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Conserved domains on  [gi|665389201|ref|NP_001284795|]
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phosphoglycerate mutase 5, isoform B [Drosophila melanogaster]

Protein Classification

histidine phosphatase family protein( domain architecture ID 27749)

histidine phosphatase family protein contains a conserved His residue that is transiently phosphorylated during the catalytic cycle

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HP super family cl11399
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 43-277 5.66e-71

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.


The actual alignment was detected with superfamily member PTZ00122:

Pssm-ID: 472174  Cd Length: 299  Bit Score: 220.83  E-value: 5.66e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  43 PWAL-WDTNWDCREPRalvrplrnsqpeeenryNAELEKAKAKKARHIILVRHGEYLDVGDSDDTHH-LTERGRKQAEFT 120
Cdd:PTZ00122  75 PWNEdWDGNYKHRPKA-----------------RGKRADKSASHQRQIILVRHGQYINESSNDDNIKrLTELGKEQARIT 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 121 GKRLCELG---IKWDKVVA---STMVRAQETSDIILKQidFEKEKVVNCAFLREGAPIPPQPPVGHWKPEAS-FLRDGSR 193
Cdd:PTZ00122 138 GKYLKEQFgeiLVDKKVKAiyhSDMTRAKETAEIISEA--FPGVRLIEDPNLAEGVPCAPDPPSRGFKPTIEeILEDMKR 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 194 IEAGFRRYFHRayPDQEKESYTLIVGHGNVIRYFVCRALQFPAEGWLRININHASITWLTISPSGNVSIKYLGDSGFMPA 273
Cdd:PTZ00122 216 IEAAFEKYFHR--PVEDEDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPP 293


                 ....
gi 665389201 274 ELLT 277
Cdd:PTZ00122 294 DMVT 297
 
Name Accession Description Interval E-value
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 43-277 5.66e-71

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 220.83  E-value: 5.66e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  43 PWAL-WDTNWDCREPRalvrplrnsqpeeenryNAELEKAKAKKARHIILVRHGEYLDVGDSDDTHH-LTERGRKQAEFT 120
Cdd:PTZ00122  75 PWNEdWDGNYKHRPKA-----------------RGKRADKSASHQRQIILVRHGQYINESSNDDNIKrLTELGKEQARIT 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 121 GKRLCELG---IKWDKVVA---STMVRAQETSDIILKQidFEKEKVVNCAFLREGAPIPPQPPVGHWKPEAS-FLRDGSR 193
Cdd:PTZ00122 138 GKYLKEQFgeiLVDKKVKAiyhSDMTRAKETAEIISEA--FPGVRLIEDPNLAEGVPCAPDPPSRGFKPTIEeILEDMKR 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 194 IEAGFRRYFHRayPDQEKESYTLIVGHGNVIRYFVCRALQFPAEGWLRININHASITWLTISPSGNVSIKYLGDSGFMPA 273
Cdd:PTZ00122 216 IEAAFEKYFHR--PVEDEDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPP 293


                 ....
gi 665389201 274 ELLT 277
Cdd:PTZ00122 294 DMVT 297
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 88-264 6.75e-34

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: 120.89  E-value: 6.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  88 HIILVRHGEY------LDVGDSDDthHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQidFEKEKVV 161
Cdd:cd07067    1 RLYLVRHGESewnaegRFQGWTDV--PLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEE--LPGLPVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 162 NCAFLREgapippqppvghwkpeasflrdgSRIEAGFRRYFHRAypdqeKESYTLIVGHGNVIRYFVCRALQFPAEGWLR 241
Cdd:cd07067   77 VDPRLRE-----------------------ARVLPALEELIAPH-----DGKNVLIVSHGGVLRALLAYLLGLSDEDILR 128

                        170       180
                 ....*....|....*....|...
gi 665389201 242 ININHASITWLTISPSGNVSIKY 264
Cdd:cd07067  129 LNLPNGSISVLELDENGGGVLLL 151
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 89-267 1.31e-22

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: 92.27  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201   89 IILVRHGE--------YLDVGDSDdthhLTERGRKQAEFTGKRLceLGIKWDKVVASTMVRAQETSDIILKQIDFEKEKv 160
Cdd:pfam00300   1 LYLVRHGEtewnlegrFQGRTDSP----LTELGREQAEALAERL--AGEPFDAIYSSPLKRARQTAEIIAEALGLPVEI- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  161 vnCAFLRE-------GAPIP------PQPPVGHWKPEASFLRDG--------SRIEAGFRRYfHRAYPDQEkesyTLIVG 219
Cdd:pfam00300  74 --DPRLREidfgdweGLTFEeiaeryPEEYDAWLADPADYRPPGgesladvrARVRAALEEL-AARHPGKT----VLVVS 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 665389201  220 HGNVIRYFVCRALQFPAEGWLRININHASITWLTISPSGNVsIKYLGD 267
Cdd:pfam00300 147 HGGVIRALLAHLLGLPLEALRRFPLDNASLSILEFDGGGWV-LVLLND 193
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
87-266 1.09e-20

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 87.31  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  87 RHIILVRHGE-------YLDvGDSDDthHLTERGRKQAEFTGKRLceLGIKWDKVVASTMVRAQETSDIILKQIDFEkek 159
Cdd:COG0406    2 TRLYLVRHGEtewnaegRLQ-GRLDV--PLTELGRAQARALAERL--ADIPFDAVYSSPLQRARQTAEALAEALGLP--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 160 VVNCAFLRE--------------GAPIPPQPPVGHWKPEASFLRDG-------SRIEAGFRRYfHRAYPDQEkesyTLIV 218
Cdd:COG0406   74 VEVDPRLREidfgdwegltfaelEARYPEALAAWLADPAEFRPPGGesladvqARVRAALEEL-LARHPGGT----VLVV 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 665389201 219 GHGNVIRYFVCRALQFPAEGWLRININHASITWLTISPsGNVSIKYLG 266
Cdd:COG0406  149 THGGVIRALLAHLLGLPLEAFWRLRIDNASVTVLEFDD-GRWRLVALN 195
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 88-227 1.03e-14

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: 70.18  E-value: 1.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201    88 HIILVRHGE-------YLDvGDSDDthHLTERGRKQAEFTGKRL-CELGIKWDKVVASTMVRAQETSDIILKQIDFEKEK 159
Cdd:smart00855   1 RLYLIRHGEtewnregRLY-GDTDV--PLTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEALAIALGLPGLR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201   160 VVNCAFLR-----EGAPIPPQPPVGHWKPEASFLRDG-----------SRIEAGFRRYFHRAYPDQEKesyTLIVGHGNV 223
Cdd:smart00855  78 ERDFGAWEgltwdEIAAKYPEEYLAAWRDPYDPAPPAppggesladlvERVEPALDELIATADASGQN---VLIVSHGGV 154


                   ....
gi 665389201   224 IRYF 227
Cdd:smart00855 155 IRAL 158
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 89-252 3.67e-14

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: 69.19  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201   89 IILVRHGE--------Y--LDVGdsddthhLTERGRKQAEFTGKRLCelGIKWDKVVASTMVRAQETSDIILKQIDFEKE 158
Cdd:TIGR03162   1 LYLIRHGEtdvnaglcYgqTDVP-------LAESGEEQAAALREKLA--DVPFDAVYSSPLSRCRELAEILAERRGLPII 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  159 KVvncAFLRE-------GAP---IPPQPP--------VGHWKP---EaSFLRDGSRIEAGFRRYfHRAYPDQEkesyTLI 217
Cdd:TIGR03162  72 KD---DRLREmdfgdweGRSwdeIPEAYPeldawaadWQHARPpggE-SFADFYQRVSEFLEEL-LKAHEGDN----VLI 142

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 665389201  218 VGHGNVIRYFVCRALQFPAEGWLRININHASITWL 252
Cdd:TIGR03162 143 VTHGGVIRALLAHLLGLPLEQWWSFAVEYGSITLI 177
 
Name Accession Description Interval E-value
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 43-277 5.66e-71

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 220.83  E-value: 5.66e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  43 PWAL-WDTNWDCREPRalvrplrnsqpeeenryNAELEKAKAKKARHIILVRHGEYLDVGDSDDTHH-LTERGRKQAEFT 120
Cdd:PTZ00122  75 PWNEdWDGNYKHRPKA-----------------RGKRADKSASHQRQIILVRHGQYINESSNDDNIKrLTELGKEQARIT 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 121 GKRLCELG---IKWDKVVA---STMVRAQETSDIILKQidFEKEKVVNCAFLREGAPIPPQPPVGHWKPEAS-FLRDGSR 193
Cdd:PTZ00122 138 GKYLKEQFgeiLVDKKVKAiyhSDMTRAKETAEIISEA--FPGVRLIEDPNLAEGVPCAPDPPSRGFKPTIEeILEDMKR 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 194 IEAGFRRYFHRayPDQEKESYTLIVGHGNVIRYFVCRALQFPAEGWLRININHASITWLTISPSGNVSIKYLGDSGFMPA 273
Cdd:PTZ00122 216 IEAAFEKYFHR--PVEDEDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPP 293


                 ....
gi 665389201 274 ELLT 277
Cdd:PTZ00122 294 DMVT 297
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 88-264 6.75e-34

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: 120.89  E-value: 6.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  88 HIILVRHGEY------LDVGDSDDthHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQidFEKEKVV 161
Cdd:cd07067    1 RLYLVRHGESewnaegRFQGWTDV--PLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEE--LPGLPVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 162 NCAFLREgapippqppvghwkpeasflrdgSRIEAGFRRYFHRAypdqeKESYTLIVGHGNVIRYFVCRALQFPAEGWLR 241
Cdd:cd07067   77 VDPRLRE-----------------------ARVLPALEELIAPH-----DGKNVLIVSHGGVLRALLAYLLGLSDEDILR 128

                        170       180
                 ....*....|....*....|...
gi 665389201 242 ININHASITWLTISPSGNVSIKY 264
Cdd:cd07067  129 LNLPNGSISVLELDENGGGVLLL 151
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 88-265 7.41e-27

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: 102.49  E-value: 7.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  88 HIILVRHGE------YLDVGDSDDthHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQIDFEKEKVV 161
Cdd:cd07040    1 VLYLVRHGErepnaeGRFTGWGDG--PLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGLPVEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 162 NcaflregapippqppvghwkpeasflrDGSRIEAGFRRYFHRAYPDQEkesYTLIVGHGNVIRYFVCRALQFPAEGWLR 241
Cdd:cd07040   79 D---------------------------PRARVLNALLELLARHLLDGK---NVLIVSHGGTIRALLAALLGLSDEEILS 128

                        170       180
                 ....*....|....*....|....
gi 665389201 242 ININHASITWLTISPSGNVSIKYL 265
Cdd:cd07040  129 LNLPNGSILVLELDECGGKYVRLL 152
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 89-267 1.31e-22

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: 92.27  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201   89 IILVRHGE--------YLDVGDSDdthhLTERGRKQAEFTGKRLceLGIKWDKVVASTMVRAQETSDIILKQIDFEKEKv 160
Cdd:pfam00300   1 LYLVRHGEtewnlegrFQGRTDSP----LTELGREQAEALAERL--AGEPFDAIYSSPLKRARQTAEIIAEALGLPVEI- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  161 vnCAFLRE-------GAPIP------PQPPVGHWKPEASFLRDG--------SRIEAGFRRYfHRAYPDQEkesyTLIVG 219
Cdd:pfam00300  74 --DPRLREidfgdweGLTFEeiaeryPEEYDAWLADPADYRPPGgesladvrARVRAALEEL-AARHPGKT----VLVVS 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 665389201  220 HGNVIRYFVCRALQFPAEGWLRININHASITWLTISPSGNVsIKYLGD 267
Cdd:pfam00300 147 HGGVIRALLAHLLGLPLEALRRFPLDNASLSILEFDGGGWV-LVLLND 193
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
87-266 1.09e-20

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 87.31  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  87 RHIILVRHGE-------YLDvGDSDDthHLTERGRKQAEFTGKRLceLGIKWDKVVASTMVRAQETSDIILKQIDFEkek 159
Cdd:COG0406    2 TRLYLVRHGEtewnaegRLQ-GRLDV--PLTELGRAQARALAERL--ADIPFDAVYSSPLQRARQTAEALAEALGLP--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 160 VVNCAFLRE--------------GAPIPPQPPVGHWKPEASFLRDG-------SRIEAGFRRYfHRAYPDQEkesyTLIV 218
Cdd:COG0406   74 VEVDPRLREidfgdwegltfaelEARYPEALAAWLADPAEFRPPGGesladvqARVRAALEEL-LARHPGGT----VLVV 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 665389201 219 GHGNVIRYFVCRALQFPAEGWLRININHASITWLTISPsGNVSIKYLG 266
Cdd:COG0406  149 THGGVIRALLAHLLGLPLEAFWRLRIDNASVTVLEFDD-GRWRLVALN 195
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 88-227 1.03e-14

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: 70.18  E-value: 1.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201    88 HIILVRHGE-------YLDvGDSDDthHLTERGRKQAEFTGKRL-CELGIKWDKVVASTMVRAQETSDIILKQIDFEKEK 159
Cdd:smart00855   1 RLYLIRHGEtewnregRLY-GDTDV--PLTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEALAIALGLPGLR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201   160 VVNCAFLR-----EGAPIPPQPPVGHWKPEASFLRDG-----------SRIEAGFRRYFHRAYPDQEKesyTLIVGHGNV 223
Cdd:smart00855  78 ERDFGAWEgltwdEIAAKYPEEYLAAWRDPYDPAPPAppggesladlvERVEPALDELIATADASGQN---VLIVSHGGV 154


                   ....
gi 665389201   224 IRYF 227
Cdd:smart00855 155 IRAL 158
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
89-171 1.45e-14

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 69.52  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  89 IILVRHG--EYLDVGDSDDTHHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQIDFEkEKVVNCAFL 166
Cdd:COG2062    1 LILVRHAkaEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLP-PKVEVEDEL 79


                 ....*
gi 665389201 167 REGAP 171
Cdd:COG2062   80 YDADP 84
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 89-252 3.67e-14

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: 69.19  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201   89 IILVRHGE--------Y--LDVGdsddthhLTERGRKQAEFTGKRLCelGIKWDKVVASTMVRAQETSDIILKQIDFEKE 158
Cdd:TIGR03162   1 LYLIRHGEtdvnaglcYgqTDVP-------LAESGEEQAAALREKLA--DVPFDAVYSSPLSRCRELAEILAERRGLPII 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  159 KVvncAFLRE-------GAP---IPPQPP--------VGHWKP---EaSFLRDGSRIEAGFRRYfHRAYPDQEkesyTLI 217
Cdd:TIGR03162  72 KD---DRLREmdfgdweGRSwdeIPEAYPeldawaadWQHARPpggE-SFADFYQRVSEFLEEL-LKAHEGDN----VLI 142

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 665389201  218 VGHGNVIRYFVCRALQFPAEGWLRININHASITWL 252
Cdd:TIGR03162 143 VTHGGVIRALLAHLLGLPLEQWWSFAVEYGSITLI 177
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 89-158 9.35e-10

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 56.00  E-value: 9.35e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201   89 IILVRHGEYLDVGDSDDTHHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQIDFEKE 158
Cdd:TIGR00249   3 LFIMRHGDAALDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCLNLPSS 72
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 89-154 4.26e-07

Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-dependent) is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440353  Cd Length: 229  Bit Score: 49.69  E-value: 4.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665389201  89 IILVRHGE-----------YLDVGdsddthhLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQID 154
Cdd:COG0588    3 LVLLRHGEsewnlenrftgWTDVD-------LSEKGRAEAKRAGRLLKEAGFLFDVAYTSVLKRAIRTLWIVLDEMD 72
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 87-154 6.52e-07

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 48.92  E-value: 6.52e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665389201  87 RHIILVRHGEY------LDVG--DSDdthhLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQID 154
Cdd:PRK01295   3 RTLVLVRHGQSewnlknLFTGwrDPD----LTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLILEELG 74
PRK06193 PRK06193
hypothetical protein; Provisional
 84-220 3.20e-05

hypothetical protein; Provisional


Pssm-ID: 235734  Cd Length: 206  Bit Score: 43.91  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  84 KKARHIILVRHGE----YLDVGDSD-----DTHHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQid 154
Cdd:PRK06193  40 QKGGYVIYFRHAAtdrsQADQDTSDmddcsTQRNLSEEGREQARAIGEAFRALAIPVGKVISSPYCRAWETAQLAFGR-- 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665389201 155 FEKEKVVNcaFLregaPIPPQPPvghwkpeasflRDGSRIEAGFRRYFHRAyPDQEKEsyTLIVGH 220
Cdd:PRK06193 118 HEKEIRLN--FL----NSEPVPA-----------ERNALLKAGLRPLLTTP-PDPGTN--TVLVGH 163
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
91-250 1.02e-04

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 42.35  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201  91 LVRHGEY------LDVGDSDDThhLTERGRKQAEFTGKRLCelGIKWDKVVASTMVRAQETSDIIL--KQIDFEKEKVVN 162
Cdd:PRK15004   5 LVRHGETqanvdgLYSGHAPTP--LTARGIEQAQNLHTLLR--DVPFDLVLCSELERAQHTARLVLsdRQLPVHIIPELN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665389201 163 CAF-----LREGAPIPPQPP------VGHWKPEA-----SFLRDGSRIEAgfrryFHRAYPDQEKESYTLIVGHGNVIRY 226
Cdd:PRK15004  81 EMFfgdweMRHHRDLMQEDAenyaawCNDWQHAIptngeGFQAFSQRVER-----FIARLSAFQHYQNLLIVSHQGVLSL 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 665389201 227 FVCRALQFPAEG----------WLRININHASIT 250
Cdd:PRK15004 156 LIARLLGMPAEAmwhfrveqgcWSAIDINQGFAT 189
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
91-149 3.24e-04

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 40.87  E-value: 3.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665389201  91 LVRHGEYL-DV-----GDSDDThhLTERGRKQAEFTGKRLCELGIKwdKVVASTMVRAQETSDII 149
Cdd:PRK03482   6 LVRHGETQwNAerriqGQSDSP--LTAKGEQQAMQVAERAKELGIT--HIISSDLGRTRRTAEII 66
gpmA PRK14118
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
108-154 2.20e-03

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172608  Cd Length: 227  Bit Score: 38.80  E-value: 2.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 665389201 108 HLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQID 154
Cdd:PRK14118  26 NLTERGVEEAKAAGKKLKEAGYEFDIAFTSVLTRAIKTCNIVLEESN 72
gpmA PRK14119
phosphoglyceromutase; Provisional
 89-154 6.21e-03

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 37.18  E-value: 6.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665389201  89 IILVRHG------EYLDVGDSDdtHHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQID 154
Cdd:PRK14119   4 LILCRHGqsewnaKNLFTGWED--VNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTTHYILTESK 73
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
87-154 7.27e-03

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 37.15  E-value: 7.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665389201  87 RHIILVRHGE-----------YLDVGdsddthhLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQID 154
Cdd:PRK14115   1 TKLVLIRHGEsqwnkenrftgWTDVD-------LSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTLWIVLDELD 72
gpmA PRK14120
phosphoglyceromutase; Provisional
 89-154 8.65e-03

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 36.94  E-value: 8.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665389201  89 IILVRHGE-----------YLDVgdsddthHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQID 154
Cdd:PRK14120   7 LVLLRHGEsewnaknlftgWVDV-------DLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRTANLALDAAD 76
 
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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