2FDR,4UAV,1O03,2QLT,3L5K,1TE2,4EEK,3QYP,3KBB,3E58


Conserved Protein Domain Family
HAD_BPGM-like

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cd07505: HAD_BPGM-like 
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beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily
This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.
Statistics
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PSSM-Id: 319808
View PSSM: cd07505
Aligned: 68 rows
Threshold Bit Score: 58.7815
Threshold Setting Gi: 30694711
Created: 8-Jul-2008
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 12 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Comment:based on various beta-phosphoglucomutase-like family members and on other haloacid dehalogenase superfamily members with structure
  • Structure:3KBB: Thermotoga maritima putative beta-phosphoglucomutase (TM1254, binds sulfate ion in the active site, contacts at 4A
    View structure with Cn3D
  • Structure:3L5K: human Haloacid Dehalogenase-Like Hydrolase domain containing 1A binds K+ in the active site
    View structure with Cn3D
  • Structure:2QLT: Saccharomyces cerevisiae Dl-glycerol-3-phosphatase binds Ca2+ (inhibitor) in the active site
    View structure with Cn3D
  • Structure:3QYP: Bacteroides thetaiotaomicron inorganic pyrophosphatase (BT2127) binds Ca2+ and phosphate ion in the active site
    View structure with Cn3D
  • Structure:4EEK: Deinococcus radiodurans Had family hydrolase Dr_1622 binds Na+ and phosphate ion in the active site
    View structure with Cn3D
  • Structure:2FDR: Agrobacterium tumefaciens hydrolase binds Mg2+ in the active site
    View structure with Cn3D
  • Structure:1O03: Lactococcus lactis beta-phosphoglucomutase binds glucose-1,6-bisphosphate and Mg2+ in the active site
    View structure with Cn3D
  • Structure:4UAV: Arabidopsis thaliana CbbY(at3g48420) binds Mg2+ in active site
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1            #####                                                                       
2FDR_A         6 LIIFDCDGVLVDSEi-IAAQVESrllteagypisveexgerfag----------xtwknillqveseasiplsasLLDKS 74
4UAV_A         5 ALLFDCDGVLVDTEkdGHRISFNdtfkerdlnvtwdvdlygellkigggkermtayfnkvgwpekapkdeaerkeFIAGL 84
1O03_A         4 AVLFDLDGVITDTAe-YHFRAWKalaeeigingvdrqfneqlkgvs------redslqkildladkkvsaeefkeLAKRK 76
3KBB_A         3 AVIFDXDGVLXDTEp-LYFEAYRrvaesygkpytedlhrrixgv----------pereglpilxealeikdslenFKKRV 71
gi 30696124   76 AVLFDMDGVLCNSEd-LSRRAAVdvftemgvevtvddfvpfmgtgea-----kflggvasvkevkgfdpdaakerFFEIY 149
gi 22297853    7 AWCIYVDRTPELRQh-INLEHLRhmggkrnaellpe--------------------------llgrslsaaeierWGAGK 59
gi 21672855   11 AFIFDMDGVLVDNMr-MHAQSWVdlfadyglsgldperylvetag--------mkgldvlryfldpsispekadrLTELK 81
gi 37522745    5 AVLFDFNGVLVDDEp-LHRALTLqvlgeafnlevsraeyrrhclgrp-----dreafravlearglavgdgalaaLMRRK 78
gi 22298239    5 AVLFDFNGVILDDEa-IHAALIEeillqenlrpqrgeydlfclgrs------dracldnllsrrgravtpayldkLVAQK 77
gi 39996938    4 AVIFDFDGIIVDTEp-LHYRAFQailepigfgysweayvdvymgyd------drdafreafrvrgadledrelegLIARK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                ##                                   #  
2FDR_A        75 EKLLDXRLerdv-----kiiDGVKFALSRLt---TPRCICSNsssHRLDXXLTKvglk-pyfaPHIYSAKDlgadrvKPK 145
4UAV_A        85 HKQKTELFmvliekkllplrPGVAKLVDQAltngVKVAVCSTsneKAVSAIVSCllgperaekIKIFAGDVvp--kkKPD 162
1O03_A        77 NDNYVKMIqdvsp---advyPGILQLLKDLrsnkIKIALASAs--KNGPFLLERmnlt--gyfDAIADPAEva--asKPA 147
3KBB_A        72 HEEKKRVFsell-----kenPGVREALEFVkskrIKLALATStpqREALERLRRldle--kyfDVXVFGDQvk--ngKPD 142
gi 30696124  150 LDKYAKPEsgi-------gfPGALELVTECknkgLKVAVASSadrIKVDANLKAagls-ltmfDAIVSADAfe--nlKPA 219
gi 22297853   60 EAVFRELLaphl-----ellPGLLPFLKSAkekgYRLGLGTSacaANVELVLSCegvg--hffDTVVMEQDvq--rgKPD 130
gi 21672855   82 DILYRVMNrnai-----vamPGLETFLDRAanagIRLGIGTGagpKNIDYVLGLtglt--srfEVVVGAHMvr--hgKPH 152
gi 37522745   79 TELYRERAapkd-----llvVGVQALLADLvgrgMHLAVVTGsggEEVSWLLENtglr--eyfALIVAAEDiq--rgKPD 149
gi 22298239   78 AAAYRARLasiep---fpffAGAIALLQKLhaarLKIAIVTGavrSDVDLALERghlh--smvDCIISAESve--rsKPY 150
gi 39996938   77 AAAFQEIIasgv-----tpyPGVVELIRNIka-nHPVALCSGalrSDILPILEGlgls--gifDVMVTADEvs--asKPD 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
Feature 1                                    ##  ##                 
2FDR_A       146 PDIFLHGAAQFGvsp-------drVVVVEDSVHGIHGARAAGx-RVIGFTG 188
4UAV_A       163 PAIYNLAAETLGvdp-------skCVVVEDSAIGLAAAKAAGm-TCIVTKS 205
1O03_A       148 PDIFIAAAHAVGvap-------seSIGLEDSQAGIQAIKDSGa-LPIGVGR 190
3KBB_A       143 PEIYLLVLERLNvvp-------ekVVVFEDSKSGVEAAKSAGieRIYGVVH 186
gi 30696124  220 PDIFLAAAKILGvpt-------seCVVIEDALAGVQAAQAANm-RCIAVKT 262
gi 22297853  131 PECYLLVAERLQvvp-------qyCLVFEDAVAGVMAAVQAGm-LCWGVLT 173
gi 21672855  153 PETFLQVAERLGadp-------asCIVFEDALPGAEAAAAAGm-SCVAVTT 195
gi 37522745  150 PEGYRTALGRLGrep-------eeALAVEDSLAGIEAARRAGl-RVLALTT 192
gi 22298239  151 PDPYLRAVEALQalgsd--ltaadCLAIEDTLVGIQSAREAGv-KVLGVAH 198
gi 39996938  147 PASYALAVRRLTaafpnrqirpetCIAIEDTPAGIASATGAGi-GVLAVTN 196

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