  81 SWRLNERHYGALQGL 95
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
5-132 1.86e-07

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 50.10  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLgKRQPL-LIVSSDLRRAYDTAV-KLGERTG--------- 73
Cdd:PRK01112   3 LLILLRHGQSVWNAKNLFTGWVDIPLSQQGIAEAIAAGEKI-KDLPIdCIFTSTLVRSLMTALlAMTNHSSgkipyivhe 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   74 -------------------LVVRVDTRLRETHLGDWQGLTHAQIdADAPGARLA--WREDATWAPHGGESRVDVAARSRP 132
Cdd:PRK01112  82 eddkkwmsriysdeepeqmIPLFQSSALNERMYGELQGKNKAET-AEKFGEEQVklWRRSYKTAPPQGESLEDTGQRTLP 160
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
6-90 7.18e-06

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 44.48  E-value: 7.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   6 LVMLRHGQTDynvgSRMQGQLDTE--LSELGRTQAVAAAEVLGKR--QPLLIVSSDLRRAYDTAVKLGERTGLV--VRVD 79
Cdd:COG2062   1 LILVRHAKAE----WRAPGGDDFDrpLTERGRRQARAMARWLAALglKPDRILSSPALRARQTAEILAEALGLPpkVEVE 76

                        90
                ....*....|.
gi 15609556  80 TRLRETHLGDW 90
Cdd:COG2062  77 DELYDADPEDL 87
gpmA PRK14117
phosphoglyceromutase; Provisional
 5-97 7.37e-06

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 45.40  E-value: 7.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKR--QPLLIVSSDLRRAYDT---AVKLGERTGLVVRVD 79
Cdd:PRK14117   3 KLVFARHGESEWNKANLFTGWADVDLSEKGTQQAIDAGKLIKEAgiEFDLAFTSVLKRAIKTtnlALEASDQLWVPVEKS 82

                         90
                 ....*....|....*...
gi 15609556   80 TRLRETHLGDWQGLTHAQ 97
Cdd:PRK14117  83 WRLNERHYGGLTGKNKAE 100
gpmA PRK14119
phosphoglyceromutase; Provisional
 5-93 8.22e-06

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 45.27  E-value: 8.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKRQPLLIV--SSDLRRAYDTAVKLGERTG---LVVRVD 79
Cdd:PRK14119   3 KLILCRHGQSEWNAKNLFTGWEDVNLSEQGINEATRAGEKVRENNIAIDVafTSLLTRALDTTHYILTESKqqwIPVYKS 82

                         90
                 ....*....|....
gi 15609556   80 TRLRETHLGDWQGL 93
Cdd:PRK14119  83 WRLNERHYGGLQGL 96
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
5-97 9.95e-06

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 44.90  E-value: 9.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    5 RLVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLgKRQPLLI---VSSDLRRAYDTAVKLGERTGLVVRVDT- 80
Cdd:PRK14116   3 KLVLIRHGQSEWNLSNQFTGWVDVDLSEKGVEEAKKAGRLI-KEAGLEFdqaYTSVLTRAIKTLHYALEESDQLWIPETk 81

                         90
                 ....*....|....*....
gi 15609556   81 --RLRETHLGDWQGLTHAQ 97
Cdd:PRK14116  82 twRLNERHYGALQGLNKKE 100
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
 16-93 8.20e-04

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 39.26  E-value: 8.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556   16 YNVGSRMQGQLDTELSELGRTQAVAAAEVLgKRQPL---LIVSSDLRRAYDTAVKLGERTGL----VVRvDTRLRETHLG 88
Cdd:PTZ00123   1 WNKENRFTGWTDVPLSEKGVQEAREAGKLL-KEKGFrfdVVYTSVLKRAIKTAWIVLEELGQlhvpVIK-SWRLNERHYG 78


                 ....*
gi 15609556   89 DWQGL 93
Cdd:PTZ00123  79 ALQGL 83
gpmA PRK14118
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
6-97 9.37e-04

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172608  Cd Length: 227  Bit Score: 39.19  E-value: 9.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609556    6 LVMLRHGQTDYNVGSRMQGQLDTELSELGRTQAVAAAEVLGKR--QPLLIVSSDLRRAYDTA-VKLGERTGL-VVRVDT- 80
Cdd:PRK14118   3 LVFIRHGFSEWNAKNLFTGWRDVNLTERGVEEAKAAGKKLKEAgyEFDIAFTSVLTRAIKTCnIVLEESNQLwIPQVKNw 82

                         90
                 ....*....|....*..
gi 15609556   81 RLRETHLGDWQGLTHAQ 97
Cdd:PRK14118  83 RLNERHYGALQGLDKKA 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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