1T8P,1E59,1FZT,1K6M,1RII,1UJB,1XQ9,1YFK,2A6P,2AXN,2P6O,2QNI,2RFL,3D8H,3DCY,3E9C,3EOZ,3EZN,3F2I,3F3K,3PGM,2F90,2IKQ,1H2E


Conserved Protein Domain Family
HP_PGM_like

?
cd07067: HP_PGM_like 
Click on image for an interactive view with Cn3D
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.
Statistics
?
PSSM-Id: 132718
View PSSM: cd07067
Aligned: 310 rows
Threshold Bit Score: 47.702
Threshold Setting Gi: 75544137
Created: 8-Jan-2008
Updated: 17-Jan-2013
Structure
?
Program:
Drawing:
Aligned Rows:
 
catalytic core
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic core [active site]
Evidence:
  • Comment:The catalytic core includes a His group which is phosphorylated during phosphoryl transfer as well as two key Arg residues and an additional His residue which are hydrogen bonded to the phospho group before, during, and after transfer.
  • Structure:1H2E_A, Bacillus stearothermophilus PhoE bound with phosphate ion, contacts calculated at 3.5A.
    View structure with Cn3D
  • Structure:2IKQ_A, Mus musculus Sts-1 (Suppressor of T- Cell Receptor) phosphatase domain bound with phosphate ion, contacts calculated at 3.5A.
    View structure with Cn3D
  • Structure:1E59_A, Escherichia coli bound with a tungstate ion (a phosphate analog), contacts calculated at 3.5 A.
    View structure with Cn3D
  • Structure:2F90_A, human bisphosphoglycerate mutase homodimer bound with 3-phosphoglycerate and Alf4-, contacts calculated at 3.5 A.
    View structure with Cn3D
  • Comment:Alf4- mimics the intermediate in phosphoryl transfer reactions.

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1            ##                                                     #                   
1T8P_A        5 KLIMLRHGEGAwnkenr-fcswvDQKLNSEGMEEARNCGKQLkaln--fefdLVFTSVLNRSIHTAWLILeelgqewvPV 81
1H2E_A        3 TLYLTRHGETKwnverr-mqgwqDSPLTEKGRQDAMRLGKRLeav----elaAIYTSTSGRALETAEIVRggr---liPI 74
gi 75368631  20 VVLLIRHGQTPttgqvl-pgqtpGLHLSDKGEEQAREVAQRLaev----pitAVYSSPMERAQETAAPTVsah---glEL 91
gi 75424147   2 KLYLVRHGQTAsnvakkldtalpGPPLTELGHEQARQLAEKLate----pveAVYASHATRAQQTAAPLAqal---gmTV 74
gi 81415185   2 QVLLVRHALPLrseh----gqgsDPDLSADGLAQIERLPKALerf----pisRVVSSPQRRAVQTAAPVAadr---glSV 70
gi 81535224   3 IVHVIRHGRPAstwg----gadeDPGLDEFGLAQARAVADEIlslpeherpsRVVSSPLRRCRETAAPLAeal---gvAL 75
gi 81539096   2 RLLLIRHGQTPsnlkhlldtaepGPGLTALGQEQAAALPGALase----eigALYASTLVRTQLTAAPLAsat---glEV 74
gi 81570903  36 TVTFVRHAQSEanasgtidtevpGPGLSPEGKGQAEQVAHQLgrk----dydSVYASTMTRAQQTAAPLAael---gkQV 108
gi 81668677   2 TVILLRHARSTsntagv-lagrsGVDLDEKGREQATGLIDRIgdl----pirAVASSPMLRCQRTVEPLAeal---clEP 73
gi 81729030   3 HVRLIRHGESAanagqp-svdhaTIPLTLKGVEQAQSVARSFtha-----paLIVASPFSRAQATAMATVstf---paTP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                       
1T8P_A       82 ESSWRLNErhygaliglnreqmalnhgeeqvrlwrrsynvtpppieeshpyyqeiyndrrykvcdvpldqlprseslkdv 161
1H2E_A       75 YQDERLREihlgdwegkthdeirqmdpiaf-----------------------------dhfwqaphlyapqrgerfcdv 125
gi 75368631  92 TVEPGLIEcdfgewtgrkltelnaleewk-------------------------------avqktpstfrfpggesfvem 140
gi 75424147  75 KRVEGVHEivvgdlegrhdreaiehyltvl-----------------------------shwtrgelhvpmpggetgeqa 125
gi 81415185  71 EIDDRFAEydrdlpvyipveqirdempe---------------------------------ewarlaqghlpsavdedaf 117
gi 81535224  76 VIDPRVGEiptpaalsaeerpawlra-------------------------------------afggrwdeivgdidytk 118
gi 81539096  75 RVRAGIREltagdlemrgdddaartymhta-----------------------------fawsagdvglrmpggengaea 125
gi 81570903 109 EVLPGIQEinagwyngksesmakstylvap-----------------------------anwlkgdvsdsipgsisgkef 159
gi 81668677  74 LIDDRFSEvdygewtgrkigdlvdeplwr-------------------------------vvqahpsaavfpggeglaqv 122
gi 81729030  74 FETWPIQEftyleparctnttvaqrrgwvea----------------------------ywarsdpaftegagaesflef 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                    ##                                                 
1T8P_A      162 lERLLPYWNERiapev---lrgkTILISAHGNSSRALLKHLegisdedi-initlptgVPILLElden-------lraVG 230
1H2E_A      126 qQRALEAVQSIvdrh-----egeTVLIVTHGVVLKTLMAAFkdtpldhlwsppymygtSVTIIEvdg--------gtfHV 192
gi 75368631 141 qDRMVEAIGNIaqqh-----pgeIVAAFSHADTIKAAVAHFvgtpldsf-qrifidtaSISAVEftgkss---gvsshML 211
gi 75424147 126 rARFTGAIAGLaerhdl-trsdgVVVLVSHGGLIRIGAEWLapnvrpeladqglipntGIVELEia----------adGG 194
gi 81415185 118 rARVRAAVDDLvaaa----dpedTVAVFSHGGVINVLLHEIlgtarll---sfpvdyaSVTRLLfsrsgqatvaavnsTE 190
gi 81535224 119 wTRAVAAALGEh----------gGAAVFSHFVALNGAVSAAtgrpevm---afrpdhcSRTVFGie-----------dDR 174
gi 81539096 126 lARFDAVVAEAhet------gaeTVALVSHGAAIRMWVAARadnvdvdyaerhplantGIVILSgs----------pgQG 189
gi 81570903 160 nDQFTAAVNKIyns------ghrNPVVFSHANSIMVWTLMNtrnakdslmnthplpntGRVVINgn----------piTG 223
gi 81668677 123 qTRAVAAVREHdrrladqhghdvLWLACTHGDVIKAVIADAfgmhldsf-qritadpgSVSVVRytql-------rpfVL 194
gi 81729030 126 iARAQSLLVRLaeh------paqYIAVFSHGQFINAVAWLIertpqri----dgramaDWREYEi-------------TN 182

                ....*
Feature 1            
1T8P_A      231 pHQFL 235
1H2E_A      193 aVEGD 197
gi 75368631 212 -LTNS 215
gi 75424147 195 -WQCL 198
gi 81415185 191 -HVWD 194
gi 81535224 175 -LILI 178
gi 81539096 190 -WRAL 193
gi 81570903 224 -WTLV 227
gi 81668677 195 -HVNH 198
gi 81729030 183 -PVPN 186

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap