Conserved Protein Domain Family
GST_C_etherase_LigE
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cd03202: GST_C_etherase_LigE 
C-terminal, alpha helical domain of Beta etherase LigE
Glutathione S-transferase (GST) C-terminal domain family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas paucimobilis beta etherase, LigE, a GST-like protein that catalyzes the cleavage of the beta-aryl ether linkages present in low-moleculer weight lignins using GSH as the hydrogen donor. This reaction is an essential step in the degradation of lignin, a complex phenolic polymer that is the most abundant aromatic material in the biosphere. The beta etherase activity of LigE is enantioselective and it complements the activity of the other GST family beta etherase, LigF. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.
Links
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Statistics
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PSSM-Id: 198311
Aligned: 22 rows
Threshold Bit Score: 165.513
Created: 9-Nov-2005
Updated: 2-Oct-2020
Structure
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Aligned Rows:
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putative dimerputativeputative
Feature 1:putative dimer interface [polypeptide binding site]
Evidence:
  • Comment:Based on dimer structures of other family members.
  • Comment:Residues from both N-terminal TRX-fold and C-terminal alpha helical domains form the dimer interface.
  • Citation:PMID 9680481
Scroll to Sequence Alignment Display
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1          ##  ##  #                                                           #         
126289        98 LMKFLDNWLWSTAVGPWFRCYIlDYHDLSLPQDRDYVRWSReqwflGGQRLEDVQAgreDRLPLVPPTLEPFRRILAETK 177 Sphingomonas pa...
NP_108131     95 MARFIERWSQLTIHPYVTTAALiDLHGMQDDENAVYFRQSReq--rFGRQLEDVVAardAGLAAFRASLEPLRSTLGYQP 172 Mesorhizobium l...
NP_053324     95 MGRFIERWSQLTLHPYIGVATLmEEVGLLEPESAAYFRKSRea--kFGRALEEVARdrgVKLAAFRSALEPLRSMLTYQP 172 Agrobacterium t...
CAC45742      95 MARFVEGWSQTTLHPAIGRIAImDIHDSLDPIDRAYFRASRee--rFGRPLEAVAEagrGDLETFSAKLEPIRHMLKFQP 172 Sinorhizobium m...
YP_002549116  95 LARFVEGYSQSTIHPAISSIALmDIYNMISPADQAHFRKTRea--lFGKVLEEIFPdrdGAIAAFPAKLQPLRHMLRSQP 172 Agrobacterium v...
ZP_02149699   70 LTRFVESYCKTVLHPSLATIAVmDMHNLMSPADQVYFRSARer--rFGMPLEVMAEggeAERALLPEKLSPIRDLLATQD 147 Phaeobacter gal...
YP_003890246  93 LTLFIKHWNDGVLAPSLFPLVIlDIYKNLDPKDKPYFRENReq--rLGKTLEEFANpsdEQLSLFRANLEPVRKTLNTAA 170 Cyanothece sp. ...
ZP_07373940   95 LTRFVGNWSQRNLHPAVSKLAMlDIHDALADTDKAFFRRTRen--tLGSTLEEFSAkfpKDGAELGRALEPFATTLQGQP 172 Ahrensia sp. R2...
BAJ11989      98 LTQGMEAWLWGAAISPWMTCFIkQYRDRSLPQDHEYVTTSRer--mFGRKIEDIIVgreDRIPKVPPTLQLLRNVLAENK 175 Sphingobium sp....
YP_001262153  97 MIGFFDQWLLQLIVTGILPIYAlDAHDGAAPHDRDYYRRSRes--fFGQTLEEVVVkreERLPDVRRSFEPVRQTIVNQP 174 Sphingomonas wi...

Feature 1                                                      
126289       178 WLGGDQPNFADYSALAVFLWTASVArtpPLTEDDPLRDWLDRGFDL 223 Sphingomonas paucimobilis
NP_108131    173 FIGGAAPLFADYIVFGALQWARIATpyqLLEDSDVVAQWFARCLDL 218 Mesorhizobium loti MAFF303099
NP_053324    173 FIGGSSPLFPDYIVFGAFQWARTTTtfqVLEESDPVNIWFERCLDL 218 Agrobacterium tumefaciens
CAC45742     173 FLGGDRPLFADYIVFGALQWARIVSphrLLAAGDVVTDWFERCLDL 218 Sinorhizobium meliloti
YP_002549116 173 FIGGEKPLFADYIVFGAFQWLKIVTgsiFLPEDDPAAQWFERCAAL 218 Agrobacterium vitis S4
ZP_02149699  148 WLSGAMPAYADYTLFGTLQWCNVCApntLFEKDDLVSHWFERCLDL 193 Phaeobacter gallaeciensis 2.10
YP_003890246 171 FIGGDQPNFADYIILATLQLGYTISplkFLEPNDPVFAWREQILAL 216 Cyanothece sp. PCC 7822
ZP_07373940  173 YLGGKTPLFADYIVFGALQWLRVTSpldVLDKTSPVGEWFERLLDM 218 Ahrensia sp. R2A130
BAJ11989     176 WLGGDTPNYADFRLLAVFLFTASVAdtpVLTDDDPLRDWIERGFDL 221 Sphingobium sp. SYK-6
YP_001262153 175 FLGGTSPNFADMCLLGLFIFVGTIGtlpLLAADDPLVAYADRGFAC 220 Sphingomonas wittichii RW1

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