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Conserved domains on  [gi|1393170003|ref|NP_001350637|]
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bisphosphoglycerate mutase isoform 2 [Mus musculus]

Protein Classification

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase( domain architecture ID 1908652)

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GpmA super family cl41876
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 4-112 6.93e-61

Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-dependent) is part of the Pathway/BioSystem: Glycolysis


The actual alignment was detected with superfamily member COG0588:

Pssm-ID: 440353  Cd Length: 229  Bit Score: 187.98  E-value: 6.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   4 HKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVES 83
Cdd:COG0588     1 YKLVLLRHGESEWNLENRFTGWTDVDLSEKGRAEAKRAGRLLKEAGFLFDVAYTSVLKRAIRTLWIVLDEMDRLWIPVEK 80

                          90       100
                  ....*....|....*....|....*....
gi 1393170003  84 SWRLNERHYGALIGLNREKMALNHGEEQV 112
Cdd:COG0588    81 SWRLNERHYGALQGLNKAETAAKYGEEQV 109
 
Name Accession Description Interval E-value
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 4-112 6.93e-61

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: 187.98  E-value: 6.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   4 HKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVES 83
Cdd:COG0588     1 YKLVLLRHGESEWNLENRFTGWTDVDLSEKGRAEAKRAGRLLKEAGFLFDVAYTSVLKRAIRTLWIVLDEMDRLWIPVEK 80

                          90       100
                  ....*....|....*....|....*....
gi 1393170003  84 SWRLNERHYGALIGLNREKMALNHGEEQV 112
Cdd:COG0588    81 SWRLNERHYGALQGLNKAETAAKYGEEQV 109
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
4-116 5.46e-56

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 175.82  E-value: 5.46e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   4 HKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVES 83
Cdd:PRK14115    1 TKLVLIRHGESQWNKENRFTGWTDVDLSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTLWIVLDELDQMWLPVEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1393170003  84 SWRLNERHYGALIGLNREKMALNHGEEQVSQTR 116
Cdd:PRK14115   81 SWRLNERHYGALQGLNKAETAAKYGDEQVKIWR 113
pgm_1 TIGR01258
phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are ...
 4-116 5.76e-53

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: 168.36  E-value: 5.76e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   4 HKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVES 83
Cdd:TIGR01258   1 MKLVLVRHGESEWNALNLFTGWVDVKLSEKGQQEAKRAGELLKEEGYEFDVAYTSLLKRAIHTLNIALDELDQLWIPVKK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1393170003  84 SWRLNERHYGALIGLNREKMALNHGEEQVSQTR 116
Cdd:TIGR01258  81 SWRLNERHYGALQGLNKAETAAKYGEEQVNIWR 113
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 5-112 4.54e-30

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: 107.02  E-value: 4.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELgqEWVPVESS 84
Cdd:cd07067     1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEEL--PGLPVEVD 78

                          90       100
                  ....*....|....*....|....*...
gi 1393170003  85 WRLNERHYGALIglnrEKMALNHGEEQV 112
Cdd:cd07067    79 PRLREARVLPAL----EELIAPHDGKNV 102
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 5-116 4.32e-26

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 96.76  E-value: 4.32e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003    5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKAL-NFEFDLVFTSILNRSIHTAWLILEELGQewvpves 83
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLASLlLPRFDVVYSSPLKRARQTAEALAIALGL------- 73

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1393170003   84 sWRLNERHYGALIGLNREKMALNHGEEQVSQTR 116
Cdd:smart00855  74 -PGLRERDFGAWEGLTWDEIAAKYPEEYLAAWR 105
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-110 7.83e-21

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: 84.18  E-value: 7.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   6 LIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNfeFDLVFTSILNRSIHTAWLILEELGqewVPVESSW 85
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEP--FDAIYSSPLKRARQTAEIIAEALG---LPVEIDP 75

                          90       100
                  ....*....|....*....|....*
gi 1393170003  86 RLNERHYGALIGLNREKMALNHGEE 110
Cdd:pfam00300  76 RLREIDFGDWEGLTFEEIAERYPEE 100
 
Name Accession Description Interval E-value
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 4-112 6.93e-61

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: 187.98  E-value: 6.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   4 HKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVES 83
Cdd:COG0588     1 YKLVLLRHGESEWNLENRFTGWTDVDLSEKGRAEAKRAGRLLKEAGFLFDVAYTSVLKRAIRTLWIVLDEMDRLWIPVEK 80

                          90       100
                  ....*....|....*....|....*....
gi 1393170003  84 SWRLNERHYGALIGLNREKMALNHGEEQV 112
Cdd:COG0588    81 SWRLNERHYGALQGLNKAETAAKYGEEQV 109
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
4-116 5.46e-56

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 175.82  E-value: 5.46e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   4 HKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVES 83
Cdd:PRK14115    1 TKLVLIRHGESQWNKENRFTGWTDVDLSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTLWIVLDELDQMWLPVEK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1393170003  84 SWRLNERHYGALIGLNREKMALNHGEEQVSQTR 116
Cdd:PRK14115   81 SWRLNERHYGALQGLNKAETAAKYGDEQVKIWR 113
pgm_1 TIGR01258
phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are ...
 4-116 5.76e-53

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: 168.36  E-value: 5.76e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   4 HKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVES 83
Cdd:TIGR01258   1 MKLVLVRHGESEWNALNLFTGWVDVKLSEKGQQEAKRAGELLKEEGYEFDVAYTSLLKRAIHTLNIALDELDQLWIPVKK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1393170003  84 SWRLNERHYGALIGLNREKMALNHGEEQVSQTR 116
Cdd:TIGR01258  81 SWRLNERHYGALQGLNKAETAAKYGEEQVNIWR 113
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
 16-116 2.52e-50

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 161.36  E-value: 2.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003  16 WNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVESSWRLNERHYGAL 95
Cdd:PTZ00123    1 WNKENRFTGWTDVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAWIVLEELGQLHVPVIKSWRLNERHYGAL 80

                          90       100
                  ....*....|....*....|.
gi 1393170003  96 IGLNREKMALNHGEEQVSQTR 116
Cdd:PTZ00123   81 QGLNKSETAEKHGEEQVKIWR 101
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-111 5.36e-43

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 142.87  E-value: 5.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   1 MSKHKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVP 80
Cdd:PRK14120    2 MMTYTLVLLRHGESEWNAKNLFTGWVDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRTANLALDAADRLWIP 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1393170003  81 VESSWRLNERHYGALIGLNREKMALNHGEEQ 111
Cdd:PRK14120   82 VRRSWRLNERHYGALQGKDKAETKAEYGEEQ 112
gpmA PRK14117
phosphoglyceromutase; Provisional
 5-112 4.12e-41

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 137.46  E-value: 4.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVESS 84
Cdd:PRK14117    3 KLVFARHGESEWNKANLFTGWADVDLSEKGTQQAIDAGKLIKEAGIEFDLAFTSVLKRAIKTTNLALEASDQLWVPVEKS 82

                          90       100
                  ....*....|....*....|....*...
gi 1393170003  85 WRLNERHYGALIGLNREKMALNHGEEQV 112
Cdd:PRK14117   83 WRLNERHYGGLTGKNKAEAAEQFGDEQV 110
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
5-125 1.76e-39

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 133.50  E-value: 1.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVESS 84
Cdd:PRK14116    3 KLVLIRHGQSEWNLSNQFTGWVDVDLSEKGVEEAKKAGRLIKEAGLEFDQAYTSVLTRAIKTLHYALEESDQLWIPETKT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1393170003  85 WRLNERHYGALIGLNREKMALNHGEEQVSQTRILSTSLCPL 125
Cdd:PRK14116   83 WRLNERHYGALQGLNKKETAEKYGDEQVHIWRRSYDVLPPL 123
gpmA PRK14118
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
5-112 8.98e-39

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172608  Cd Length: 227  Bit Score: 131.63  E-value: 8.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVESS 84
Cdd:PRK14118    2 ELVFIRHGFSEWNAKNLFTGWRDVNLTERGVEEAKAAGKKLKEAGYEFDIAFTSVLTRAIKTCNIVLEESNQLWIPQVKN 81

                          90       100
                  ....*....|....*....|....*...
gi 1393170003  85 WRLNERHYGALIGLNREKMALNHGEEQV 112
Cdd:PRK14118   82 WRLNERHYGALQGLDKKATAEQYGDEQV 109
gpmA PRK14119
phosphoglyceromutase; Provisional
 5-116 1.61e-38

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 130.78  E-value: 1.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVESS 84
Cdd:PRK14119    3 KLILCRHGQSEWNAKNLFTGWEDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTTHYILTESKQQWIPVYKS 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1393170003  85 WRLNERHYGALIGLNREKMALNHGEEQVSQTR 116
Cdd:PRK14119   83 WRLNERHYGGLQGLNKDDARKEFGEEQVHIWR 114
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 6-112 2.08e-32

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 114.40  E-value: 2.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   6 LIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVESSW 85
Cdd:PRK01295    5 LVLVRHGQSEWNLKNLFTGWRDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLILEELGQPGLETIRDQ 84

                          90       100
                  ....*....|....*....|....*..
gi 1393170003  86 RLNERHYGALIGLNREKMALNHGEEQV 112
Cdd:PRK01295   85 ALNERDYGDLSGLNKDDARAKWGEEQV 111
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 5-112 4.54e-30

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: 107.02  E-value: 4.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELgqEWVPVESS 84
Cdd:cd07067     1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEEL--PGLPVEVD 78

                          90       100
                  ....*....|....*....|....*...
gi 1393170003  85 WRLNERHYGALIglnrEKMALNHGEEQV 112
Cdd:cd07067    79 PRLREARVLPAL----EELIAPHDGKNV 102
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
5-116 2.04e-27

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 102.11  E-value: 2.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKalNFEFDLVFTSILNRSIHTAWLIL------------- 71
Cdd:PRK01112    3 LLILLRHGQSVWNAKNLFTGWVDIPLSQQGIAEAIAAGEKIK--DLPIDCIFTSTLVRSLMTALLAMtnhssgkipyivh 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1393170003  72 EELGQEW-------------VPVESSWRLNERHYGALIGLNREKMALNHGEEQVSQTR 116
Cdd:PRK01112   81 EEDDKKWmsriysdeepeqmIPLFQSSALNERMYGELQGKNKAETAEKFGEEQVKLWR 138
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 5-116 4.32e-26

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 96.76  E-value: 4.32e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003    5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKAL-NFEFDLVFTSILNRSIHTAWLILEELGQewvpves 83
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLASLlLPRFDVVYSSPLKRARQTAEALAIALGL------- 73

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1393170003   84 sWRLNERHYGALIGLNREKMALNHGEEQVSQTR 116
Cdd:smart00855  74 -PGLRERDFGAWEGLTWDEIAAKYPEEYLAAWR 105
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 5-86 1.51e-24

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: 92.86  E-value: 1.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQeWVPVESS 84
Cdd:cd07040     1 VLYLVRHGEREPNAEGRFTGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFE-GLPVEVD 79


                  ..
gi 1393170003  85 WR 86
Cdd:cd07040    80 PR 81
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-110 7.83e-21

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: 84.18  E-value: 7.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   6 LIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNfeFDLVFTSILNRSIHTAWLILEELGqewVPVESSW 85
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEP--FDAIYSSPLKRARQTAEIIAEALG---LPVEIDP 75

                          90       100
                  ....*....|....*....|....*
gi 1393170003  86 RLNERHYGALIGLNREKMALNHGEE 110
Cdd:pfam00300  76 RLREIDFGDWEGLTFEEIAERYPEE 100
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
5-110 6.78e-20

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 81.91  E-value: 6.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNfeFDLVFTSILNRSIHTAWLILEELGqewVPVESS 84
Cdd:COG0406     3 RLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIP--FDAVYSSPLQRARQTAEALAEALG---LPVEVD 77

                          90       100
                  ....*....|....*....|....*.
gi 1393170003  85 WRLNERHYGALIGLNREKMALNHGEE 110
Cdd:COG0406    78 PRLREIDFGDWEGLTFAELEARYPEA 103
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
5-94 3.59e-10

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 55.83  E-value: 3.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   5 KLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALnfEFDLVFTSILNRSIHTAWLILEELGqewVPVESS 84
Cdd:PRK15004    2 RLWLVRHGETQANVDGLYSGHAPTPLTARGIEQAQNLHTLLRDV--PFDLVLCSELERAQHTARLVLSDRQ---LPVHII 76

                          90
                  ....*....|
gi 1393170003  85 WRLNERHYGA 94
Cdd:PRK15004   77 PELNEMFFGD 86
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
6-98 6.75e-09

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 51.80  E-value: 6.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   6 LIILRHGEGQWNKEnrfcsWV---DQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEwVPVE 82
Cdd:COG2062     1 LILVRHAKAEWRAP-----GGddfDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLP-PKVE 74

                          90
                  ....*....|....*.
gi 1393170003  83 SSWRLNERHYGALIGL 98
Cdd:COG2062    75 VEDELYDADPEDLLDL 90
PRK13462 PRK13462
acid phosphatase; Provisional
 4-69 7.46e-08

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 49.83  E-value: 7.46e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393170003   4 HKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWL 69
Cdd:PRK13462    6 HRLLLLRHGETEWSKSGRHTGRTELELTETGRTQAELAGQALGELELDDPLVISSPRRRALDTAKL 71
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
8-111 3.48e-06

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 45.10  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   8 ILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFdlVFTSILNRSIHTAWLILEELGqewVPVESSWRL 87
Cdd:PRK03482    6 LVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVAERAKELGITH--IISSDLGRTRRTAEIIAQACG---CDIIFDPRL 80

                          90       100
                  ....*....|....*....|....
gi 1393170003  88 NERHYGALigLNREKMALNHGEEQ 111
Cdd:PRK03482   81 RELNMGVL--EKRHIDSLTEEEEG 102
PRK13463 PRK13463
phosphoserine phosphatase 1;
3-73 1.55e-05

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 43.11  E-value: 1.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393170003   3 KHKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEfdLVFTSILNRSIHTAWLILEE 73
Cdd:PRK13463    2 KTTVYVTRHGETEWNVAKRMQGRKNSALTENGILQAKQLGERMKDLSIH--AIYSSPSERTLHTAELIKGE 70
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 6-98 2.76e-04

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 39.96  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393170003   6 LIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNfEFDLVFTSILNRSIHTAWLILEELGqewVPVESSW 85
Cdd:PRK07238  174 LLLLRHGQTELSVQRRYSGRGNPELTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAAAKALG---LDVTVDD 249

                          90
                  ....*....|...
gi 1393170003  86 RLNERHYGALIGL 98
Cdd:PRK07238  250 DLIETDFGAWEGL 262
 
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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