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Conserved domains on  [gi|81295410|ref|NP_001032249|]
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2-phosphoxylose phosphatase 1 isoform 1 [Homo sapiens]

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 ...
87-424 1.65e-41

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 pfam00328:

Pssm-ID: 472174 [Multi-domain]  Cd Length: 356  Bit Score: 151.41  E-value: 1.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410    87 KLVSVHVFIRHGDRYPLYVIPKTKRPEIDCTLVANrkpyhpkleafishmskgsgASFESPLNSLPLYPNHPL---CEMG 163
Cdd:pfam00328   1 ELEQVQVVSRHGDRTPTQKFKKSYESLIFKILSLA--------------------GSLEGKLSFPGDYRYFKLqytLGWG 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410   164 ELTQTGVVQHLQNGQLLRDIYlkKHKLLPNDWSADQLYLETTGKSRTLQSGLALLYGFLP------------DFDWKKIY 231
Cdd:pfam00328  61 GLTPSGRVQAENLGRYFRQRY--VGGLLRDGYNAKDIYIRASSEGRVIASAQAFAEGLFGpegedvdkdlldDSNVAKVT 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410   232 FR---HQPSALFCSGSCYCPVRNQYLEKEQRRQYLLR-LKNSQLEKTYGEMAKIVDVPTKQLRAANPIDSMLCHFCHNVS 307
Cdd:pfam00328 139 IDedkKALANNLTAGYCSCPAFEWPLQLLKQVDEALDyYLPVFLEPIAKRLEQLCPGETNLTADDVWALLFLCFFETNKA 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410   308 ----FPCTRNgCVDMEHFKvikthQIEDERErrekklYFGYSLLG-------AHPILNQTIGRM-------QRATEGRKE 369
Cdd:pfam00328 219 dlspFCDLFT-EEDALHNE-----YLLDLEE------YYGLAGIGnelkktiGGPLLNELLARLtndlvctQEATFPLDA 286
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81295410   370 ELFaLYSAHDVTLSPVLSALGL----------------SEARFPRFAARLIFELWQDREKPSEHSVRILYN 424
Cdd:pfam00328 287 KLY-LYFTHDTTIYSLLSALGLfddlpplsslrvldgySASGEVPYGARLVFELYECSSEKDSRYVRLLLN 356
 
Name Accession Description Interval E-value
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
87-424 1.65e-41

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: 151.41  E-value: 1.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410    87 KLVSVHVFIRHGDRYPLYVIPKTKRPEIDCTLVANrkpyhpkleafishmskgsgASFESPLNSLPLYPNHPL---CEMG 163
Cdd:pfam00328   1 ELEQVQVVSRHGDRTPTQKFKKSYESLIFKILSLA--------------------GSLEGKLSFPGDYRYFKLqytLGWG 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410   164 ELTQTGVVQHLQNGQLLRDIYlkKHKLLPNDWSADQLYLETTGKSRTLQSGLALLYGFLP------------DFDWKKIY 231
Cdd:pfam00328  61 GLTPSGRVQAENLGRYFRQRY--VGGLLRDGYNAKDIYIRASSEGRVIASAQAFAEGLFGpegedvdkdlldDSNVAKVT 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410   232 FR---HQPSALFCSGSCYCPVRNQYLEKEQRRQYLLR-LKNSQLEKTYGEMAKIVDVPTKQLRAANPIDSMLCHFCHNVS 307
Cdd:pfam00328 139 IDedkKALANNLTAGYCSCPAFEWPLQLLKQVDEALDyYLPVFLEPIAKRLEQLCPGETNLTADDVWALLFLCFFETNKA 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410   308 ----FPCTRNgCVDMEHFKvikthQIEDERErrekklYFGYSLLG-------AHPILNQTIGRM-------QRATEGRKE 369
Cdd:pfam00328 219 dlspFCDLFT-EEDALHNE-----YLLDLEE------YYGLAGIGnelkktiGGPLLNELLARLtndlvctQEATFPLDA 286
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81295410   370 ELFaLYSAHDVTLSPVLSALGL----------------SEARFPRFAARLIFELWQDREKPSEHSVRILYN 424
Cdd:pfam00328 287 KLY-LYFTHDTTIYSLLSALGLfddlpplsslrvldgySASGEVPYGARLVFELYECSSEKDSRYVRLLLN 356
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
87-424 1.52e-33

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: 126.72  E-value: 1.52e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410  87 KLVSVHVFIRHGDRYPlyvipktkrpeidctlvanrkpyhpkleafishmskgsgasfesplnslplypnhplcemGELT 166
Cdd:cd07061   1 ELEQVQVLSRHGDRYP------------------------------------------------------------GELT 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410 167 QTGVVQHLQNGQLLRDIYlkKHKLLPNDWSADQLYLETTGKSRTLQSGLALLYGFLPDFDWKKIYFRHQPSalfcsgscy 246
Cdd:cd07061  21 PFGRQQAFELGRYFRQRY--GELLLLHSYNRSDLYIRSSDSQRTLQSAQAFLAGLFPPDGWQPIAVHTIPE--------- 89
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410 247 cpvrnqylekeqrrqyllrlknsqlekTYGEMAKIVDVPTKQLRAANPidsmLCHFCHNVSfpctrngcvdmehfkvikT 326
Cdd:cd07061  90 ---------------------------EEDDVSNLFDLCAYETVAKGY----SAPFCDLFT------------------E 120
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410 327 HQIEDERERREKKLYFGYSL------LGAHPILNQTIGRMQRATEGR----KEELFALYSAHDVTLSPVLSALGL----- 391
Cdd:cd07061 121 EEWVKLEYLNDLKFYYGYGPgnplarAQGSPLLNELLARLTNGPSGSqtfpLDRKLYLYFSHDTTILPLLTALGLfdfae 200
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 81295410 392 ----------SEARFPRFAARLIFELWQDrEKPSEHSVRILYN 424
Cdd:cd07061 201 plppdflrgfSESDYPPFAARLVFELWRC-PGDGESYVRVLVN 242
 
Name Accession Description Interval E-value
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
87-424 1.65e-41

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: 151.41  E-value: 1.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410    87 KLVSVHVFIRHGDRYPLYVIPKTKRPEIDCTLVANrkpyhpkleafishmskgsgASFESPLNSLPLYPNHPL---CEMG 163
Cdd:pfam00328   1 ELEQVQVVSRHGDRTPTQKFKKSYESLIFKILSLA--------------------GSLEGKLSFPGDYRYFKLqytLGWG 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410   164 ELTQTGVVQHLQNGQLLRDIYlkKHKLLPNDWSADQLYLETTGKSRTLQSGLALLYGFLP------------DFDWKKIY 231
Cdd:pfam00328  61 GLTPSGRVQAENLGRYFRQRY--VGGLLRDGYNAKDIYIRASSEGRVIASAQAFAEGLFGpegedvdkdlldDSNVAKVT 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410   232 FR---HQPSALFCSGSCYCPVRNQYLEKEQRRQYLLR-LKNSQLEKTYGEMAKIVDVPTKQLRAANPIDSMLCHFCHNVS 307
Cdd:pfam00328 139 IDedkKALANNLTAGYCSCPAFEWPLQLLKQVDEALDyYLPVFLEPIAKRLEQLCPGETNLTADDVWALLFLCFFETNKA 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410   308 ----FPCTRNgCVDMEHFKvikthQIEDERErrekklYFGYSLLG-------AHPILNQTIGRM-------QRATEGRKE 369
Cdd:pfam00328 219 dlspFCDLFT-EEDALHNE-----YLLDLEE------YYGLAGIGnelkktiGGPLLNELLARLtndlvctQEATFPLDA 286
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81295410   370 ELFaLYSAHDVTLSPVLSALGL----------------SEARFPRFAARLIFELWQDREKPSEHSVRILYN 424
Cdd:pfam00328 287 KLY-LYFTHDTTIYSLLSALGLfddlpplsslrvldgySASGEVPYGARLVFELYECSSEKDSRYVRLLLN 356
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
87-424 1.52e-33

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: 126.72  E-value: 1.52e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410  87 KLVSVHVFIRHGDRYPlyvipktkrpeidctlvanrkpyhpkleafishmskgsgasfesplnslplypnhplcemGELT 166
Cdd:cd07061   1 ELEQVQVLSRHGDRYP------------------------------------------------------------GELT 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410 167 QTGVVQHLQNGQLLRDIYlkKHKLLPNDWSADQLYLETTGKSRTLQSGLALLYGFLPDFDWKKIYFRHQPSalfcsgscy 246
Cdd:cd07061  21 PFGRQQAFELGRYFRQRY--GELLLLHSYNRSDLYIRSSDSQRTLQSAQAFLAGLFPPDGWQPIAVHTIPE--------- 89
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410 247 cpvrnqylekeqrrqyllrlknsqlekTYGEMAKIVDVPTKQLRAANPidsmLCHFCHNVSfpctrngcvdmehfkvikT 326
Cdd:cd07061  90 ---------------------------EEDDVSNLFDLCAYETVAKGY----SAPFCDLFT------------------E 120
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81295410 327 HQIEDERERREKKLYFGYSL------LGAHPILNQTIGRMQRATEGR----KEELFALYSAHDVTLSPVLSALGL----- 391
Cdd:cd07061 121 EEWVKLEYLNDLKFYYGYGPgnplarAQGSPLLNELLARLTNGPSGSqtfpLDRKLYLYFSHDTTILPLLTALGLfdfae 200
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 81295410 392 ----------SEARFPRFAARLIFELWQDrEKPSEHSVRILYN 424
Cdd:cd07061 201 plppdflrgfSESDYPPFAARLVFELWRC-PGDGESYVRVLVN 242
 
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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