2B0C,1CQZ,1S8O,2I6X,5AHX,3CNH,4JB3


Conserved Protein Domain Family
HAD_sEH-N_like

?
cd02603: HAD_sEH-N_like 
Click on image for an interactive view with Cn3D
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive
This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family 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
?
PSSM-Id: 319790
View PSSM: cd02603
Aligned: 46 rows
Threshold Bit Score: 117.446
Threshold Setting Gi: 55981581
Created: 3-Feb-2005
Updated: 18-Aug-2016
Structure
?
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 Escherichia coli soluble epoxide hydrolase phosphatase domain and on other haloacid dehalogenase superfamily members with structure
  • Structure:2B0C: Escherichia coli soluble epoxide hydrolase phosphatase domain binds glucose-1-phosphate, contacts at 4A
    View structure with Cn3D
  • Structure:3CNH: Deinococcus radiodurans predicted haloacid dehalogenase-like hydrolase binds phosphate ion and Na+ in the active site
    View structure with Cn3D

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1              #####                                                                     
2B0C_A         7 KMLYIFDLGNVIVDidf-------------nrVLGAWSdltriplas-lkksfhmgeAFHQHERGEISd----------- 61
gi 55981581    1 MRGALLDRDGVLLLldekalyrkavelaargaGLERSLaalaravralneavrglavRTLEEEEALWRtl---------- 70
gi 15888140    4 IDHIVFDIGKVLIHydphipy----srlipdaDERQWFfenv-----------cthdWNLEQDRGRRWedaealllerfp 68
gi 15806361    7 LQAVLFDRDDTLALtdpavy------reaalwMQERFGldprqa-------ghtlaqVWEERMNDWWDlrsh-------e 66
gi 31794558    3 ISAVVFDRDGVLTSfdwt----------raeeDVRRITglp--------------leEIERRWGGWLNgltiddafvetq 58
gi 27379935    9 ADALLFDLGRVVLDidf-------------skAIACWAghagckpeaiiaryvrdseAYRLHEVGKISd----------- 64
gi 27376469   69 IKLVLFDMDNVLCNydr-------------gqRVACLAelagstsel-vhkaiwdsgFELLGDSGALDa----------- 123
gi 19551370    4 TRTFLFDLYGVLIKehg-------------aaQFERVAravgepskn-dklhevyesLRLDLDAGRVSe----------- 58
gi 46581381    9 ARAVLYDFSGVLAEegf-------------isGLRAIAaeng-----------ldpqAFVRAATDVCYtsgyad---gla 61
gi 300790876   1 MNWIVFDYGDVLSKps---------------aALPGLAaam--------------gaPLPEFLEAYWAyripyd---ags 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                         ##             
2B0C_A        62 --EAFAEALCHemalp------lsyeQFSHGWqavf---valRPEVIAIMHKLRe--QGHRVVVLSNTnrlh--ttfWPE 126
gi 55981581   71 -vLEVARELRVppe----------elLPWRYYrfm-----rpAPGAERLLHRLKa--RNLKVGVLSNTlpslreslaHHG 132
gi 15888140   69 erEEHIRAFRK---------------FWHEMVsh-------sYDDSVAIMVALId--SGHDVTMLTNFasdt--freAQK 122
gi 15806361   67 deEQFWEEYGSdltarlglgpeaaaeVMAAYPyery---mkpVAGAREVLSELRr--RGLKTGVLSNTlpsi-drtlDAL 140
gi 31794558   59 piSEFLSSLARelelgsk--ardelvRLDYMAfa------qgYPDARPALEEARr--RGLKVGVLTNNsllv--sarSLL 126
gi 27379935   65 --EEYFASLRAslg----------igISDAQFlegw--naifAGEMPDVAELLPraaKQMPLYAFSNTnrph--vdhFSK 128
gi 27376469  124 --PDYLRGFGErmgyp------lsldEWVEARrrs----mqpDHAMLEIARRLR---KTVDIAVLTNNttlv--adhIDT 186
gi 19551370   59 --VNYWNQIKLlvgl--------eflDIQEVIaadyrglyerDQDMVDYVLSLKa--KGHRIGILSNIpegl--aklLKE 124
gi 46581381   62 paSAFWQGVRQvtgit------hddaTLQEAVlsr----fviRPDMFADVDALRe--QGLTVALVSDHt-------dWLE 122
gi 300790876  49 tpLEYWQAVGNavgap------vdeaLSAELTrvdvegwghlEPSSAALLEALSe--AGANLALLSNApia---fgeWVR 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                #                       ##  ##                          
2B0C_A       127 EYPei---rdAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSDTVFFDDNADNIEGANQLGITSILVKDktt----ipD 199
gi 55981581  133 LAR-------YVDGFFASCALGVAKPDPRAFLLALEGLGLAPEETLYLDDDPENVEAARRLGLRAEVYAPi--------G 197
gi 15888140  123 MFPfl----tLPRGVTVSGDVKLLKPDVAIYHLHAKEFGLNPATSLFIDDTLANVEGAKAAGWQAVHFTGa-------eK 191
gi 15806361  141 GLAd------LIDVPLATCLLGVHKPEARAFTLAAEALGCRPEEVLFIDDRPENVSAAQAVGMRAALIDHsgqt-pgalS 213
gi 31794558  127 QCAal---hdLVDVVLSSQMIGAAKPDPRAYQAIAEALGVSTTSCLFFDDIADWVEGARCAGMRAYLVDRsgqtrdgvvR 203
gi 27379935  129 EYAdl---lgHFRELYLSSSIGLRKPDAAAFDHVVAAIGVPARRIVFFDDLAENVEGARARGLTAVHVTSprd----vgD 201
gi 27376469  187 LLPdlr--plFGSRIYTSAQFKTAKPDPRCYRRCLAELDVMPQTVLFVDDLPANVAGAREAGLFAHHHTSv-------eA 257
gi 19551370  125 HNSew---ldQLDAVTLSCDIGAAKPEPKSFHVALEALGEKAEDVTFIDDRVRNIEAAREEGLSTIHFTGl--------D 193
gi 46581381  123 TLDdrhgvfhHFDHAFSSFREKRNKRTGELFDRALDVLGLAPEQTMFFDDNAGNVERAILRGIDARLFTDk-------pA 195
gi 300790876 118 AQDwa----rYFRVTMFSGDVRCVKPEAKIFRLLLDELGAEPADCLFFDDRESNVEGARAVGLQAHVWNGa--------D 185

                 ....*.
Feature 1              
2B0C_A       200 YFAKVL 205
gi 55981581  198 APGRRA 203
gi 15888140  192 LKQDLR 197
gi 15806361  214 DLREVL 219
gi 31794558  204 DLSSLG 209
gi 27379935  202 ALEALG 207
gi 27376469  258 FRQALS 263
gi 19551370  194 SLKESI 199
gi 46581381  196 YRADLA 201
gi 300790876 186 AARAWL 191

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