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Conserved domains on  [gi|495102390|ref|WP_007827213|]
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histidine phosphatase family protein [Streptomyces sp. Tu6071]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10447784)

histidine phosphatase family protein contains a conserved His residue that is transiently phosphorylated during the catalytic cycle; similar to fructose-2,6-bisphosphatase TIGAR

CATH:  3.40.50.1240
EC:  3.1.3.-
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 ...
 7-185 1.77e-22

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


:

Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 89.58  E-value: 1.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390    7 VHLVRHAEPA---------PDGSGLTARGRGQAELLGERLKRLPLTSLHHGPLPRAAETARIVGERAGVRPEPAET---- 73
Cdd:pfam00300   1 LYLVRHGETEwnlegrfqgRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRlrei 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390   74 -AGDY--VPHLPRRDELPPHLADFyLGFLADTTPEEAEAGRALARRATDLYTGPAE---GDTVrhdVVVTHNFLVAWLVR 147
Cdd:pfam00300  81 dFGDWegLTFEEIAERYPEEYDAW-LADPADYRPPGGESLADVRARVRAALEELAArhpGKTV---LVVSHGGVIRALLA 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 495102390  148 EALHAPRWRWLGINHSHASLTTIRHTPGRAPCLHVQND 185
Cdd:pfam00300 157 HLLGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 7-185 1.77e-22

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


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 89.58  E-value: 1.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390    7 VHLVRHAEPA---------PDGSGLTARGRGQAELLGERLKRLPLTSLHHGPLPRAAETARIVGERAGVRPEPAET---- 73
Cdd:pfam00300   1 LYLVRHGETEwnlegrfqgRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRlrei 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390   74 -AGDY--VPHLPRRDELPPHLADFyLGFLADTTPEEAEAGRALARRATDLYTGPAE---GDTVrhdVVVTHNFLVAWLVR 147
Cdd:pfam00300  81 dFGDWegLTFEEIAERYPEEYDAW-LADPADYRPPGGESLADVRARVRAALEELAArhpGKTV---LVVSHGGVIRALLA 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 495102390  148 EALHAPRWRWLGINHSHASLTTIRHTPGRAPCLHVQND 185
Cdd:pfam00300 157 HLLGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
7-176 1.05e-21

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 87.69  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390   7 VHLVRHAEPA---------PDGSGLTARGRGQAELLGERLKRLPLTSLHHGPLPRAAETARIVGERAGVRPEPAET---- 73
Cdd:COG0406    4 LYLVRHGETEwnaegrlqgRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPRlrei 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390  74 -AGDYvpHLPRRDELPPHLADFYLGFLAD---TTPEEAEAGRALARRATDLYTGPAEGDTVRHDVVVTHNFLVAWLVREA 149
Cdd:COG0406   84 dFGDW--EGLTFAELEARYPEALAAWLADpaeFRPPGGESLADVQARVRAALEELLARHPGGTVLVVTHGGVIRALLAHL 161

                        170       180
                 ....*....|....*....|....*..
gi 495102390 150 LHAPRWRWLGINHSHASLTTIRHTPGR 176
Cdd:COG0406  162 LGLPLEAFWRLRIDNASVTVLEFDDGR 188
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 2-170 7.49e-11

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 59.82  E-value: 7.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390   2 PATRFVH--LVRHAEPAPDGS------GLTARGRGQAELLGERLKRL--------PLTSLHHGPLPRAAETARIVGERAG 65
Cdd:PTZ00122  98 SASHQRQiiLVRHGQYINESSnddnikRLTELGKEQARITGKYLKEQfgeilvdkKVKAIYHSDMTRAKETAEIISEAFP 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390  66 VRP---EPAETAGdyVPHLPRrdelPPHLadfylGFLADTTPEEAEAGRALARRATDLYTGPAEGDTVrhDVVVTHNFLV 142
Cdd:PTZ00122 178 GVRlieDPNLAEG--VPCAPD----PPSR-----GFKPTIEEILEDMKRIEAAFEKYFHRPVEDEDSV--EIIVCHGNVI 244

                        170       180
                 ....*....|....*....|....*...
gi 495102390 143 AWLVREALHAPRWRWLGINHSHASLTTI 170
Cdd:PTZ00122 245 RYLVCRALQLPPEAWLRLSLYNCGITWI 272
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 7-62 3.35e-07

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: 48.09  E-value: 3.35e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495102390   7 VHLVRHAEPAPDGSG---------LTARGRGQAELLGERLKRL--PLTSLHHGPLPRAAETARIVGE 62
Cdd:cd07067    2 LYLVRHGESEWNAEGrfqgwtdvpLTEKGREQARALGKRLKELgiKFDRIYSSPLKRAIQTAEIILE 68
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 7-138 4.73e-06

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: 44.76  E-value: 4.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390     7 VHLVRHAEPA---------PDGSGLTARGRGQAELLGERLKRLPLTSLHH---GPLPRAAETARIVGERAGVRP----EP 70
Cdd:smart00855   2 LYLIRHGETEwnregrlygDTDVPLTELGRAQAEALGRLLASLLLPRFDVvysSPLKRARQTAEALAIALGLPGlrerDF 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390    71 AETAGDYVPHLPRRDELPPHLADFYLGFLADTTPEEAEAGRALARRATDLYTGPAEGDTVRHD--VVVTH 138
Cdd:smart00855  82 GAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPPAPPGGESLADLVERVEPALDELIATADASGQnvLIVSH 151
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 7-185 1.77e-22

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


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 89.58  E-value: 1.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390    7 VHLVRHAEPA---------PDGSGLTARGRGQAELLGERLKRLPLTSLHHGPLPRAAETARIVGERAGVRPEPAET---- 73
Cdd:pfam00300   1 LYLVRHGETEwnlegrfqgRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRlrei 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390   74 -AGDY--VPHLPRRDELPPHLADFyLGFLADTTPEEAEAGRALARRATDLYTGPAE---GDTVrhdVVVTHNFLVAWLVR 147
Cdd:pfam00300  81 dFGDWegLTFEEIAERYPEEYDAW-LADPADYRPPGGESLADVRARVRAALEELAArhpGKTV---LVVSHGGVIRALLA 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 495102390  148 EALHAPRWRWLGINHSHASLTTIRHTPGRAPCLHVQND 185
Cdd:pfam00300 157 HLLGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
7-176 1.05e-21

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 87.69  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390   7 VHLVRHAEPA---------PDGSGLTARGRGQAELLGERLKRLPLTSLHHGPLPRAAETARIVGERAGVRPEPAET---- 73
Cdd:COG0406    4 LYLVRHGETEwnaegrlqgRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPRlrei 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390  74 -AGDYvpHLPRRDELPPHLADFYLGFLAD---TTPEEAEAGRALARRATDLYTGPAEGDTVRHDVVVTHNFLVAWLVREA 149
Cdd:COG0406   84 dFGDW--EGLTFAELEARYPEALAAWLADpaeFRPPGGESLADVQARVRAALEELLARHPGGTVLVVTHGGVIRALLAHL 161

                        170       180
                 ....*....|....*....|....*..
gi 495102390 150 LHAPRWRWLGINHSHASLTTIRHTPGR 176
Cdd:COG0406  162 LGLPLEAFWRLRIDNASVTVLEFDDGR 188
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 2-170 7.49e-11

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 59.82  E-value: 7.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390   2 PATRFVH--LVRHAEPAPDGS------GLTARGRGQAELLGERLKRL--------PLTSLHHGPLPRAAETARIVGERAG 65
Cdd:PTZ00122  98 SASHQRQiiLVRHGQYINESSnddnikRLTELGKEQARITGKYLKEQfgeilvdkKVKAIYHSDMTRAKETAEIISEAFP 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390  66 VRP---EPAETAGdyVPHLPRrdelPPHLadfylGFLADTTPEEAEAGRALARRATDLYTGPAEGDTVrhDVVVTHNFLV 142
Cdd:PTZ00122 178 GVRlieDPNLAEG--VPCAPD----PPSR-----GFKPTIEEILEDMKRIEAAFEKYFHRPVEDEDSV--EIIVCHGNVI 244

                        170       180
                 ....*....|....*....|....*...
gi 495102390 143 AWLVREALHAPRWRWLGINHSHASLTTI 170
Cdd:PTZ00122 245 RYLVCRALQLPPEAWLRLSLYNCGITWI 272
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
9-158 2.01e-07

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 48.72  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390   9 LVRHAEPAPDGSG-------LTARGRGQAELLGERLKR--LPLTSLHHGPLPRAAETARIVGERAGVRPEPAETAGdyvp 79
Cdd:COG2062    3 LVRHAKAEWRAPGgddfdrpLTERGRRQARAMARWLAAlgLKPDRILSSPALRARQTAEILAEALGLPPKVEVEDE---- 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495102390  80 hlprrdelpphladfylgfLADTTPEEAeagRALARRAtdlytgpAEGDTVrhdVVVTHNFLVAWLVREALHAPRWRWL 158
Cdd:COG2062   79 -------------------LYDADPEDL---LDLLREL-------DDGETV---LLVGHNPGLSELAALLAGGEPLDGF 125
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 7-62 3.35e-07

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: 48.09  E-value: 3.35e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495102390   7 VHLVRHAEPAPDGSG---------LTARGRGQAELLGERLKRL--PLTSLHHGPLPRAAETARIVGE 62
Cdd:cd07067    2 LYLVRHGESEWNAEGrfqgwtdvpLTEKGREQARALGKRLKELgiKFDRIYSSPLKRAIQTAEIILE 68
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 7-62 1.53e-06

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: 46.25  E-value: 1.53e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495102390   7 VHLVRHAEPAPDGSG---------LTARGRGQAELLGERLKRLPLTSLH--HGPLPRAAETARIVGE 62
Cdd:cd07040    2 LYLVRHGEREPNAEGrftgwgdgpLTEKGRQQARELGKALRERYIKFDRiySSPLKRAIQTAEIILE 68
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 7-138 4.73e-06

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: 44.76  E-value: 4.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390     7 VHLVRHAEPA---------PDGSGLTARGRGQAELLGERLKRLPLTSLHH---GPLPRAAETARIVGERAGVRP----EP 70
Cdd:smart00855   2 LYLIRHGETEwnregrlygDTDVPLTELGRAQAEALGRLLASLLLPRFDVvysSPLKRARQTAEALAIALGLPGlrerDF 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390    71 AETAGDYVPHLPRRDELPPHLADFYLGFLADTTPEEAEAGRALARRATDLYTGPAEGDTVRHD--VVVTH 138
Cdd:smart00855  82 GAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPPAPPGGESLADLVERVEPALDELIATADASGQnvLIVSH 151
PRK13463 PRK13463
phosphoserine phosphatase 1;
7-63 1.54e-04

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 41.19  E-value: 1.54e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495102390   7 VHLVRHAEP---------APDGSGLTARGRGQAELLGERLKRLPLTSLHHGPLPRAAETARIV-GER 63
Cdd:PRK13463   5 VYVTRHGETewnvakrmqGRKNSALTENGILQAKQLGERMKDLSIHAIYSSPSERTLHTAELIkGER 71
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
9-112 3.27e-04

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 40.03  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495102390   9 LVRHAEPAPDGSG---------LTARGRGQAELLGERLKRLPLTSLHHGPLPRAAETARIVgerAGVRPEPAETagdyvp 79
Cdd:PRK15004   5 LVRHGETQANVDGlysghaptpLTARGIEQAQNLHTLLRDVPFDLVLCSELERAQHTARLV---LSDRQLPVHI------ 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 495102390  80 hLPRRDELppHLADFYLGFLADTTPEEAEAGRA 112
Cdd:PRK15004  76 -IPELNEM--FFGDWEMRHHRDLMQEDAENYAA 105
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
7-65 1.62e-03

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 38.17  E-value: 1.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495102390   7 VHLVRHAEP---------APDGSGLTARGRGQAELLGERLKRLPLTSLHHGPLPRAAETARIVGERAG 65
Cdd:PRK03482   4 VYLVRHGETqwnaerriqGQSDSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAEIIAQACG 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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