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Conserved domains on  [gi|499269880|ref|WP_010967273|]
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MULTISPECIES: histidine phosphatase family protein [Sinorhizobium]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10001383)

histidine phosphatase family protein is a probable phosphatase that may catalyze the dephosphorylation of a phosphorylated substrate involving a conserved catalytic histidine residue which becomes phosphorylated during the reaction

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-187 2.98e-55

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


:

Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 173.98  E-value: 2.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   1 MKRIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAALLGYPH---AQLSPAL 77
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALglpVEVDPRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880  78 REIDVGDWTGRAIGDLMAEDQDAYLGWRAG--TYAPRGGERWQEFRDRVTAGLGKAV-SIPGERLLVVCHGGVIRALLDG 154
Cdd:COG0406   81 REIDFGDWEGLTFAELEARYPEALAAWLADpaEFRPPGGESLADVQARVRAALEELLaRHPGGTVLVVTHGGVIRALLAH 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499269880 155 LLGLPPKRI--IPVGPASVTVLADKPGGMRLETFN 187
Cdd:COG0406  161 LLGLPLEAFwrLRIDNASVTVLEFDDGRWRLVALN 195
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-187 2.98e-55

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 173.98  E-value: 2.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   1 MKRIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAALLGYPH---AQLSPAL 77
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALglpVEVDPRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880  78 REIDVGDWTGRAIGDLMAEDQDAYLGWRAG--TYAPRGGERWQEFRDRVTAGLGKAV-SIPGERLLVVCHGGVIRALLDG 154
Cdd:COG0406   81 REIDFGDWEGLTFAELEARYPEALAAWLADpaEFRPPGGESLADVQARVRAALEELLaRHPGGTVLVVTHGGVIRALLAH 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499269880 155 LLGLPPKRI--IPVGPASVTVLADKPGGMRLETFN 187
Cdd:COG0406  161 LLGLPLEAFwrLRIDNASVTVLEFDDGRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-187 3.67e-49

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 158.14  E-value: 3.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880    4 IILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAALLGYPH---AQLSPALREI 80
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALglpVEIDPRLREI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   81 DVGDWTGRAIGDLMAEDQDAYLGWRAG--TYAPRGGERWQEFRDRVTAGLGKAVSI-PGERLLVVCHGGVIRA--LLDGL 155
Cdd:pfam00300  81 DFGDWEGLTFEEIAERYPEEYDAWLADpaDYRPPGGESLADVRARVRAALEELAARhPGKTVLVVSHGGVIRAllAHLLG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 499269880  156 LGLPPKRIIPVGPASVTVLADKPGGMRLETFN 187
Cdd:pfam00300 161 LPLEALRRFPLDNASLSILEFDGGGWVLVLLN 192
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-150 1.65e-37

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: 127.19  E-value: 1.65e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880     3 RIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAM---RPDHVIASDLLRARHTAALLGYphAQLSPALRE 79
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLASLllpRFDVVYSSPLKRARQTAEALAI--ALGLPGLRE 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499269880    80 IDVGDWTGRAIGDLMAEDQDAYL-GWRAGT----YAPRGGERWQEFRDRVTAGLGKAVSI---PGERLLVVCHGGVIRA 150
Cdd:smart00855  79 RDFGAWEGLTWDEIAAKYPEEYLaAWRDPYdpapPAPPGGESLADLVERVEPALDELIATadaSGQNVLIVSHGGVIRA 157
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 4-174 8.28e-35

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: 121.19  E-value: 8.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880    4 IILVRHGESAWNSVRRLqGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAALLGYPH---AQLSPALREI 80
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCY-GQTDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAERRglpIIKDDRLREM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   81 DVGDWTGRAIGDLMaedqDAYLGWRA-----GTYAPRGGERWQEFRDRVTAGLGK-AVSIPGERLLVVCHGGVIRALLDG 154
Cdd:TIGR03162  80 DFGDWEGRSWDEIP----EAYPELDAwaadwQHARPPGGESFADFYQRVSEFLEElLKAHEGDNVLIVTHGGVIRALLAH 155

                         170       180
                  ....*....|....*....|..
gi 499269880  155 LLGLPPKRI--IPVGPASVTVL 174
Cdd:TIGR03162 156 LLGLPLEQWwsFAVEYGSITLI 177
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-150 2.28e-25

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: 95.85  E-value: 2.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   3 RIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAM--RPDHVIASDLLRARHTAALLG----YPHAQLSPA 76
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELgiKFDRIYSSPLKRAIQTAEIILeelpGLPVEVDPR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499269880  77 LREIDVGDWtgraigdlmaedqdaylgwragtyaprggerWQEFRDRvtaglgkavsIPGERLLVVCHGGVIRA 150
Cdd:cd07067   81 LREARVLPA-------------------------------LEELIAP----------HDGKNVLIVSHGGVLRA 113
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
1-145 6.60e-25

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 96.72  E-value: 6.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   1 MKRIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAALLgyphAQ-------L 73
Cdd:PRK03482   1 MLQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAEII----AQacgcdiiF 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499269880  74 SPALREIDVGDWTGRAIGDLMAEDQdaylGWRA----GTYAPR--GGERWQEFRDRVTAGLGKAVSIP-GERLLVVCHG 145
Cdd:PRK03482  77 DPRLRELNMGVLEKRHIDSLTEEEE----GWRRqlvnGTVDGRipEGESMQELSDRMHAALESCLELPqGSRPLLVSHG 151
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-187 2.98e-55

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 173.98  E-value: 2.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   1 MKRIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAALLGYPH---AQLSPAL 77
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALglpVEVDPRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880  78 REIDVGDWTGRAIGDLMAEDQDAYLGWRAG--TYAPRGGERWQEFRDRVTAGLGKAV-SIPGERLLVVCHGGVIRALLDG 154
Cdd:COG0406   81 REIDFGDWEGLTFAELEARYPEALAAWLADpaEFRPPGGESLADVQARVRAALEELLaRHPGGTVLVVTHGGVIRALLAH 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499269880 155 LLGLPPKRI--IPVGPASVTVLADKPGGMRLETFN 187
Cdd:COG0406  161 LLGLPLEAFwrLRIDNASVTVLEFDDGRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-187 3.67e-49

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 158.14  E-value: 3.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880    4 IILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAALLGYPH---AQLSPALREI 80
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALglpVEIDPRLREI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   81 DVGDWTGRAIGDLMAEDQDAYLGWRAG--TYAPRGGERWQEFRDRVTAGLGKAVSI-PGERLLVVCHGGVIRA--LLDGL 155
Cdd:pfam00300  81 DFGDWEGLTFEEIAERYPEEYDAWLADpaDYRPPGGESLADVRARVRAALEELAARhPGKTVLVVSHGGVIRAllAHLLG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 499269880  156 LGLPPKRIIPVGPASVTVLADKPGGMRLETFN 187
Cdd:pfam00300 161 LPLEALRRFPLDNASLSILEFDGGGWVLVLLN 192
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-150 1.65e-37

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: 127.19  E-value: 1.65e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880     3 RIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAM---RPDHVIASDLLRARHTAALLGYphAQLSPALRE 79
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLASLllpRFDVVYSSPLKRARQTAEALAI--ALGLPGLRE 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499269880    80 IDVGDWTGRAIGDLMAEDQDAYL-GWRAGT----YAPRGGERWQEFRDRVTAGLGKAVSI---PGERLLVVCHGGVIRA 150
Cdd:smart00855  79 RDFGAWEGLTWDEIAAKYPEEYLaAWRDPYdpapPAPPGGESLADLVERVEPALDELIATadaSGQNVLIVSHGGVIRA 157
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 4-174 8.28e-35

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: 121.19  E-value: 8.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880    4 IILVRHGESAWNSVRRLqGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAALLGYPH---AQLSPALREI 80
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCY-GQTDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAERRglpIIKDDRLREM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   81 DVGDWTGRAIGDLMaedqDAYLGWRA-----GTYAPRGGERWQEFRDRVTAGLGK-AVSIPGERLLVVCHGGVIRALLDG 154
Cdd:TIGR03162  80 DFGDWEGRSWDEIP----EAYPELDAwaadwQHARPPGGESFADFYQRVSEFLEElLKAHEGDNVLIVTHGGVIRALLAH 155

                         170       180
                  ....*....|....*....|..
gi 499269880  155 LLGLPPKRI--IPVGPASVTVL 174
Cdd:TIGR03162 156 LLGLPLEQWwsFAVEYGSITLI 177
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-150 2.28e-25

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: 95.85  E-value: 2.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   3 RIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAM--RPDHVIASDLLRARHTAALLG----YPHAQLSPA 76
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELgiKFDRIYSSPLKRAIQTAEIILeelpGLPVEVDPR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499269880  77 LREIDVGDWtgraigdlmaedqdaylgwragtyaprggerWQEFRDRvtaglgkavsIPGERLLVVCHGGVIRA 150
Cdd:cd07067   81 LREARVLPA-------------------------------LEELIAP----------HDGKNVLIVSHGGVLRA 113
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
1-145 6.60e-25

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 96.72  E-value: 6.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   1 MKRIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAALLgyphAQ-------L 73
Cdd:PRK03482   1 MLQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAEII----AQacgcdiiF 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499269880  74 SPALREIDVGDWTGRAIGDLMAEDQdaylGWRA----GTYAPR--GGERWQEFRDRVTAGLGKAVSIP-GERLLVVCHG 145
Cdd:PRK03482  77 DPRLRELNMGVLEKRHIDSLTEEEE----GWRRqlvnGTVDGRipEGESMQELSDRMHAALESCLELPqGSRPLLVSHG 151
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
3-148 9.99e-23

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 90.50  E-value: 9.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   3 RIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAALLGYPH---AQLSPALRE 79
Cdd:PRK15004   2 RLWLVRHGETQANVDGLYSGHAPTPLTARGIEQAQNLHTLLRDVPFDLVLCSELERAQHTARLVLSDRqlpVHIIPELNE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499269880  80 IDVGDWTGRAIGDLMAEDQDAYLGWRAG--TYAPRGGERWQEFRDRVTAGLGKAVS-IPGERLLVVCHGGVI 148
Cdd:PRK15004  82 MFFGDWEMRHHRDLMQEDAENYAAWCNDwqHAIPTNGEGFQAFSQRVERFIARLSAfQHYQNLLIVSHQGVL 153
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 3-150 1.04e-19

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: 81.31  E-value: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   3 RIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAM--RPDHVIASDLLRARHTAALLGYPHAQLSPALRei 80
Cdd:cd07040    1 VLYLVRHGEREPNAEGRFTGWGDGPLTEKGRQQARELGKALRERyiKFDRIYSSPLKRAIQTAEIILEGLFEGLPVEV-- 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880  81 dvgDWTGRAIGDLMAEDQDAYLgwragtyaprggerwqefrdrvtaglgkavsiPGERLLVVCHGGVIRA 150
Cdd:cd07040   79 ---DPRARVLNALLELLARHLL--------------------------------DGKNVLIVSHGGTIRA 113
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 3-144 1.39e-15

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 73.86  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   3 RIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRP-DHVIASDLLRARHTAA----LLGYPhAQLSPAL 77
Cdd:PRK07238 173 RLLLLRHGQTELSVQRRYSGRGNPELTEVGRRQAAAAARYLAARGGiDAVVSSPLQRARDTAAaaakALGLD-VTVDDDL 251

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499269880  78 REIDVGDWTGRAIGDLMAEDQDAYLGWRAGTY-APRGGERWQEFRDRVTAGLGK-AVSIPGERLLVVCH 144
Cdd:PRK07238 252 IETDFGAWEGLTFAEAAERDPELHRAWLADTSvAPPGGESFDAVARRVRRARDRlIAEYPGATVLVVSH 320
PRK13462 PRK13462
acid phosphatase; Provisional
 3-150 1.80e-14

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 68.70  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   3 RIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRPDH--VIASDLLRARHTAALLGYPHAQLSPALREI 80
Cdd:PRK13462   7 RLLLLRHGETEWSKSGRHTGRTELELTETGRTQAELAGQALGELELDDplVISSPRRRALDTAKLAGLTVDEVSGLLAEW 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499269880  81 DVGDWTGRAIGDLMAEDQDaylgWRAGTYAPRGGERWQEFRDRVTAGLGKAVSIPGER-LLVVCHGGVIRA 150
Cdd:PRK13462  87 DYGSYEGLTTPQIRESEPD----WLVWTHGCPGGESVAQVNERADRAVALALEHMESRdVVFVSHGHFSRA 153
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
4-85 2.14e-11

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 59.12  E-value: 2.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   4 IILVRHGESAWNSvrrlQGQADI--GLSARGEAQATALRATIEAM--RPDHVIASDLLRARHTAAL----LGYPHA-QLS 74
Cdd:COG2062    1 LILVRHAKAEWRA----PGGDDFdrPLTERGRRQARAMARWLAALglKPDRILSSPALRARQTAEIlaeaLGLPPKvEVE 76

                         90
                 ....*....|.
gi 499269880  75 PALREIDVGDW 85
Cdd:COG2062   77 DELYDADPEDL 87
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 1-150 2.46e-11

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 60.09  E-value: 2.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   1 MKRI-ILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEA--MRPDHVIASDLLRARHTAAL----LGYPHAQL 73
Cdd:PRK01295   1 MSRTlVLVRHGQSEWNLKNLFTGWRDPDLTEQGVAEAKAAGRKLKAagLKFDIAFTSALSRAQHTCQLileeLGQPGLET 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880  74 --SPALREIDVGDWTGRAIGDLMAE--DQDAYLGWRAGTYAPRGGErwqEFRDRVTAGLGKAVS------IPGERLLVVC 143
Cdd:PRK01295  81 irDQALNERDYGDLSGLNKDDARAKwgEEQVHIWRRSYDVPPPGGE---SLKDTGARVLPYYLQeilprvLRGERVLVAA 157


                 ....*..
gi 499269880 144 HGGVIRA 150
Cdd:PRK01295 158 HGNSLRA 164
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 2-81 2.47e-11

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: 60.48  E-value: 2.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   2 KRIILVRHGESAWNSVRRLQGQADIGLSARGEAQATA----LRAtiEAMRPDHVIASDLLRARHTAALlgyphaqlspAL 77
Cdd:COG0588    1 YKLVLLRHGESEWNLENRFTGWTDVDLSEKGRAEAKRagrlLKE--AGFLFDVAYTSVLKRAIRTLWI----------VL 68


                 ....
gi 499269880  78 REID 81
Cdd:COG0588   69 DEMD 72
PRK13463 PRK13463
phosphoserine phosphatase 1;
1-149 4.81e-11

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 59.29  E-value: 4.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   1 MKRIILV-RHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAALL-GYPHAQL--SPA 76
Cdd:PRK13463   1 MKTTVYVtRHGETEWNVAKRMQGRKNSALTENGILQAKQLGERMKDLSIHAIYSSPSERTLHTAELIkGERDIPIiaDEH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499269880  77 LREIDVGDWTGRAIGDL-MAEDQDAYLGW-RAGTYAPRGGERWQEFRDRVTAGLGKAVSI-PGERLLVVCHGGVIR 149
Cdd:PRK13463  81 FYEINMGIWEGQTIDDIeRQYPDDIQLFWnEPHLFQSTSGENFEAVHKRVIEGMQLLLEKhKGESILIVSHAAAAK 156
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
1-65 7.31e-10

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 56.27  E-value: 7.31e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499269880   1 MKRIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEAMRPDHVIASDLLRARHTAAL 65
Cdd:PRK01112   1 MALLILLRHGQSVWNAKNLFTGWVDIPLSQQGIAEAIAAGEKIKDLPIDCIFTSTLVRSLMTALL 65
pgm_1 TIGR01258
phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are ...
 3-150 1.74e-08

phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are phosphoglycerate mutase (EC 5.4.2.1). This enzyme interconverts 2-phosphoglycerate and 3-phosphoglycerate. The enzyme is transiently phosphorylated on an active site histidine by 2,3-diphosphoglyerate, which is both substrate and product. Some members of this family have are phosphoglycerate mutase as a minor activity and act primarily as a bisphoglycerate mutase, interconverting 2,3-diphosphoglycerate and 1,3-diphosphoglycerate (EC 5.4.2.4). This model is designated as a subfamily for this reason. The second and third paralogs in S. cerevisiae are somewhat divergent and apparently inactive (see PUBMED:9544241) but are also part of this subfamily phylogenetically.


Pssm-ID: 213596 [Multi-domain]  Cd Length: 245  Bit Score: 52.80  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880    3 RIILVRHGESAWNSVRRLQGQADIGLSARG--EAQATALRATIEAMRPDHVIASDLLRARHTAALlgyphaqlspALREI 80
Cdd:TIGR01258   2 KLVLVRHGESEWNALNLFTGWVDVKLSEKGqqEAKRAGELLKEEGYEFDVAYTSLLKRAIHTLNI----------ALDEL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   81 D------VGDW--TGRAIGDLMAED---------QDAYLGWRAGTYAP-----RGGERWQEfRDRVTAGLGKAV------ 132
Cdd:TIGR01258  72 DqlwipvKKSWrlNERHYGALQGLNkaetaakygEEQVNIWRRSFDVPpppidESDPRSPH-NDPRYAHLDPKVlpltes 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 499269880  133 -------SIP------------GERLLVVCHGGVIRA 150
Cdd:TIGR01258 151 lkdtiarVLPywndeiapdllsGKRVLIVAHGNSLRA 187
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-65 5.41e-07

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 48.50  E-value: 5.41e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499269880   1 MKRIILVRHGESAWNSVRRLQGQADIGLSARGEAQAT-ALRATIEA-MRPDHVIASDLLRARHTAAL 65
Cdd:PRK14120   4 TYTLVLLRHGESEWNAKNLFTGWVDVDLTEKGEAEAKrGGELLAEAgVLPDVVYTSLLRRAIRTANL 70
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
2-62 5.84e-07

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 48.32  E-value: 5.84e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499269880   2 KRIILVRHGESAWNSVRRLQGQADIGLSARGEAQATA----LRAtiEAMRPDHVIASDLLRARHT 62
Cdd:PRK14115   1 TKLVLIRHGESQWNKENRFTGWTDVDLSEKGVSEAKAagklLKE--EGYTFDVAYTSVLKRAIRT 63
gpmA PRK14117
phosphoglyceromutase; Provisional
 1-141 1.17e-05

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 44.63  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   1 MKRIILVRHGESAWNSVRRLQGQADIGLSARGEAQATALRATIEA--MRPDHVIASDLLRARHTAALLGYPHAQL----- 73
Cdd:PRK14117   1 MVKLVFARHGESEWNKANLFTGWADVDLSEKGTQQAIDAGKLIKEagIEFDLAFTSVLKRAIKTTNLALEASDQLwvpve 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499269880  74 -SPALREIDVGDWTGRAIGDLMAE--DQDAYLGWRAGTYAPRGGERWQEF---RDRVTAGLGKAVSIPGERLLV 141
Cdd:PRK14117  81 kSWRLNERHYGGLTGKNKAEAAEQfgDEQVHIWRRSYDVLPPAMAKDDEYsahTDRRYASLDDSVIPDAENLKV 154
gpmA PRK14119
phosphoglyceromutase; Provisional
 1-62 5.39e-05

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 42.57  E-value: 5.39e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499269880   1 MKRIILVRHGESAWNSVRRLQGQADIGLSARG--EAQATALRATIEAMRPDHVIASDLLRARHT 62
Cdd:PRK14119   1 MPKLILCRHGQSEWNAKNLFTGWEDVNLSEQGinEATRAGEKVRENNIAIDVAFTSLLTRALDT 64
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
1-62 1.50e-04

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 41.05  E-value: 1.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499269880   1 MKRIILVRHGESAWNSVRRLQGQADIGLSARG--EAQATALRATIEAMRPDHVIASDLLRARHT 62
Cdd:PRK14116   1 MAKLVLIRHGQSEWNLSNQFTGWVDVDLSEKGveEAKKAGRLIKEAGLEFDQAYTSVLTRAIKT 64
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 2-149 1.60e-04

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 41.33  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880   2 KRIILVRHG----ESAWN-SVRRL----QGQADIglsaRGEAQATALRATIEAMRPDHVIASDLLRARHTAALL--GYPH 70
Cdd:PTZ00122 103 RQIILVRHGqyinESSNDdNIKRLtelgKEQARI----TGKYLKEQFGEILVDKKVKAIYHSDMTRAKETAEIIseAFPG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499269880  71 AQL--SPALREidvgdwtgraigdlmaedqdaylGWragTYAP----RG----GERWQEFRDRVTAGLGKAVSIPGERL- 139
Cdd:PTZ00122 179 VRLieDPNLAE-----------------------GV---PCAPdppsRGfkptIEEILEDMKRIEAAFEKYFHRPVEDEd 232

                        170
                 ....*....|...
gi 499269880 140 ---LVVCHGGVIR 149
Cdd:PTZ00122 233 sveIIVCHGNVIR 245
 
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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