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Conserved domains on  [gi|1806256999|dbj|BBX46920|]
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phosphoglycerate mutase [Mycobacterium cookii]

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

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];
1-187 3.93e-40

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


:

Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 135.46  E-value: 3.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   1 MQLLLVRHALPHRSEPGE---GADPVLSDEGRAQVARLPDALARYPISRVISSPQRRAVQTAEPVAAARGLTVEIDDRFA 77
Cdd:COG0406     2 TRLYLVRHGETEWNAEGRlqgRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPRLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  78 EYDRELPVYIPIEQIRAENPQEWARMAEGHLPSSVDE----DAFRARVRAAVDHVAvTADHDDTVAVFSHGGVINVVLHE 153
Cdd:COG0406    82 EIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGgeslADVQARVRAALEELL-ARHPGGTVLVVTHGGVIRALLAH 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1806256999 154 ILGTR--RILSFPIDYVSVTRLLFSRsGQASVVAVN 187
Cdd:COG0406   161 LLGLPleAFWRLRIDNASVTVLEFDD-GRWRLVALN 195
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-187 3.93e-40

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 135.46  E-value: 3.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   1 MQLLLVRHALPHRSEPGE---GADPVLSDEGRAQVARLPDALARYPISRVISSPQRRAVQTAEPVAAARGLTVEIDDRFA 77
Cdd:COG0406     2 TRLYLVRHGETEWNAEGRlqgRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPRLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  78 EYDRELPVYIPIEQIRAENPQEWARMAEGHLPSSVDE----DAFRARVRAAVDHVAvTADHDDTVAVFSHGGVINVVLHE 153
Cdd:COG0406    82 EIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGgeslADVQARVRAALEELL-ARHPGGTVLVVTHGGVIRALLAH 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1806256999 154 ILGTR--RILSFPIDYVSVTRLLFSRsGQASVVAVN 187
Cdd:COG0406   161 LLGLPleAFWRLRIDNASVTVLEFDD-GRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 3-187 4.45e-37

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: 127.71  E-value: 4.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   3 LLLVRHA---LPHRSEPGEGADPVLSDEGRAQVARLPDALARYPISRVISSPQRRAVQTAEPVAAARGLTVEIDDRFAEY 79
Cdd:pfam00300   1 LYLVRHGeteWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRLREI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  80 DreLPVY--IPIEQIRAENPQE----WARMAEGHLPSSVDEDAFRARVRAAVDHVaVTADHDDTVAVFSHGGVINVVLHE 153
Cdd:pfam00300  81 D--FGDWegLTFEEIAERYPEEydawLADPADYRPPGGESLADVRARVRAALEEL-AARHPGKTVLVVSHGGVIRALLAH 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1806256999 154 ILGT--RRILSFPIDYVSVTRLLFSRsGQASVVAVN 187
Cdd:pfam00300 158 LLGLplEALRRFPLDNASLSILEFDG-GGWVLVLLN 192
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 3-173 1.32e-20

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: 84.60  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   3 LLLVRHAlphrsEPGEGA-------DPVLSDEGRAQVARLPDALARYPISRVISSPQRRAVQTAEPVAAARGLTVEIDDR 75
Cdd:TIGR03162   1 LYLIRHG-----ETDVNAglcygqtDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAERRGLPIIKDDR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  76 FAEYD---------RELPVYIPIEQIRAENPQeWARMAEGHLPSsvdedAFRARVRAAVDHVAVtADHDDTVAVFSHGGV 146
Cdd:TIGR03162  76 LREMDfgdwegrswDEIPEAYPELDAWAADWQ-HARPPGGESFA-----DFYQRVSEFLEELLK-AHEGDNVLIVTHGGV 148

                         170       180
                  ....*....|....*....|....*....
gi 1806256999 147 INVVLHEILG--TRRILSFPIDYVSVTRL 173
Cdd:TIGR03162 149 IRALLAHLLGlpLEQWWSFAVEYGSITLI 177
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 2-184 4.72e-19

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: 80.06  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   2 QLLLVRHALPHRSEPGE---GADPVLSDEGRAQVARLPDALAR--YPISRVISSPQRRAVQTAEPVAAAR-GLTVEIDDR 75
Cdd:cd07067     1 RLYLVRHGESEWNAEGRfqgWTDVPLTEKGREQARALGKRLKElgIKFDRIYSSPLKRAIQTAEIILEELpGLPVEVDPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  76 FAEydrelpvyipieqiraenpqewarmaeghlpssvdedafrARVRAAVDHVAVTADhDDTVAVFSHGGVINVVLHEIL 155
Cdd:cd07067    81 LRE----------------------------------------ARVLPALEELIAPHD-GKNVLIVSHGGVLRALLAYLL 119

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1806256999 156 G--TRRILSFPIDYVSVTRLLFSRSGQASVV 184
Cdd:cd07067   120 GlsDEDILRLNLPNGSISVLELDENGGGVLL 150
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 2-150 5.23e-17

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: 74.80  E-value: 5.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999    2 QLLLVRHALPHRSEPG---EGADPVLSDEGRAQVARLPDALARY---PISRVISSPQRRAVQTAEPVAAARGLtveidDR 75
Cdd:smart00855   1 RLYLIRHGETEWNREGrlyGDTDVPLTELGRAQAEALGRLLASLllpRFDVVYSSPLKRARQTAEALAIALGL-----PG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   76 FAEydRELPVY--IPIEQIRAENPQEWARMAEGHLPSSVDE-------DAFRARVRAAVDHVAVTAD-HDDTVAVFSHGG 145
Cdd:smart00855  76 LRE--RDFGAWegLTWDEIAAKYPEEYLAAWRDPYDPAPPAppggeslADLVERVEPALDELIATADaSGQNVLIVSHGG 153


                   ....*
gi 1806256999  146 VINVV 150
Cdd:smart00855 154 VIRAL 158
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 3-191 8.48e-15

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 71.93  E-value: 8.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   3 LLLVRH---AL-PHRSEPGEGaDPVLSDEGRAQVARLPDALA-RYPISRVISSPQRRAVQTAEPVAAARGLTVEIDDRFA 77
Cdd:PRK07238  174 LLLLRHgqtELsVQRRYSGRG-NPELTEVGRRQAAAAARYLAaRGGIDAVVSSPLQRARDTAAAAAKALGLDVTVDDDLI 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  78 EYDRELPVYIPIEQIRAENPQEWAR-MAEGHLPSSVDE--DAFRARVRAAVDhvAVTADHD-DTVAVFSHGGVINVVLHE 153
Cdd:PRK07238  253 ETDFGAWEGLTFAEAAERDPELHRAwLADTSVAPPGGEsfDAVARRVRRARD--RLIAEYPgATVLVVSHVTPIKTLLRL 330

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1806256999 154 ILGT-----RRIlsfPIDYVSVTRLLFSRSGQASVVAVNGTEH 191
Cdd:PRK07238  331 ALDAgpgvlYRL---HLDLASLSIAEFYPDGPASVRLVNDTSH 370
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-187 3.93e-40

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 135.46  E-value: 3.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   1 MQLLLVRHALPHRSEPGE---GADPVLSDEGRAQVARLPDALARYPISRVISSPQRRAVQTAEPVAAARGLTVEIDDRFA 77
Cdd:COG0406     2 TRLYLVRHGETEWNAEGRlqgRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPRLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  78 EYDRELPVYIPIEQIRAENPQEWARMAEGHLPSSVDE----DAFRARVRAAVDHVAvTADHDDTVAVFSHGGVINVVLHE 153
Cdd:COG0406    82 EIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGgeslADVQARVRAALEELL-ARHPGGTVLVVTHGGVIRALLAH 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1806256999 154 ILGTR--RILSFPIDYVSVTRLLFSRsGQASVVAVN 187
Cdd:COG0406   161 LLGLPleAFWRLRIDNASVTVLEFDD-GRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 3-187 4.45e-37

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: 127.71  E-value: 4.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   3 LLLVRHA---LPHRSEPGEGADPVLSDEGRAQVARLPDALARYPISRVISSPQRRAVQTAEPVAAARGLTVEIDDRFAEY 79
Cdd:pfam00300   1 LYLVRHGeteWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRLREI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  80 DreLPVY--IPIEQIRAENPQE----WARMAEGHLPSSVDEDAFRARVRAAVDHVaVTADHDDTVAVFSHGGVINVVLHE 153
Cdd:pfam00300  81 D--FGDWegLTFEEIAERYPEEydawLADPADYRPPGGESLADVRARVRAALEEL-AARHPGKTVLVVSHGGVIRALLAH 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1806256999 154 ILGT--RRILSFPIDYVSVTRLLFSRsGQASVVAVN 187
Cdd:pfam00300 158 LLGLplEALRRFPLDNASLSILEFDG-GGWVLVLLN 192
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 3-173 1.32e-20

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: 84.60  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   3 LLLVRHAlphrsEPGEGA-------DPVLSDEGRAQVARLPDALARYPISRVISSPQRRAVQTAEPVAAARGLTVEIDDR 75
Cdd:TIGR03162   1 LYLIRHG-----ETDVNAglcygqtDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAERRGLPIIKDDR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  76 FAEYD---------RELPVYIPIEQIRAENPQeWARMAEGHLPSsvdedAFRARVRAAVDHVAVtADHDDTVAVFSHGGV 146
Cdd:TIGR03162  76 LREMDfgdwegrswDEIPEAYPELDAWAADWQ-HARPPGGESFA-----DFYQRVSEFLEELLK-AHEGDNVLIVTHGGV 148

                         170       180
                  ....*....|....*....|....*....
gi 1806256999 147 INVVLHEILG--TRRILSFPIDYVSVTRL 173
Cdd:TIGR03162 149 IRALLAHLLGlpLEQWWSFAVEYGSITLI 177
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 2-184 4.72e-19

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: 80.06  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   2 QLLLVRHALPHRSEPGE---GADPVLSDEGRAQVARLPDALAR--YPISRVISSPQRRAVQTAEPVAAAR-GLTVEIDDR 75
Cdd:cd07067     1 RLYLVRHGESEWNAEGRfqgWTDVPLTEKGREQARALGKRLKElgIKFDRIYSSPLKRAIQTAEIILEELpGLPVEVDPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  76 FAEydrelpvyipieqiraenpqewarmaeghlpssvdedafrARVRAAVDHVAVTADhDDTVAVFSHGGVINVVLHEIL 155
Cdd:cd07067    81 LRE----------------------------------------ARVLPALEELIAPHD-GKNVLIVSHGGVLRALLAYLL 119

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1806256999 156 G--TRRILSFPIDYVSVTRLLFSRSGQASVV 184
Cdd:cd07067   120 GlsDEDILRLNLPNGSISVLELDENGGGVLL 150
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 2-150 5.23e-17

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: 74.80  E-value: 5.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999    2 QLLLVRHALPHRSEPG---EGADPVLSDEGRAQVARLPDALARY---PISRVISSPQRRAVQTAEPVAAARGLtveidDR 75
Cdd:smart00855   1 RLYLIRHGETEWNREGrlyGDTDVPLTELGRAQAEALGRLLASLllpRFDVVYSSPLKRARQTAEALAIALGL-----PG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   76 FAEydRELPVY--IPIEQIRAENPQEWARMAEGHLPSSVDE-------DAFRARVRAAVDHVAVTAD-HDDTVAVFSHGG 145
Cdd:smart00855  76 LRE--RDFGAWegLTWDEIAAKYPEEYLAAWRDPYDPAPPAppggeslADLVERVEPALDELIATADaSGQNVLIVSHGG 153


                   ....*
gi 1806256999  146 VINVV 150
Cdd:smart00855 154 VIRAL 158
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 3-191 8.48e-15

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 71.93  E-value: 8.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   3 LLLVRH---AL-PHRSEPGEGaDPVLSDEGRAQVARLPDALA-RYPISRVISSPQRRAVQTAEPVAAARGLTVEIDDRFA 77
Cdd:PRK07238  174 LLLLRHgqtELsVQRRYSGRG-NPELTEVGRRQAAAAARYLAaRGGIDAVVSSPLQRARDTAAAAAKALGLDVTVDDDLI 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  78 EYDRELPVYIPIEQIRAENPQEWAR-MAEGHLPSSVDE--DAFRARVRAAVDhvAVTADHD-DTVAVFSHGGVINVVLHE 153
Cdd:PRK07238  253 ETDFGAWEGLTFAEAAERDPELHRAwLADTSVAPPGGEsfDAVARRVRRARD--RLIAEYPgATVLVVSHVTPIKTLLRL 330

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1806256999 154 ILGT-----RRIlsfPIDYVSVTRLLFSRSGQASVVAVNGTEH 191
Cdd:PRK07238  331 ALDAgpgvlYRL---HLDLASLSIAEFYPDGPASVRLVNDTSH 370
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 2-187 3.43e-13

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: 64.36  E-value: 3.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   2 QLLLVRHAlphRSEP------GEGADPVLSDEGRAQVARLPDALAR--YPISRVISSPQRRAVQTAEPVAAargltveid 73
Cdd:cd07040     1 VLYLVRHG---EREPnaegrfTGWGDGPLTEKGRQQARELGKALREryIKFDRIYSSPLKRAIQTAEIILE--------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  74 drfaeydrELPVYIPIEQIRaenpqewarmaeghlpssvdedafRARVRAAV-DHVAVTADHDDTVAVFSHGGVINVVLH 152
Cdd:cd07040    69 --------GLFEGLPVEVDP------------------------RARVLNALlELLARHLLDGKNVLIVSHGGTIRALLA 116

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1806256999 153 EILGT--RRILSFPIDYVSVTRLLFSRSGQASVVAVN 187
Cdd:cd07040   117 ALLGLsdEEILSLNLPNGSILVLELDECGGKYVRLLN 153
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
3-164 1.47e-12

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 62.58  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   3 LLLVRHAlphRSEPGEG----ADPVLSDEGRAQVARLPDALARY--PISRVISSPQRRAVQTAEPVAAARGLTVEIddrf 76
Cdd:COG2062     1 LILVRHA---KAEWRAPggddFDRPLTERGRRQARAMARWLAALglKPDRILSSPALRARQTAEILAEALGLPPKV---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  77 aeydrelpvyipieqiraenpQEWARMAEGhlpssvDEDAFRARVRAavdhvavtADHDDTVAVFSHGGVINVVLHEILG 156
Cdd:COG2062    74 ---------------------EVEDELYDA------DPEDLLDLLRE--------LDDGETVLLVGHNPGLSELAALLAG 118


                  ....*...
gi 1806256999 157 TRRILSFP 164
Cdd:COG2062   119 GEPLDGFP 126
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
1-156 3.31e-07

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 48.89  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   1 MQLLLVRHALPHRSEPG---EGADPVLSDEGRAQVARLPDALARYPISRVISSPQRRAVQTAEPVAAARGLTVEIDDRFA 77
Cdd:PRK15004    1 MRLWLVRHGETQANVDGlysGHAPTPLTARGIEQAQNLHTLLRDVPFDLVLCSELERAQHTARLVLSDRQLPVHIIPELN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  78 EY---DRELPVYIPIEQIRAENPQEWARMAEGHLPSSVDE-DAFRARVRAAVDHVAvTADHDDTVAVFSHGGVINVVLHE 153
Cdd:PRK15004   81 EMffgDWEMRHHRDLMQEDAENYAAWCNDWQHAIPTNGEGfQAFSQRVERFIARLS-AFQHYQNLLIVSHQGVLSLLIAR 159


                  ...
gi 1806256999 154 ILG 156
Cdd:PRK15004  160 LLG 162
PRK13462 PRK13462
acid phosphatase; Provisional
 2-100 2.37e-06

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 46.36  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999   2 QLLLVRHALPHRSEPGE---GADPVLSDEGRAQVARLPDALARYPISR--VISSPQRRAVQTAEpvaaARGLTV-EIDDR 75
Cdd:PRK13462    7 RLLLLRHGETEWSKSGRhtgRTELELTETGRTQAELAGQALGELELDDplVISSPRRRALDTAK----LAGLTVdEVSGL 82

                          90       100
                  ....*....|....*....|....*
gi 1806256999  76 FAEYDRELPVYIPIEQIRAENPqEW 100
Cdd:PRK13462   83 LAEWDYGSYEGLTTPQIRESEP-DW 106
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 1-71 4.94e-05

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 41.75  E-value: 4.94e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1806256999   1 MQLLLVRHALPHRSEPGEGADPVL---SDEGRAQVARLPDALARypISRVISSPQRRAVQTAEPVAAARGLTVE 71
Cdd:TIGR00249   1 MQLFIMRHGDAALDAASDSVRPLTtngCDESRLVAQWLKGQGVE--IERILVSPFVRAEQTAEIVGDCLNLPSS 72
PRK13463 PRK13463
phosphoserine phosphatase 1;
24-156 4.06e-04

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 40.03  E-value: 4.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806256999  24 LSDEGRAQVARLPDALARYPISRVISSPQRRAVQTAEPVAAARGLTVEIDDRFAEYDRELPVYIPIEQIRAENPQE---- 99
Cdd:PRK13463   29 LTENGILQAKQLGERMKDLSIHAIYSSPSERTLHTAELIKGERDIPIIADEHFYEINMGIWEGQTIDDIERQYPDDiqlf 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1806256999 100 WarmAEGHLPSSVDEDAFRARVRAAVD--HVAVTADHDDTVAVFSHGGVINVVLHEILG 156
Cdd:PRK13463  109 W---NEPHLFQSTSGENFEAVHKRVIEgmQLLLEKHKGESILIVSHAAAAKLLVGHFAG 164
PRK06193 PRK06193
hypothetical protein; Provisional
 24-59 1.45e-03

hypothetical protein; Provisional


Pssm-ID: 235734  Cd Length: 206  Bit Score: 38.13  E-value: 1.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1806256999  24 LSDEGRAQVARLPDALARY--PISRVISSPQRRAVQTA 59
Cdd:PRK06193   74 LSEEGREQARAIGEAFRALaiPVGKVISSPYCRAWETA 111
 
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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