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Conserved domains on  [gi|506282526|ref|WP_015802301|]
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histidine phosphatase family protein [Actinosynnema mirum]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10800271)

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

CATH:  3.40.50.1240
PubMed:  18092946|2543188

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MSMEG_4193 TIGR03848
probable phosphomutase, MSMEG_4193 family; A three-gene system broadly conserved among the ...
 3-206 8.88e-112

probable phosphomutase, MSMEG_4193 family; A three-gene system broadly conserved among the Actinobacteria includes MSMEG_4193 and homologs, a subgroup among the larger phosphoglycerate mutase family protein (pfam00300). Another member of the trio is a probable kinase, related to phosphatidylinositol kinases; that context supports the hypothesis that this protein acts as a phosphomutase.


:

Pssm-ID: 163560  Cd Length: 204  Bit Score: 318.54  E-value: 8.88e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526    3 TVILLRHARSTANGSAILAGRQPGVRLAEDGERQARALVDRLAGVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPDLA 82
Cdd:TIGR03848   1 TVILVRHGRSTANTAGTLAGRTPGVDLDERGREQAAALAERLADLPIAAIVSSPLERCRETAEPIAEARGLPPRVDERLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   83 EVEYGDWTGRPIKELLQEPLWKVVQQHPSAAVFPGGEGLARVQARAVAAVRAHDARITGEFGPGAVWLACSHGDVIKSLL 162
Cdd:TIGR03848  81 ECDYGDWTGRELKELAKEPLWPVVQAHPSAAVFPGGESLAQVQARAVAAVREHDARLAAEHGPDAVWVACSHGDVIKSVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 506282526  163 ADALGAHLDGFQRIVVDPASLSVVRYTETRPFVLRVNDNGGDLA 206
Cdd:TIGR03848 161 ADALGMHLDLFQRIVVDPCSVSVVRYTPLRPFVLRVNDTGGDLS 204
 
Name Accession Description Interval E-value
MSMEG_4193 TIGR03848
probable phosphomutase, MSMEG_4193 family; A three-gene system broadly conserved among the ...
 3-206 8.88e-112

probable phosphomutase, MSMEG_4193 family; A three-gene system broadly conserved among the Actinobacteria includes MSMEG_4193 and homologs, a subgroup among the larger phosphoglycerate mutase family protein (pfam00300). Another member of the trio is a probable kinase, related to phosphatidylinositol kinases; that context supports the hypothesis that this protein acts as a phosphomutase.


Pssm-ID: 163560  Cd Length: 204  Bit Score: 318.54  E-value: 8.88e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526    3 TVILLRHARSTANGSAILAGRQPGVRLAEDGERQARALVDRLAGVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPDLA 82
Cdd:TIGR03848   1 TVILVRHGRSTANTAGTLAGRTPGVDLDERGREQAAALAERLADLPIAAIVSSPLERCRETAEPIAEARGLPPRVDERLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   83 EVEYGDWTGRPIKELLQEPLWKVVQQHPSAAVFPGGEGLARVQARAVAAVRAHDARITGEFGPGAVWLACSHGDVIKSLL 162
Cdd:TIGR03848  81 ECDYGDWTGRELKELAKEPLWPVVQAHPSAAVFPGGESLAQVQARAVAAVREHDARLAAEHGPDAVWVACSHGDVIKSVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 506282526  163 ADALGAHLDGFQRIVVDPASLSVVRYTETRPFVLRVNDNGGDLA 206
Cdd:TIGR03848 161 ADALGMHLDLFQRIVVDPCSVSVVRYTPLRPFVLRVNDTGGDLS 204
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-199 2.75e-49

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 159.72  E-value: 2.75e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   1 MATVILLRHARSTANGSAILAGRQpGVRLAEDGERQARALVDRLAGVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPD 80
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGRL-DVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526  81 LAEVEYGDWTGRPIKELLQE--PLWKVVQQHPSAAVFPGGEGLARVQaravaavrahdARITGEF------GPGAVWLAC 152
Cdd:COG0406   80 LREIDFGDWEGLTFAELEARypEALAAWLADPAEFRPPGGESLADVQ-----------ARVRAALeellarHPGGTVLVV 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 506282526 153 SHGDVIKSLLADALGAHLDGFQRIVVDPASLSVVRYTETRPFVLRVN 199
Cdd:COG0406  149 THGGVIRALLAHLLGLPLEAFWRLRIDNASVTVLEFDDGRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-201 9.72e-46

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: 150.44  E-value: 9.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526    4 VILLRHARSTANGSAILaGRQPGVRLAEDGERQARALVDRLAGVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPDLAE 83
Cdd:pfam00300   1 LYLVRHGETEWNLEGRF-QGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRLRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   84 VEYGDWTGRPIKELLQE--PLWKVVQQHPSAAVFPGGEGLARVQaravaavrahdARITGEF------GPGAVWLACSHG 155
Cdd:pfam00300  80 IDFGDWEGLTFEEIAERypEEYDAWLADPADYRPPGGESLADVR-----------ARVRAALeelaarHPGKTVLVVSHG 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 506282526  156 DVIKSLLADALGAHLDGFQRIVVDPASLSVVRYTETRPFVLRVNDN 201
Cdd:pfam00300 149 GVIRALLAHLLGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-161 1.22e-26

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: 100.23  E-value: 1.22e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526     3 TVILLRHARSTANGSAILAGRqPGVRLAEDGERQARALVDRLA---GVRLDAVVTSPLERCGQTLEPLLAERGLtaaveP 79
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGD-TDVPLTELGRAQAEALGRLLAsllLPRFDVVYSSPLKRARQTAEALAIALGL-----P 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526    80 DLAEVEYGDWTGRPIKELLQEPLWKVVQ-----QHPSAAVFPGGEGLarvQARAVAAVRAHDARITGEFGPGAVWLACSH 154
Cdd:smart00855  75 GLRERDFGAWEGLTWDEIAAKYPEEYLAawrdpYDPAPPAPPGGESL---ADLVERVEPALDELIATADASGQNVLIVSH 151


                   ....*..
gi 506282526   155 GDVIKSL 161
Cdd:smart00855 152 GGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-200 2.31e-18

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: 78.52  E-value: 2.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   3 TVILLRHARSTANGSAILAGrQPGVRLAEDGERQARALVDRLA--GVRLDAVVTSPLERCGQTLEPLLAER-GLTAAVEP 79
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQG-WTDVPLTEKGREQARALGKRLKelGIKFDRIYSSPLKRAIQTAEIILEELpGLPVEVDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526  80 DLAEveygdwtgRPIKELLQEplwkVVQQHPSAAVfpggeglarvqaravaavrahdaritgefgpgavwLACSHGDVIK 159
Cdd:cd07067   80 RLRE--------ARVLPALEE----LIAPHDGKNV-----------------------------------LIVSHGGVLR 112

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 506282526 160 SLLADALGAHLDGFQRIVVDPASLSVVRYTETRPFVLRVND 200
Cdd:cd07067  113 ALLAYLLGLSDEDILRLNLPNGSISVLELDENGGGVLLLRL 153
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 2-202 1.47e-16

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 77.33  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   2 ATVILLRHARSTANGSAILAGR-QPGvrLAEDGERQARALVDRLAGVR-LDAVVTSPLERCGQTLEPLLAERGLTAAVEP 79
Cdd:PRK07238 172 TRLLLLRHGQTELSVQRRYSGRgNPE--LTEVGRRQAAAAARYLAARGgIDAVVSSPLQRARDTAAAAAKALGLDVTVDD 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526  80 DLAEVEYGDWTGRPIKEllqeplwkVVQQHP---------SAAVFPGGEGLARVQARAVAAVrahdARITGEFgPGAVWL 150
Cdd:PRK07238 250 DLIETDFGAWEGLTFAE--------AAERDPelhrawladTSVAPPGGESFDAVARRVRRAR----DRLIAEY-PGATVL 316

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 506282526 151 ACSHGDVIKSLLADALGAHLDGFQRIVVDPASLSVVRYTETRPFVLR-VNDNG 202
Cdd:PRK07238 317 VVSHVTPIKTLLRLALDAGPGVLYRLHLDLASLSIAEFYPDGPASVRlVNDTS 369
 
Name Accession Description Interval E-value
MSMEG_4193 TIGR03848
probable phosphomutase, MSMEG_4193 family; A three-gene system broadly conserved among the ...
 3-206 8.88e-112

probable phosphomutase, MSMEG_4193 family; A three-gene system broadly conserved among the Actinobacteria includes MSMEG_4193 and homologs, a subgroup among the larger phosphoglycerate mutase family protein (pfam00300). Another member of the trio is a probable kinase, related to phosphatidylinositol kinases; that context supports the hypothesis that this protein acts as a phosphomutase.


Pssm-ID: 163560  Cd Length: 204  Bit Score: 318.54  E-value: 8.88e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526    3 TVILLRHARSTANGSAILAGRQPGVRLAEDGERQARALVDRLAGVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPDLA 82
Cdd:TIGR03848   1 TVILVRHGRSTANTAGTLAGRTPGVDLDERGREQAAALAERLADLPIAAIVSSPLERCRETAEPIAEARGLPPRVDERLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   83 EVEYGDWTGRPIKELLQEPLWKVVQQHPSAAVFPGGEGLARVQARAVAAVRAHDARITGEFGPGAVWLACSHGDVIKSLL 162
Cdd:TIGR03848  81 ECDYGDWTGRELKELAKEPLWPVVQAHPSAAVFPGGESLAQVQARAVAAVREHDARLAAEHGPDAVWVACSHGDVIKSVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 506282526  163 ADALGAHLDGFQRIVVDPASLSVVRYTETRPFVLRVNDNGGDLA 206
Cdd:TIGR03848 161 ADALGMHLDLFQRIVVDPCSVSVVRYTPLRPFVLRVNDTGGDLS 204
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-199 2.75e-49

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 159.72  E-value: 2.75e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   1 MATVILLRHARSTANGSAILAGRQpGVRLAEDGERQARALVDRLAGVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPD 80
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGRL-DVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526  81 LAEVEYGDWTGRPIKELLQE--PLWKVVQQHPSAAVFPGGEGLARVQaravaavrahdARITGEF------GPGAVWLAC 152
Cdd:COG0406   80 LREIDFGDWEGLTFAELEARypEALAAWLADPAEFRPPGGESLADVQ-----------ARVRAALeellarHPGGTVLVV 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 506282526 153 SHGDVIKSLLADALGAHLDGFQRIVVDPASLSVVRYTETRPFVLRVN 199
Cdd:COG0406  149 THGGVIRALLAHLLGLPLEAFWRLRIDNASVTVLEFDDGRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-201 9.72e-46

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: 150.44  E-value: 9.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526    4 VILLRHARSTANGSAILaGRQPGVRLAEDGERQARALVDRLAGVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPDLAE 83
Cdd:pfam00300   1 LYLVRHGETEWNLEGRF-QGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRLRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   84 VEYGDWTGRPIKELLQE--PLWKVVQQHPSAAVFPGGEGLARVQaravaavrahdARITGEF------GPGAVWLACSHG 155
Cdd:pfam00300  80 IDFGDWEGLTFEEIAERypEEYDAWLADPADYRPPGGESLADVR-----------ARVRAALeelaarHPGKTVLVVSHG 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 506282526  156 DVIKSLLADALGAHLDGFQRIVVDPASLSVVRYTETRPFVLRVNDN 201
Cdd:pfam00300 149 GVIRALLAHLLGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 4-186 2.12e-28

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: 105.40  E-value: 2.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526    4 VILLRHARsTANGSAILAGRQPgVRLAEDGERQARALVDRLAGVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPDLAE 83
Cdd:TIGR03162   1 LYLIRHGE-TDVNAGLCYGQTD-VPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAERRGLPIIKDDRLRE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   84 VEYGDWTGRPIKELLQE-PLWKVVQQHPSAAVFPGGEGLARVQaravaavrahdARITG------EFGPGAVWLACSHGD 156
Cdd:TIGR03162  79 MDFGDWEGRSWDEIPEAyPELDAWAADWQHARPPGGESFADFY-----------QRVSEfleellKAHEGDNVLIVTHGG 147

                         170       180       190
                  ....*....|....*....|....*....|
gi 506282526  157 VIKSLLADALGAHLDGFQRIVVDPASLSVV 186
Cdd:TIGR03162 148 VIRALLAHLLGLPLEQWWSFAVEYGSITLI 177
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-161 1.22e-26

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: 100.23  E-value: 1.22e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526     3 TVILLRHARSTANGSAILAGRqPGVRLAEDGERQARALVDRLA---GVRLDAVVTSPLERCGQTLEPLLAERGLtaaveP 79
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGD-TDVPLTELGRAQAEALGRLLAsllLPRFDVVYSSPLKRARQTAEALAIALGL-----P 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526    80 DLAEVEYGDWTGRPIKELLQEPLWKVVQ-----QHPSAAVFPGGEGLarvQARAVAAVRAHDARITGEFGPGAVWLACSH 154
Cdd:smart00855  75 GLRERDFGAWEGLTWDEIAAKYPEEYLAawrdpYDPAPPAPPGGESL---ADLVERVEPALDELIATADASGQNVLIVSH 151


                   ....*..
gi 506282526   155 GDVIKSL 161
Cdd:smart00855 152 GGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-200 2.31e-18

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: 78.52  E-value: 2.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   3 TVILLRHARSTANGSAILAGrQPGVRLAEDGERQARALVDRLA--GVRLDAVVTSPLERCGQTLEPLLAER-GLTAAVEP 79
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQG-WTDVPLTEKGREQARALGKRLKelGIKFDRIYSSPLKRAIQTAEIILEELpGLPVEVDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526  80 DLAEveygdwtgRPIKELLQEplwkVVQQHPSAAVfpggeglarvqaravaavrahdaritgefgpgavwLACSHGDVIK 159
Cdd:cd07067   80 RLRE--------ARVLPALEE----LIAPHDGKNV-----------------------------------LIVSHGGVLR 112

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 506282526 160 SLLADALGAHLDGFQRIVVDPASLSVVRYTETRPFVLRVND 200
Cdd:cd07067  113 ALLAYLLGLSDEDILRLNLPNGSISVLELDENGGGVLLLRL 153
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 2-202 1.47e-16

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 77.33  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   2 ATVILLRHARSTANGSAILAGR-QPGvrLAEDGERQARALVDRLAGVR-LDAVVTSPLERCGQTLEPLLAERGLTAAVEP 79
Cdd:PRK07238 172 TRLLLLRHGQTELSVQRRYSGRgNPE--LTEVGRRQAAAAARYLAARGgIDAVVSSPLQRARDTAAAAAKALGLDVTVDD 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526  80 DLAEVEYGDWTGRPIKEllqeplwkVVQQHP---------SAAVFPGGEGLARVQARAVAAVrahdARITGEFgPGAVWL 150
Cdd:PRK07238 250 DLIETDFGAWEGLTFAE--------AAERDPelhrawladTSVAPPGGESFDAVARRVRRAR----DRLIAEY-PGATVL 316

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 506282526 151 ACSHGDVIKSLLADALGAHLDGFQRIVVDPASLSVVRYTETRPFVLR-VNDNG 202
Cdd:PRK07238 317 VVSHVTPIKTLLRLALDAGPGVLYRLHLDLASLSIAEFYPDGPASVRlVNDTS 369
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 3-199 6.60e-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: 72.06  E-value: 6.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   3 TVILLRHARSTANGSAILAGrQPGVRLAEDGERQARALVDRLA--GVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPd 80
Cdd:cd07040    1 VLYLVRHGEREPNAEGRFTG-WGDGPLTEKGRQQARELGKALRerYIKFDRIYSSPLKRAIQTAEIILEGLFEGLPVEV- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526  81 laeveygDWTGRPIKELLqeplwkvvqqhpsaavfpggeglarvqaravaavrahdARITGEFGPGAVWLACSHGDVIKS 160
Cdd:cd07040   79 -------DPRARVLNALL--------------------------------------ELLARHLLDGKNVLIVSHGGTIRA 113

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 506282526 161 LLADALGAHLDGFQRIVVDPASLSVV-RYTETRPFVLRVN 199
Cdd:cd07040  114 LLAALLGLSDEEILSLNLPNGSILVLeLDECGGKYVRLLN 153
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
6-120 3.40e-15

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 71.24  E-value: 3.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   6 LLRHARSTANGSAILAGRQPgVRLAEDGERQARALVDRLAGVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPDLAEVE 85
Cdd:PRK15004   5 LVRHGETQANVDGLYSGHAP-TPLTARGIEQAQNLHTLLRDVPFDLVLCSELERAQHTARLVLSDRQLPVHIIPELNEMF 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 506282526  86 YGDWTGRPIKELLQE-----PLWKVVQQHpsaAVFPGGEG 120
Cdd:PRK15004  84 FGDWEMRHHRDLMQEdaenyAAWCNDWQH---AIPTNGEG 120
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
4-83 4.65e-10

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 56.04  E-value: 4.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   4 VILLRHARSTANGSAILAGRQPgvrLAEDGERQARALVDRLA--GVRLDAVVTSPLERCGQTLEPLLAERGLTAAVE--P 79
Cdd:COG2062    1 LILVRHAKAEWRAPGGDDFDRP---LTERGRRQARAMARWLAalGLKPDRILSSPALRARQTAEILAEALGLPPKVEveD 77


                 ....
gi 506282526  80 DLAE 83
Cdd:COG2062   78 ELYD 81
PRK13463 PRK13463
phosphoserine phosphatase 1;
3-97 7.32e-08

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 51.20  E-value: 7.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   3 TVILLRHARSTANGSAILAGRQPGVrLAEDGERQARALVDRLAGVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPDLA 82
Cdd:PRK13463   4 TVYVTRHGETEWNVAKRMQGRKNSA-LTENGILQAKQLGERMKDLSIHAIYSSPSERTLHTAELIKGERDIPIIADEHFY 82

                         90
                 ....*....|....*
gi 506282526  83 EVEYGDWTGRPIKEL 97
Cdd:PRK13463  83 EINMGIWEGQTIDDI 97
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
1-119 1.63e-05

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 44.33  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   1 MATVILLRHARSTANGSAILAGrQPGVRLAEDGERQARALVDRLAGVRLDAVVTSPLERCGQTLEPLLAERGLTAAVEPD 80
Cdd:PRK03482   1 MLQVYLVRHGETQWNAERRIQG-QSDSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAEIIAQACGCDIIFDPR 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506282526  81 LAEVEYGDWTGRPIKEL-LQEPLWK--VVQQHPSAAVfPGGE 119
Cdd:PRK03482  80 LRELNMGVLEKRHIDSLtEEEEGWRrqLVNGTVDGRI-PEGE 120
PRK13462 PRK13462
acid phosphatase; Provisional
 4-121 3.65e-05

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 43.28  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506282526   4 VILLRHARSTANGSAILAGRQPgVRLAEDGERQARALVDRLAGVRLD--AVVTSPLERCGQTLEplLAerGLTAA-VEPD 80
Cdd:PRK13462   8 LLLLRHGETEWSKSGRHTGRTE-LELTETGRTQAELAGQALGELELDdpLVISSPRRRALDTAK--LA--GLTVDeVSGL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506282526  81 LAEVEYGDWTGRPIKELLQ-EPLWkVVQQHPSaavfPGGEGL 121
Cdd:PRK13462  83 LAEWDYGSYEGLTTPQIREsEPDW-LVWTHGC----PGGESV 119
gpmA PRK14119
phosphoglyceromutase; Provisional
 1-70 1.07e-03

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 39.10  E-value: 1.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506282526   1 MATVILLRHARSTANGSAILAGRQpGVRLAEDGERQARALVDRLA--GVRLDAVVTSPLERCGQTLEPLLAE 70
Cdd:PRK14119   1 MPKLILCRHGQSEWNAKNLFTGWE-DVNLSEQGINEATRAGEKVRenNIAIDVAFTSLLTRALDTTHYILTE 71
 
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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