NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1933691799|gb|QPE83116|]
View 

histidine phosphatase family protein (plasmid) [Escherichia coli]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10794156)

histidine phosphatase family protein similar to Salmonella lipopolysaccharide core heptose(II)-phosphate phosphatase, which helps remodel lipopolysaccharide via removal of the Hep(II) phosphate in the LPS inner core region

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK15416 PRK15416
lipopolysaccharide core heptose(II)-phosphate phosphatase; Provisional
 1-193 3.53e-109

lipopolysaccharide core heptose(II)-phosphate phosphatase; Provisional


:

Pssm-ID: 185314  Cd Length: 201  Bit Score: 310.57  E-value: 3.53e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799   1 MMKPRSSYSKTAFILLFSVFLVAAVTK----AKSSLPDITLEQAKEINADNTVIFLFRHGERCDRSDMPCYSDKSGITIT 76
Cdd:PRK15416    4 FCRSSSKSKKYFFILLGALAAIAGLTTqaawSSNGLPRIDNKTLAELAKQHPVVVLFRHAERCDRSDNQCLSDKTGITVK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799  77 GTEKAQQEGIKFATIFSEYDIYSSNAVRTIQTAKFFS-GKEPVVMDSLSDCNNDLYKTLESIARESHKRNIVIMTHNHCL 155
Cdd:PRK15416   84 GTQDARELGKAFSADIPDYDLYSSNTVRTIQSATWFSaGKKLTVDKRLSDCGNGIYSAIKDLQRKSPDKNIVIFTHNHCL 163

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1933691799 156 SFLARDRLGKKFKPAYLDALIMHYDGTRLILDGKYNKE 193
Cdd:PRK15416  164 TYIAKDKRGVKFKPDYLDALVMHVEKGKLYLDGEFVNH 201
 
Name Accession Description Interval E-value
PRK15416 PRK15416
lipopolysaccharide core heptose(II)-phosphate phosphatase; Provisional
 1-193 3.53e-109

lipopolysaccharide core heptose(II)-phosphate phosphatase; Provisional


Pssm-ID: 185314  Cd Length: 201  Bit Score: 310.57  E-value: 3.53e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799   1 MMKPRSSYSKTAFILLFSVFLVAAVTK----AKSSLPDITLEQAKEINADNTVIFLFRHGERCDRSDMPCYSDKSGITIT 76
Cdd:PRK15416    4 FCRSSSKSKKYFFILLGALAAIAGLTTqaawSSNGLPRIDNKTLAELAKQHPVVVLFRHAERCDRSDNQCLSDKTGITVK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799  77 GTEKAQQEGIKFATIFSEYDIYSSNAVRTIQTAKFFS-GKEPVVMDSLSDCNNDLYKTLESIARESHKRNIVIMTHNHCL 155
Cdd:PRK15416   84 GTQDARELGKAFSADIPDYDLYSSNTVRTIQSATWFSaGKKLTVDKRLSDCGNGIYSAIKDLQRKSPDKNIVIFTHNHCL 163

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1933691799 156 SFLARDRLGKKFKPAYLDALIMHYDGTRLILDGKYNKE 193
Cdd:PRK15416  164 TYIAKDKRGVKFKPDYLDALVMHVEKGKLYLDGEFVNH 201
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 49-187 7.17e-12

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: 60.51  E-value: 7.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799  49 VIFLFRHGERCDRSDMPCYSDK-SGITITGTEKAQQEGIKFATIFSEYD-IYSSNAVRTIQTAKFFS----GKEPVVMDS 122
Cdd:cd07040     1 VLYLVRHGEREPNAEGRFTGWGdGPLTEKGRQQARELGKALRERYIKFDrIYSSPLKRAIQTAEIILeglfEGLPVEVDP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933691799 123 LSDCNNDLYKTLESIAREShkRNIVIMTHNHCLSFLARdRLGkKFKPAYLDALIMHYdGTRLILD 187
Cdd:cd07040    81 RARVLNALLELLARHLLDG--KNVLIVSHGGTIRALLA-ALL-GLSDEEILSLNLPN-GSILVLE 140
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
50-184 1.46e-08

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 51.41  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799  50 IFLFRHGERCDRSDMPcySDKS-GITITGTEKAQQEGIKFATIFSEYD-IYSSNAVRTIQTAKFFSG-----KEPVVMDS 122
Cdd:COG2062     1 LILVRHAKAEWRAPGG--DDFDrPLTERGRRQARAMARWLAALGLKPDrILSSPALRARQTAEILAEalglpPKVEVEDE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933691799 123 LSDCN-NDLYKTLESIAREshkRNIVIMTHNHCLSFLA-----RDRLGkKFKPAylDALIMHYDGTRL 184
Cdd:COG2062    79 LYDADpEDLLDLLRELDDG---ETVLLVGHNPGLSELAallagGEPLD-GFPTG--GLAVLEFDIDDL 140
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
 72-157 5.99e-03

Histidine phosphatase superfamily (branch 2); 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 smaller branch 2 contains predominantly eukaryotic proteins. The catalytic functions in members include phytase, glucose-1-phosphatase and multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in branch 2 are not fully understood, although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated.


Pssm-ID: 395259 [Multi-domain]  Cd Length: 356  Bit Score: 36.62  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799  72 GITITGTEKAQQEGIKFATIF-----------SEYDIYSSNAVRTIQTAK-----FFSGKEPVVMDSLSDCNNDLYKTLE 135
Cdd:pfam00328  61 GLTPSGRVQAENLGRYFRQRYvggllrdgynaKDIYIRASSEGRVIASAQafaegLFGPEGEDVDKDLLDDSNVAKVTID 140

                          90       100
                  ....*....|....*....|..
gi 1933691799 136 SIarESHKRNIVIMTHNHCLSF 157
Cdd:pfam00328 141 ED--KKALANNLTAGYCSCPAF 160
 
Name Accession Description Interval E-value
PRK15416 PRK15416
lipopolysaccharide core heptose(II)-phosphate phosphatase; Provisional
 1-193 3.53e-109

lipopolysaccharide core heptose(II)-phosphate phosphatase; Provisional


Pssm-ID: 185314  Cd Length: 201  Bit Score: 310.57  E-value: 3.53e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799   1 MMKPRSSYSKTAFILLFSVFLVAAVTK----AKSSLPDITLEQAKEINADNTVIFLFRHGERCDRSDMPCYSDKSGITIT 76
Cdd:PRK15416    4 FCRSSSKSKKYFFILLGALAAIAGLTTqaawSSNGLPRIDNKTLAELAKQHPVVVLFRHAERCDRSDNQCLSDKTGITVK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799  77 GTEKAQQEGIKFATIFSEYDIYSSNAVRTIQTAKFFS-GKEPVVMDSLSDCNNDLYKTLESIARESHKRNIVIMTHNHCL 155
Cdd:PRK15416   84 GTQDARELGKAFSADIPDYDLYSSNTVRTIQSATWFSaGKKLTVDKRLSDCGNGIYSAIKDLQRKSPDKNIVIFTHNHCL 163

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1933691799 156 SFLARDRLGKKFKPAYLDALIMHYDGTRLILDGKYNKE 193
Cdd:PRK15416  164 TYIAKDKRGVKFKPDYLDALVMHVEKGKLYLDGEFVNH 201
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 49-187 7.17e-12

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: 60.51  E-value: 7.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799  49 VIFLFRHGERCDRSDMPCYSDK-SGITITGTEKAQQEGIKFATIFSEYD-IYSSNAVRTIQTAKFFS----GKEPVVMDS 122
Cdd:cd07040     1 VLYLVRHGEREPNAEGRFTGWGdGPLTEKGRQQARELGKALRERYIKFDrIYSSPLKRAIQTAEIILeglfEGLPVEVDP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933691799 123 LSDCNNDLYKTLESIAREShkRNIVIMTHNHCLSFLARdRLGkKFKPAYLDALIMHYdGTRLILD 187
Cdd:cd07040    81 RARVLNALLELLARHLLDG--KNVLIVSHGGTIRALLA-ALL-GLSDEEILSLNLPN-GSILVLE 140
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 50-164 6.63e-09

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: 52.32  E-value: 6.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799  50 IFLFRHGERCDRSDMPCYSDK-SGITITGTEKAQQEGIKFATIFSEYD-IYSSNAVRTIQTAKF----FSGKEPVVMDSL 123
Cdd:cd07067     2 LYLVRHGESEWNAEGRFQGWTdVPLTEKGREQARALGKRLKELGIKFDrIYSSPLKRAIQTAEIileeLPGLPVEVDPRL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1933691799 124 sdCNNDLYKTLESIARESHKRNIVIMTHNHCLSFLARDRLG 164
Cdd:cd07067    82 --REARVLPALEELIAPHDGKNVLIVSHGGVLRALLAYLLG 120
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
50-184 1.46e-08

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 51.41  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799  50 IFLFRHGERCDRSDMPcySDKS-GITITGTEKAQQEGIKFATIFSEYD-IYSSNAVRTIQTAKFFSG-----KEPVVMDS 122
Cdd:COG2062     1 LILVRHAKAEWRAPGG--DDFDrPLTERGRRQARAMARWLAALGLKPDrILSSPALRARQTAEILAEalglpPKVEVEDE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933691799 123 LSDCN-NDLYKTLESIAREshkRNIVIMTHNHCLSFLA-----RDRLGkKFKPAylDALIMHYDGTRL 184
Cdd:COG2062    79 LYDADpEDLLDLLRELDDG---ETVLLVGHNPGLSELAallagGEPLD-GFPTG--GLAVLEFDIDDL 140
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
 49-112 5.39e-03

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.


Pssm-ID: 132717 [Multi-domain]  Cd Length: 242  Bit Score: 36.58  E-value: 5.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933691799  49 VIFLFRHGERcdrsdmpcYSDKsgITITGTEKAQQEGIKFATIF-----------SEYDIYSSNAVRTIQTAKFF 112
Cdd:cd07061     5 VQVLSRHGDR--------YPGE--LTPFGRQQAFELGRYFRQRYgellllhsynrSDLYIRSSDSQRTLQSAQAF 69
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
 72-157 5.99e-03

Histidine phosphatase superfamily (branch 2); 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 smaller branch 2 contains predominantly eukaryotic proteins. The catalytic functions in members include phytase, glucose-1-phosphatase and multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in branch 2 are not fully understood, although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated.


Pssm-ID: 395259 [Multi-domain]  Cd Length: 356  Bit Score: 36.62  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933691799  72 GITITGTEKAQQEGIKFATIF-----------SEYDIYSSNAVRTIQTAK-----FFSGKEPVVMDSLSDCNNDLYKTLE 135
Cdd:pfam00328  61 GLTPSGRVQAENLGRYFRQRYvggllrdgynaKDIYIRASSEGRVIASAQafaegLFGPEGEDVDKDLLDDSNVAKVTID 140

                          90       100
                  ....*....|....*....|..
gi 1933691799 136 SIarESHKRNIVIMTHNHCLSF 157
Cdd:pfam00328 141 ED--KKALANNLTAGYCSCPAF 160
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH