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Conserved domains on  [gi|1393428003|ref|NP_001350638|]
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bisphosphoglycerate mutase isoform 3 [Mus musculus]

Protein Classification

histidine phosphatase family protein( domain architecture ID 27749)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HP super family cl11399
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 1-153 3.54e-70

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.


The actual alignment was detected with superfamily member PRK14115:

Pssm-ID: 472174  Cd Length: 247  Bit Score: 211.64  E-value: 3.54e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   1 MALNHGEEQVRLWRRSYNVTPPPIEESHPYFHeiYSDRRYKvcDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKS 80
Cdd:PRK14115  100 TAAKYGDEQVKIWRRSYDVPPPALEKDDERYP--GHDPRYA--KLPEEELPLTESLKDTIARVLPYWNETIAPQLKSGKR 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393428003  81 ILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGpHQFLGNQEAIQAAIKKVDDQGKVK 153
Cdd:PRK14115  176 VLIAAHGNSLRALVKYLDNISDEEILELNIPTGVPLVYELDENLKPIK-HYYLGDADEIAAAAAAVANQGKAK 247
 
Name Accession Description Interval E-value
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
1-153 3.54e-70

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 211.64  E-value: 3.54e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   1 MALNHGEEQVRLWRRSYNVTPPPIEESHPYFHeiYSDRRYKvcDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKS 80
Cdd:PRK14115  100 TAAKYGDEQVKIWRRSYDVPPPALEKDDERYP--GHDPRYA--KLPEEELPLTESLKDTIARVLPYWNETIAPQLKSGKR 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393428003  81 ILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGpHQFLGNQEAIQAAIKKVDDQGKVK 153
Cdd:PRK14115  176 VLIAAHGNSLRALVKYLDNISDEEILELNIPTGVPLVYELDENLKPIK-HYYLGDADEIAAAAAAVANQGKAK 247
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 5-135 4.55e-66

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: 200.69  E-value: 4.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   5 HGEEQVRLWRRSYNVTPPPIEESHPYFHeiYSDRRYKvcDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKSILIS 84
Cdd:COG0588   104 YGEEQVHIWRRSYDVPPPPLDPDDPRHP--GNDPRYA--DLPPAELPLTESLKDTVARVLPYWEEEIAPALKAGKRVLIA 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1393428003  85 AHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGpHQFLGN 135
Cdd:COG0588   180 AHGNSLRALVKHLDGISDEEIVGLNIPTGIPLVYELDDDLKPIK-KYYLDD 229
pgm_1 TIGR01258
phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are ...
 5-151 1.68e-65

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: 199.94  E-value: 1.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   5 HGEEQVRLWRRSYNVTPPPIEESHPYFHEiySDRRYKvcDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKSILIS 84
Cdd:TIGR01258 104 YGEEQVNIWRRSFDVPPPPIDESDPRSPH--NDPRYA--HLDPKVLPLTESLKDTIARVLPYWNDEIAPDLLSGKRVLIV 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393428003  85 AHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHqFLGNQEAIQAAIKKVDDQGK 151
Cdd:TIGR01258 180 AHGNSLRALVKHLEGISDEEILELNIPTGIPLVYELDENLKPIKHY-YLGDPEAAAAAAEAVANQGK 245
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 57-123 1.48e-16

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


Pssm-ID: 132716 [Multi-domain]  Cd Length: 153  Bit Score: 71.68  E-value: 1.48e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393428003  57 KDVLERLLPYWKERIAPEILKGKSILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDEN 123
Cdd:cd07040    78 VDPRARVLNALLELLARHLLDGKNVLIVSHGGTIRALLAALLGLSDEEILSLNLPNGSILVLELDEC 144
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 23-93 1.11e-09

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: 54.00  E-value: 1.11e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393428003   23 PIEESHPYFHEIYSDRRYKVCDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKSILISAHGNSSRAL 93
Cdd:smart00855  88 TWDEIAAKYPEEYLAAWRDPYDPAPPAPPGGESLADLVERVEPALDELIATADASGQNVLIVSHGGVIRAL 158
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 20-113 2.39e-06

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: 45.28  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003  20 TPPPIEESHPYFHEIYSDRRYKVcdvpldQLPRSESLKDVLERLLPyWKERIAPEiLKGKSILISAHGNSSRALLKHLEG 99
Cdd:pfam00300  89 TFEEIAERYPEEYDAWLADPADY------RPPGGESLADVRARVRA-ALEELAAR-HPGKTVLVVSHGGVIRALLAHLLG 160

                          90
                  ....*....|....
gi 1393428003 100 ISDEDIINITLPTG 113
Cdd:pfam00300 161 LPLEALRRFPLDNA 174
 
Name Accession Description Interval E-value
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
1-153 3.54e-70

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 211.64  E-value: 3.54e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   1 MALNHGEEQVRLWRRSYNVTPPPIEESHPYFHeiYSDRRYKvcDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKS 80
Cdd:PRK14115  100 TAAKYGDEQVKIWRRSYDVPPPALEKDDERYP--GHDPRYA--KLPEEELPLTESLKDTIARVLPYWNETIAPQLKSGKR 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393428003  81 ILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGpHQFLGNQEAIQAAIKKVDDQGKVK 153
Cdd:PRK14115  176 VLIAAHGNSLRALVKYLDNISDEEILELNIPTGVPLVYELDENLKPIK-HYYLGDADEIAAAAAAVANQGKAK 247
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
 2-154 1.61e-66

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 202.19  E-value: 1.61e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   2 ALNHGEEQVRLWRRSYNVTPPPIEESHPYFHEiySDRRYKvcDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKSI 81
Cdd:PTZ00123   89 AEKHGEEQVKIWRRSYDIPPPPLEKSDERYPG--NDPVYK--DIPKDALPNTECLKDTVERVLPYWEDHIAPDILAGKKV 164

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393428003  82 LISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGpHQFLGNQEAIQAAIKKVDDQGKVKQ 154
Cdd:PTZ00123  165 LVAAHGNSLRALVKYLDKMSEEDILELNIPTGVPLVYELDENLKPIK-KYYLLDEEELKAKMEAVANQGKAKS 236
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 5-135 4.55e-66

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: 200.69  E-value: 4.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   5 HGEEQVRLWRRSYNVTPPPIEESHPYFHeiYSDRRYKvcDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKSILIS 84
Cdd:COG0588   104 YGEEQVHIWRRSYDVPPPPLDPDDPRHP--GNDPRYA--DLPPAELPLTESLKDTVARVLPYWEEEIAPALKAGKRVLIA 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1393428003  85 AHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGpHQFLGN 135
Cdd:COG0588   180 AHGNSLRALVKHLDGISDEEIVGLNIPTGIPLVYELDDDLKPIK-KYYLDD 229
pgm_1 TIGR01258
phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are ...
 5-151 1.68e-65

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: 199.94  E-value: 1.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   5 HGEEQVRLWRRSYNVTPPPIEESHPYFHEiySDRRYKvcDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKSILIS 84
Cdd:TIGR01258 104 YGEEQVNIWRRSFDVPPPPIDESDPRSPH--NDPRYA--HLDPKVLPLTESLKDTIARVLPYWNDEIAPDLLSGKRVLIV 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393428003  85 AHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHqFLGNQEAIQAAIKKVDDQGK 151
Cdd:TIGR01258 180 AHGNSLRALVKHLEGISDEEILELNIPTGIPLVYELDENLKPIKHY-YLGDPEAAAAAAEAVANQGK 245
gpmA PRK14120
phosphoglyceromutase; Provisional
 6-151 2.87e-54

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 171.38  E-value: 2.87e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   6 GEEQVRLWRRSYNVTPPPIEESHPYFHEiySDRRYKvcdvPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKSILISA 85
Cdd:PRK14120  109 GEEQFMLWRRSYDTPPPPIEDGSEYSQD--NDPRYA----DLGVGPRTECLKDVVARFLPYWEDDIVPDLKAGKTVLIAA 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393428003  86 HGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGNQEAIQAAIKKVDDQGK 151
Cdd:PRK14120  183 HGNSLRALVKHLDGISDEDIAGLNIPTGIPLVYELDEDFKPLNPGGTYLDPEAAAAGAAAVANQGK 248
gpmA PRK14118
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
2-127 8.47e-47

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172608  Cd Length: 227  Bit Score: 151.66  E-value: 8.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   2 ALNHGEEQVRLWRRSYNVTPPPIEESHPyfHEIYSDRRYkvCDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKSI 81
Cdd:PRK14118  101 AEQYGDEQVHIWRRSYDTLPPDLDPQDP--NSAHNDRRY--AHLPADVVPDAENLKVTLERVLPFWEDQIAPALLSGKRV 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1393428003  82 LISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAV 127
Cdd:PRK14118  177 LVAAHGNSLRALAKHIEGISDADIMDLEIPTGQPLVYKLDDNLKVV 222
gpmA PRK14119
phosphoglyceromutase; Provisional
 6-130 1.00e-41

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 138.87  E-value: 1.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   6 GEEQVRLWRRSYNVTPPPIEESHpyfHEIY-SDRRYKVCDVPLdqLPRSESLKDVLERLLPYWKERIAPEILKGKSILIS 84
Cdd:PRK14119  106 GEEQVHIWRRSYDVKPPAETEEQ---REAYlADRRYNHLDKRM--MPYSESLKDTLVRVIPFWTDHISQYLLDGQTVLVS 180

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1393428003  85 AHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPH 130
Cdd:PRK14119  181 AHGNSIRALIKYLEDVSDEDIINYEIKTGAPLVYELTDDLEVIDKY 226
gpmA PRK14117
phosphoglyceromutase; Provisional
 2-134 1.52e-41

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 138.23  E-value: 1.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   2 ALNHGEEQVRLWRRSYNVTPPPIEESHPYfhEIYSDRRYKVCDVPLdqLPRSESLKDVLERLLPYWKERIAPEILKGKSI 81
Cdd:PRK14117  102 AEQFGDEQVHIWRRSYDVLPPAMAKDDEY--SAHTDRRYASLDDSV--IPDAENLKVTLERALPFWEDKIAPALKDGKNV 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1393428003  82 LISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHqFLG 134
Cdd:PRK14117  178 FVGAHGNSIRALVKHIKGLSDDEIMDVEIPNFPPLVFEFDEKLNVVKEY-YLG 229
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
2-128 1.89e-36

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 125.41  E-value: 1.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   2 ALNHGEEQVRLWRRSYNVTPPPIEESHPYfhEIYSDRRYKVCDVPLdqLPRSESLKDVLERLLPYWKERIAPEILKGKSI 81
Cdd:PRK14116  102 AEKYGDEQVHIWRRSYDVLPPLLDADDEG--SAAKDRRYANLDPRI--IPGGENLKVTLERVIPFWEDHIAPDLLDGKNV 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1393428003  82 LISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVG 128
Cdd:PRK14116  178 IIAAHGNSLRALTKYIENISDEDIMNLEMATGEPVVYDFDEKLNVVS 224
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
1-122 7.04e-29

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 105.57  E-value: 7.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   1 MALNHGEEQVRLWRRSYNVTPPpieeshpyfheiysdrrykvcdvpldqlpRSESLKDVLERLLPYWKERIAPEILKGKS 80
Cdd:PRK01112  125 TAEKFGEEQVKLWRRSYKTAPP-----------------------------QGESLEDTGQRTLPYFQNRILPHLQQGKN 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1393428003  81 ILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDE 122
Cdd:PRK01112  176 VFVSAHGNSLRSLIMDLEKLSEEEVLSLELPTGKPIVYEWTG 217
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 6-121 7.77e-28

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 102.46  E-value: 7.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003   6 GEEQVRLWRRSYNVTPPpieeshpyfheiysdrrykvcdvpldqlpRSESLKDVLERLLPYWKERIAPEILKGKSILISA 85
Cdd:PRK01295  107 GEEQVHIWRRSYDVPPP-----------------------------GGESLKDTGARVLPYYLQEILPRVLRGERVLVAA 157

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1393428003  86 HGNSSRALLKHLEGISDEDIINITLPTGVPILLELD 121
Cdd:PRK01295  158 HGNSLRALVMVLDGLTPEQILKLELATGVPIVYRLN 193
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 57-123 1.48e-16

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


Pssm-ID: 132716 [Multi-domain]  Cd Length: 153  Bit Score: 71.68  E-value: 1.48e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393428003  57 KDVLERLLPYWKERIAPEILKGKSILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDEN 123
Cdd:cd07040    78 VDPRARVLNALLELLARHLLDGKNVLIVSHGGTIRALLAALLGLSDEEILSLNLPNGSILVLELDEC 144
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 61-127 1.00e-15

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: 69.66  E-value: 1.00e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393428003  61 ERLLPYWKERIAPEilKGKSILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAV 127
Cdd:cd07067    84 ARVLPALEELIAPH--DGKNVLIVSHGGVLRALLAYLLGLSDEDILRLNLPNGSISVLELDENGGGV 148
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 23-93 1.11e-09

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: 54.00  E-value: 1.11e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393428003   23 PIEESHPYFHEIYSDRRYKVCDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKSILISAHGNSSRAL 93
Cdd:smart00855  88 TWDEIAAKYPEEYLAAWRDPYDPAPPAPPGGESLADLVERVEPALDELIATADASGQNVLIVSHGGVIRAL 158
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 20-113 2.39e-06

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: 45.28  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393428003  20 TPPPIEESHPYFHEIYSDRRYKVcdvpldQLPRSESLKDVLERLLPyWKERIAPEiLKGKSILISAHGNSSRALLKHLEG 99
Cdd:pfam00300  89 TFEEIAERYPEEYDAWLADPADY------RPPGGESLADVRARVRA-ALEELAAR-HPGKTVLVVSHGGVIRALLAHLLG 160

                          90
                  ....*....|....
gi 1393428003 100 ISDEDIINITLPTG 113
Cdd:pfam00300 161 LPLEALRRFPLDNA 174
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
49-122 1.17e-05

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 43.39  E-value: 1.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393428003  49 QLPRSESLKDVLERLLPYWkERIAPEiLKGKSILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDE 122
Cdd:COG0406   115 RPPGGESLADVQARVRAAL-EELLAR-HPGGTVLVVTHGGVIRALLAHLLGLPLEAFWRLRIDNASVTVLEFDD 186
 
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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