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Conserved domains on  [gi|492452864|ref|WP_005849119|]
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histidine phosphatase family protein [Phocaeicola vulgatus]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10447784)

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:0003824
PubMed:  18092946
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-172 2.09e-47

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: 152.75  E-value: 2.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864    4 LYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLLREI 83
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRLREI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   84 DWGSWTGLAIKEV---------DLQHFPADV-----ETEAMLYERAGRFVDYLKEQYDGKQVLAVGHGLINRAVQAHIQG 149
Cdd:pfam00300  81 DFGDWEGLTFEEIaerypeeydAWLADPADYrppggESLADVRARVRAALEELAARHPGKTVLVVSHGGVIRALLAHLLG 160

                         170       180
                  ....*....|....*....|...
gi 492452864  150 VTLEHLRSVPkMNNAELRRFKLT 172
Cdd:pfam00300 161 LPLEALRRFP-LDNASLSILEFD 182
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-172 2.09e-47

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: 152.75  E-value: 2.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864    4 LYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLLREI 83
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRLREI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   84 DWGSWTGLAIKEV---------DLQHFPADV-----ETEAMLYERAGRFVDYLKEQYDGKQVLAVGHGLINRAVQAHIQG 149
Cdd:pfam00300  81 DFGDWEGLTFEEIaerypeeydAWLADPADYrppggESLADVRARVRAALEELAARHPGKTVLVVSHGGVIRALLAHLLG 160

                         170       180
                  ....*....|....*....|...
gi 492452864  150 VTLEHLRSVPkMNNAELRRFKLT 172
Cdd:pfam00300 161 LPLEALRRFP-LDNASLSILEFD 182
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-172 3.13e-47

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 152.41  E-value: 3.13e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   1 MITLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLL 80
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864  81 REIDWGSWTGLAIKEV--------------DLQHFPADVETEAMLYERAGRFVDYLKEQYDGKQVLAVGHGLINRAVQAH 146
Cdd:COG0406   81 REIDFGDWEGLTFAELearypealaawladPAEFRPPGGESLADVQARVRAALEELLARHPGGTVLVVTHGGVIRALLAH 160

                        170       180
                 ....*....|....*....|....*.
gi 492452864 147 IQGVTLEHLRSVPkMNNAELRRFKLT 172
Cdd:COG0406  161 LLGLPLEAFWRLR-IDNASVTVLEFD 185
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 4-155 6.25e-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: 120.42  E-value: 6.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864    4 LYLARHGQTEENiARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLLREI 83
Cdd:TIGR03162   1 LYLIRHGETDVN-AGLCYGQTDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAERRGLPIIKDDRLREM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   84 DWGSWTGLAIKEV------------DLQHFPA-DVETEAMLYERAGRFVDYLKEQYDGKQVLAVGHGLINRAVQAHIQGV 150
Cdd:TIGR03162  80 DFGDWEGRSWDEIpeaypeldawaaDWQHARPpGGESFADFYQRVSEFLEELLKAHEGDNVLIVTHGGVIRALLAHLLGL 159


                  ....*
gi 492452864  151 TLEHL 155
Cdd:TIGR03162 160 PLEQW 164
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-143 2.98e-29

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: 105.24  E-value: 2.98e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864     3 TLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLR---NISLDAVVSSDLKRCVDTARIAVEGRNLPwektvL 79
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLAsllLPRFDVVYSSPLKRARQTAEALAIALGLP-----G 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864    80 LREIDWGSWTGLAIKEVDLQHF-----------------PADVETEAMLYERAGRFVDYLKEQ--YDGKQVLAVGHGLIN 140
Cdd:smart00855  76 LRERDFGAWEGLTWDEIAAKYPeeylaawrdpydpappaPPGGESLADLVERVEPALDELIATadASGQNVLIVSHGGVI 155


                   ...
gi 492452864   141 RAV 143
Cdd:smart00855 156 RAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-171 1.53e-27

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: 100.86  E-value: 1.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   3 TLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRN--ISLDAVVSSDLKRCVDTARIAVEGR-NLPWEKTVL 79
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKElgIKFDRIYSSPLKRAIQTAEIILEELpGLPVEVDPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864  80 LREidwgswtglaikevdlqhfpadveteamlyERAGRFVDYLKEQYDGKQVLAVGHGLINRAVQAHIQGVTLEHLRSVp 159
Cdd:cd07067   81 LRE------------------------------ARVLPALEELIAPHDGKNVLIVSHGGVLRALLAYLLGLSDEDILRL- 129

                        170
                 ....*....|..
gi 492452864 160 KMNNAELRRFKL 171
Cdd:cd07067  130 NLPNGSISVLEL 141
PRK13463 PRK13463
phosphoserine phosphatase 1;
3-166 7.61e-25

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 95.12  E-value: 7.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   3 TLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLLRE 82
Cdd:PRK13463   4 TVYVTRHGETEWNVAKRMQGRKNSALTENGILQAKQLGERMKDLSIHAIYSSPSERTLHTAELIKGERDIPIIADEHFYE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864  83 IDWGSWTGLAIKEVDLQhFPADV---------------ETEAMLYERAGRFVDYLKEQYDGKQVLAVGHGLINRAVQAHI 147
Cdd:PRK13463  84 INMGIWEGQTIDDIERQ-YPDDIqlfwnephlfqstsgENFEAVHKRVIEGMQLLLEKHKGESILIVSHAAAAKLLVGHF 162

                        170
                 ....*....|....*....
gi 492452864 148 QGVTLEHLRSVPKMNNAEL 166
Cdd:PRK13463 163 AGIEIENVWDDPFMHSASL 181
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-172 2.09e-47

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: 152.75  E-value: 2.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864    4 LYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLLREI 83
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRLREI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   84 DWGSWTGLAIKEV---------DLQHFPADV-----ETEAMLYERAGRFVDYLKEQYDGKQVLAVGHGLINRAVQAHIQG 149
Cdd:pfam00300  81 DFGDWEGLTFEEIaerypeeydAWLADPADYrppggESLADVRARVRAALEELAARHPGKTVLVVSHGGVIRALLAHLLG 160

                         170       180
                  ....*....|....*....|...
gi 492452864  150 VTLEHLRSVPkMNNAELRRFKLT 172
Cdd:pfam00300 161 LPLEALRRFP-LDNASLSILEFD 182
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-172 3.13e-47

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 152.41  E-value: 3.13e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   1 MITLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLL 80
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864  81 REIDWGSWTGLAIKEV--------------DLQHFPADVETEAMLYERAGRFVDYLKEQYDGKQVLAVGHGLINRAVQAH 146
Cdd:COG0406   81 REIDFGDWEGLTFAELearypealaawladPAEFRPPGGESLADVQARVRAALEELLARHPGGTVLVVTHGGVIRALLAH 160

                        170       180
                 ....*....|....*....|....*.
gi 492452864 147 IQGVTLEHLRSVPkMNNAELRRFKLT 172
Cdd:COG0406  161 LLGLPLEAFWRLR-IDNASVTVLEFD 185
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 4-155 6.25e-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: 120.42  E-value: 6.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864    4 LYLARHGQTEENiARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLLREI 83
Cdd:TIGR03162   1 LYLIRHGETDVN-AGLCYGQTDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAERRGLPIIKDDRLREM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   84 DWGSWTGLAIKEV------------DLQHFPA-DVETEAMLYERAGRFVDYLKEQYDGKQVLAVGHGLINRAVQAHIQGV 150
Cdd:TIGR03162  80 DFGDWEGRSWDEIpeaypeldawaaDWQHARPpGGESFADFYQRVSEFLEELLKAHEGDNVLIVTHGGVIRALLAHLLGL 159


                  ....*
gi 492452864  151 TLEHL 155
Cdd:TIGR03162 160 PLEQW 164
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-143 2.98e-29

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: 105.24  E-value: 2.98e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864     3 TLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLR---NISLDAVVSSDLKRCVDTARIAVEGRNLPwektvL 79
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLAsllLPRFDVVYSSPLKRARQTAEALAIALGLP-----G 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864    80 LREIDWGSWTGLAIKEVDLQHF-----------------PADVETEAMLYERAGRFVDYLKEQ--YDGKQVLAVGHGLIN 140
Cdd:smart00855  76 LRERDFGAWEGLTWDEIAAKYPeeylaawrdpydpappaPPGGESLADLVERVEPALDELIATadASGQNVLIVSHGGVI 155


                   ...
gi 492452864   141 RAV 143
Cdd:smart00855 156 RAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-171 1.53e-27

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: 100.86  E-value: 1.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   3 TLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRN--ISLDAVVSSDLKRCVDTARIAVEGR-NLPWEKTVL 79
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKElgIKFDRIYSSPLKRAIQTAEIILEELpGLPVEVDPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864  80 LREidwgswtglaikevdlqhfpadveteamlyERAGRFVDYLKEQYDGKQVLAVGHGLINRAVQAHIQGVTLEHLRSVp 159
Cdd:cd07067   81 LRE------------------------------ARVLPALEELIAPHDGKNVLIVSHGGVLRALLAYLLGLSDEDILRL- 129

                        170
                 ....*....|..
gi 492452864 160 KMNNAELRRFKL 171
Cdd:cd07067  130 NLPNGSISVLEL 141
PRK13463 PRK13463
phosphoserine phosphatase 1;
3-166 7.61e-25

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 95.12  E-value: 7.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   3 TLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLLRE 82
Cdd:PRK13463   4 TVYVTRHGETEWNVAKRMQGRKNSALTENGILQAKQLGERMKDLSIHAIYSSPSERTLHTAELIKGERDIPIIADEHFYE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864  83 IDWGSWTGLAIKEVDLQhFPADV---------------ETEAMLYERAGRFVDYLKEQYDGKQVLAVGHGLINRAVQAHI 147
Cdd:PRK13463  84 INMGIWEGQTIDDIERQ-YPDDIqlfwnephlfqstsgENFEAVHKRVIEGMQLLLEKHKGESILIVSHAAAAKLLVGHF 162

                        170
                 ....*....|....*....
gi 492452864 148 QGVTLEHLRSVPKMNNAEL 166
Cdd:PRK13463 163 AGIEIENVWDDPFMHSASL 181
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
4-136 4.17e-24

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 93.19  E-value: 4.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   4 LYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLLREI 83
Cdd:PRK15004   3 LWLVRHGETQANVDGLYSGHAPTPLTARGIEQAQNLHTLLRDVPFDLVLCSELERAQHTARLVLSDRQLPVHIIPELNEM 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492452864  84 DWGSWtglaikEV----DLQH----------------FPADVETEAMLYERAGRFVDYLKEQYDGKQVLAVGH 136
Cdd:PRK15004  83 FFGDW------EMrhhrDLMQedaenyaawcndwqhaIPTNGEGFQAFSQRVERFIARLSAFQHYQNLLIVSH 149
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 3-145 4.30e-19

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 82.72  E-value: 4.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   3 TLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTL-RNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLLR 81
Cdd:PRK07238 173 RLLLLRHGQTELSVQRRYSGRGNPELTEVGRRQAAAAARYLaARGGIDAVVSSPLQRARDTAAAAAKALGLDVTVDDDLI 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864  82 EIDWGSWTGLAIKEVDlQHFPADV--------------ETEAMLYERAGRFVDYLKEQYDGKQVLAVGH-----GLINRA 142
Cdd:PRK07238 253 ETDFGAWEGLTFAEAA-ERDPELHrawladtsvappggESFDAVARRVRRARDRLIAEYPGATVLVVSHvtpikTLLRLA 331


                 ...
gi 492452864 143 VQA 145
Cdd:PRK07238 332 LDA 334
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 3-158 6.91e-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: 78.22  E-value: 6.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   3 TLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRN--ISLDAVVSSDLKRCVDTARIAVEGRNLPWEKtvll 80
Cdd:cd07040    1 VLYLVRHGEREPNAEGRFTGWGDGPLTEKGRQQARELGKALREryIKFDRIYSSPLKRAIQTAEIILEGLFEGLPV---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864  81 rEIDWGswtglaikevdlqhfpadveteamlyERAGRFVDYLKEQY--DGKQVLAVGHGLINRAVQAHIQGVTLEHLRSV 158
Cdd:cd07040   77 -EVDPR--------------------------ARVLNALLELLARHllDGKNVLIVSHGGTIRALLAALLGLSDEEILSL 129
PRK13462 PRK13462
acid phosphatase; Provisional
 4-143 5.34e-12

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 61.39  E-value: 5.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   4 LYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRNISLD--AVVSSDLKRCVDTARIAveGRNLPwEKTVLLR 81
Cdd:PRK13462   8 LLLLRHGETEWSKSGRHTGRTELELTETGRTQAELAGQALGELELDdpLVISSPRRRALDTAKLA--GLTVD-EVSGLLA 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864  82 EIDWGSWTGLA---IKEVD-----LQHFPADVETEAMLYERAGRFVDYLKEQYDGKQVLAVGHGLINRAV 143
Cdd:PRK13462  85 EWDYGSYEGLTtpqIRESEpdwlvWTHGCPGGESVAQVNERADRAVALALEHMESRDVVFVSHGHFSRAV 154
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
1-86 2.05e-10

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 57.04  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   1 MITLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIAVEGRNLPWEKTVLL 80
Cdd:PRK03482   1 MLQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAEIIAQACGCDIIFDPRL 80


                 ....*.
gi 492452864  81 REIDWG 86
Cdd:PRK03482  81 RELNMG 86
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
4-136 2.02e-09

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 53.34  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   4 LYLARHGQTEEN------IARifqghmpgTLTVEGIAQAEALRDTLR--NISLDAVVSSDLKRCVDTARIAVEGRNLpwe 75
Cdd:COG2062    1 LILVRHAKAEWRapggddFDR--------PLTERGRRQARAMARWLAalGLKPDRILSSPALRARQTAEILAEALGL--- 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492452864  76 ktvllreidwgswtglaikevdlqhfPADVETEAMLYER-AGRFVDYLKEQYDGKQVLAVGH 136
Cdd:COG2062   70 --------------------------PPKVEVEDELYDAdPEDLLDLLRELDDGETVLLVGH 105
gpmA PRK14117
phosphoglyceromutase; Provisional
 1-100 7.54e-09

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 53.10  E-value: 7.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   1 MITLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLR--NISLDAVVSSDLKRCVDTARIAVEGRNLPW---E 75
Cdd:PRK14117   1 MVKLVFARHGESEWNKANLFTGWADVDLSEKGTQQAIDAGKLIKeaGIEFDLAFTSVLKRAIKTTNLALEASDQLWvpvE 80

                         90       100
                 ....*....|....*....|....*
gi 492452864  76 KTVLLREIDWGSWTGLAIKEVDLQH 100
Cdd:PRK14117  81 KSWRLNERHYGGLTGKNKAEAAEQF 105
gpmA PRK14118
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
4-151 3.75e-07

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172608  Cd Length: 227  Bit Score: 48.04  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   4 LYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRN--ISLDAVVSSDLKRCVDTARIAVEGRN---LPWEKTV 78
Cdd:PRK14118   3 LVFIRHGFSEWNAKNLFTGWRDVNLTERGVEEAKAAGKKLKEagYEFDIAFTSVLTRAIKTCNIVLEESNqlwIPQVKNW 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864  79 LLREIDWGSWTGLAIKEVDLQ-----------------------------------HFPADV----ETEAMLYERAGRFV 119
Cdd:PRK14118  83 RLNERHYGALQGLDKKATAEQygdeqvhiwrrsydtlppdldpqdpnsahndrryaHLPADVvpdaENLKVTLERVLPFW 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 492452864 120 D--YLKEQYDGKQVLAVGHGLINRAVQAHIQGVT 151
Cdd:PRK14118 163 EdqIAPALLSGKRVLVAAHGNSLRALAKHIEGIS 196
gpmA PRK14119
phosphoglyceromutase; Provisional
 1-153 7.02e-07

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 47.58  E-value: 7.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   1 MITLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLR--NISLDAVVSSDLKRCVDTARIAVEGRN---LPWE 75
Cdd:PRK14119   1 MPKLILCRHGQSEWNAKNLFTGWEDVNLSEQGINEATRAGEKVRenNIAIDVAFTSLLTRALDTTHYILTESKqqwIPVY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864  76 KTVLLREIDWGSWTGL----AIKEV--DLQHF---------PADVET--EAMLYERAGRFVDY--------LKE------ 124
Cdd:PRK14119  81 KSWRLNERHYGGLQGLnkddARKEFgeEQVHIwrrsydvkpPAETEEqrEAYLADRRYNHLDKrmmpysesLKDtlvrvi 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 492452864 125 --------QY--DGKQVLAVGHGLINRAVQAHIQGVTLE 153
Cdd:PRK14119 161 pfwtdhisQYllDGQTVLVSAHGNSIRALIKYLEDVSDE 199
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 3-91 1.16e-06

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 46.61  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   3 TLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTL--RNISLDAVVSSDLKRCVDTARIAVE--GR-NLPWEKT 77
Cdd:PRK01295   4 TLVLVRHGQSEWNLKNLFTGWRDPDLTEQGVAEAKAAGRKLkaAGLKFDIAFTSALSRAQHTCQLILEelGQpGLETIRD 83

                         90
                 ....*....|....
gi 492452864  78 VLLREIDWGSWTGL 91
Cdd:PRK01295  84 QALNERDYGDLSGL 97
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
1-95 1.17e-06

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 46.83  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492452864   1 MITLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRN--ISLDAVVSSDLKRCVDTARIAVEGRN---LPWE 75
Cdd:PRK14116   1 MAKLVLIRHGQSEWNLSNQFTGWVDVDLSEKGVEEAKKAGRLIKEagLEFDQAYTSVLTRAIKTLHYALEESDqlwIPET 80

                         90       100
                 ....*....|....*....|
gi 492452864  76 KTVLLREIDWGSWTGLAIKE 95
Cdd:PRK14116  81 KTWRLNERHYGALQGLNKKE 100
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
1-66 1.52e-05

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 43.56  E-value: 1.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492452864   1 MITLYLARHGQTEENIARIFQGHMPGTLTVEGIAQAEALRDTLRNISLDAVVSSDLKRCVDTARIA 66
Cdd:PRK01112   1 MALLILLRHGQSVWNAKNLFTGWVDIPLSQQGIAEAIAAGEKIKDLPIDCIFTSTLVRSLMTALLA 66
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-74 2.14e-05

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 43.10  E-value: 2.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492452864   1 MITLYLARHGQTEENIARIFQGHMPGTLTVEGIAQA----EALRDtlRNISLDAVVSSDLKRCVDTARIAVEGRNLPW 74
Cdd:PRK14120   4 TYTLVLLRHGESEWNAKNLFTGWVDVDLTEKGEAEAkrggELLAE--AGVLPDVVYTSLLRRAIRTANLALDAADRLW 79
 
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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