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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554698641  55 VVVLFRHAERCDRSTNQCLSDKTG-ITVKGTQDARELGNAFSADIPDFDL-YSSNTVRTIQSATWFSAGKKLTV------ 126
Cdd:cd07040    1 VLYLVRHGEREPNAEGRFTGWGDGpLTEKGRQQARELGKALRERYIKFDRiYSSPLKRAIQTAEIILEGLFEGLpvevdp 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 554698641 127 DKRLLqcgNEIYSAIKdlQSKAPDKNIVIFTHNHCLTYIAK 167
Cdd:cd07040   81 RARVL---NALLELLA--RHLLDGKNVLIVSHGGTIRALLA 116

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 554698641    56 VVLFRHAE-------RCDRSTNQCLSDKtgitvkGTQDARELGNAFSADIPD-FD-LYSSNTVRTIQSATWFSAGKKL 124
Cdd:smart00855   2 LYLIRHGEtewnregRLYGDTDVPLTEL------GRAQAEALGRLLASLLLPrFDvVYSSPLKRARQTAEALAIALGL 73

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554698641  55 VVVLFRHAERCDRSTNQCLSDKTG-ITVKGTQDARELGNAFSADIPDFDL-YSSNTVRTIQSATWFSAGKKLTV------ 126
Cdd:cd07040    1 VLYLVRHGEREPNAEGRFTGWGDGpLTEKGRQQARELGKALRERYIKFDRiYSSPLKRAIQTAEIILEGLFEGLpvevdp 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 554698641 127 DKRLLqcgNEIYSAIKdlQSKAPDKNIVIFTHNHCLTYIAK 167
Cdd:cd07040   81 RARVL---NALLELLA--RHLLDGKNVLIVSHGGTIRALLA 116

Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of HAP (histidine acid phosphatases) and phytases (myo-inositol hexakisphosphate phosphohydrolases). The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. Functions in this subgroup include roles in metabolism, signaling, or regulation, for example Escherichia coli glucose-1-phosphatase functions to scavenge glucose from glucose-1-phosphate and the signaling molecules inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) are in vivo substrates for eukaryotic multiple inositol polyphosphate phosphatase 1 (Minpp1). Phytases scavenge phosphate from extracellular sources and are added to animal feed while prostatic acid phosphatase (PAP) has been used for many years as a serum marker for prostate cancer. Recently PAP has been shown in mouse models to suppress pain by functioning as an ecto-5prime-nucleotidase. In vivo it dephosphorylates extracellular adenosine monophosphate (AMP) generating adenosine,and leading to the activation of A1-adenosine receptors in dorsal spinal cord.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 554698641  55 VVVLFRHAercDRSTNQclsdktgITVKGTQDARELGNAFSADIP-----------DFDLYSSNTVRTIQSATWFSAG 121
Cdd:cd07061    5 VQVLSRHG---DRYPGE-------LTPFGRQQAFELGRYFRQRYGellllhsynrsDLYIRSSDSQRTLQSAQAFLAG 72

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 554698641    56 VVLFRHAE-------RCDRSTNQCLSDKtgitvkGTQDARELGNAFSADIPD-FD-LYSSNTVRTIQSATWFSAGKKL 124
Cdd:smart00855   2 LYLIRHGEtewnregRLYGDTDVPLTEL------GRAQAEALGRLLASLLLPrFDvVYSSPLKRARQTAEALAIALGL 73