3DHA,2A7M,2BR6,3DHB,4J5F,2R2D,4KEP,3AJ3


Conserved Protein Domain Family
AHL_lactonase_MBL-fold

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cd07729: AHL_lactonase_MBL-fold 
Click on image for an interactive view with Cn3D
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain
Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Statistics
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PSSM-Id: 293815
Aligned: 248 rows
Threshold Bit Score: 150.443
Created: 9-Jun-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 11 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:3DHB: Bacillus thuringiensis quorum-quenching lactonase (AiiA) binds the product N-hexanoyl-l-homoserine and two zinc ions
  • Structure:2BR6: Bacillus thuringiensis quorum-quenching lactonase (AiiA) binds homoserine lactone and two zinc ions

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1              # #                                                                    
3DHA_A      9 KLYFIPAGRCMLDhssvns-----altpgkLLNLPVWCYLLETEEGPILVDTGMPesavnneglfngtfveGQILPKMte 83  Bacillus thuringie...
3DHB_A      9 KLYFIPAGRCMLDhssvns-----altpgkLLNLPVWCYLLETEEGPILVDTGMPesavnneglfngtfveGQILPKMte 83  Bacillus thuringie...
EPG73904   47 GLYAVLYGKGKYPnyltds------getdgEQELAFFFYLVKLNKRIILVDSGISse-------------eTRSKYGIqd 107 Leptospira fainei ...
KIA72934   11 RVVVVRVGTRATErsdvylny-rlygeddgPATVDYYFWILQGPEGTVVVDTGFGe--------------eAGRRRGRtl 75  Arthrobacter sp. M...
ABQ29014    5 EILAVRYGTRKTEkseiyydy-arygeadgEAVMDYYFWILRDGTETIVIDTGFSa--------------aSGAARKRdt 69  Acidiphilium crypt...
AJE49187    7 ELFAVCYARQPERrpahltyv--dgreaesTTGFDYFFWYAVQGERVVVIDTGFSe--------------eACRRLGRaw 70  Celeribacter sp. P73
EHI39502    7 EVYALRYATRPNCmtseafyrhdlygetdtPVGMDYFFWLIRSQGQTVVVDCGFNe--------------nVGPTRNRwi 72  Rhodococcus opacus...
AGZ41416    6 QVTIVKYGTRQTVrsdvylnh-hlygepdgPIGMDYFFWVVRNTERTIVVDTGFSa--------------iGGANRKRtt 70  Actinoplanes friul...
KJC64843   14 SIWQVKYGERVVRksdvffdy-asyglpdgDLDMDYNFWVLRAGDATILVDTGYDi--------------pAHDWLGEis 78  Agreia bicolorata
EHI39511   10 EVYALRYGSAKTTkaskylny-kaygepdeEIVADFYFWLVRNAERTVLVDCGFDg--------------eRARPRGYfq 74  Rhodococcus opacus...
Feature 1                             # ####                                                  
3DHA_A     84 edrivnILKRVGYEPDDLLYIISSHLHFDHAGGNGAFTNTPIIVQRTEYEAALHreeym--------------kecilPH 149 Bacillus thuringie...
3DHB_A     84 edrivnILKRVGYEPDDLLYIISSHLHFDHAGGNGAFTNTPIIVQRTEYEAALHreeym--------------kecilPH 149 Bacillus thuringie...
EPG73904  108 wvspdkILLKAGIRPTMITDIILTHFHFDHAGGLDLFRNARIYVHPKEWELLKKtnwfsnqa---------ktlyareKE 178 Leptospira fainei ...
KIA72934   76 llhpakALAHMGIDPNDIGDVIVTHGHYDHIGNLDLFPNARIHIAEAEYRFWTSptagrvqfsfyaedgeidqlrlaeTQ 155 Arthrobacter sp. M...
ABQ29014   70 tiapaaALARLGIDPASVRDVILTHAHYDHTGNLDLFPNALITMSRTEYAFISGpfadrvplavamdsddnrgivrlhEA 149 Acidiphilium crypt...
AJE49187   71 agdpatLLARAGIDAGAVRDVILTHAHPDHVGNLDQFPNATFWIHAEEMRALTGeemsfdffrhsyhgedvcalvrllHA 150 Celeribacter sp. P73
EHI39502   73 sttpseLLSRMGVDPKAVDHVVLSHMHFDHVGNTHLFPNATFHMSRAEYEYWTGrhrdvpafswpvesdevrlleslrRE 152 Rhodococcus opacus...
AGZ41416   71 liepaaAFDALGVDRAAGPPVVITHAHYDHIGNLGLFPASPLTVAGAEYAFWTGpyadrtllhhsvedeeiaslkqadAE 150 Actinoplanes friul...
KJC64843   79 vtppprALELVDVDPLTVDMVITSHFHYDHIGYLKLFTNAQVVSGRAEYDYWFGkweagqlegeftveehlvpvriaeVE 158 Agreia bicolorata
EHI39511   75 ssdpaaLLARFGVTPADIDHVVISHMHFDHVGNVGLFPNATFSVARDEFDFWTGryaerkmfalfaeaeeiktvvelhQS 154 Rhodococcus opacus...
Feature 1                             #                     #  #                              
3DHA_A    150 LNYKIIEGDYEVV-PGVQLLYTPGHSPGHQSLFIETEqsGSVLLTIDASYTKENFEdevp---fagfDPELALSSIKRLK 225 Bacillus thuringie...
3DHB_A    150 LNYKIIEGDYEVV-PGVQLLYTPGHSPGHQSLFIETEqsGSVLLTIDASYTKENFEdevp---fagfDPELALSSIKRLK 225 Bacillus thuringie...
EPG73904  179 RKVIFLESSAELF-PNFRIIFTRGHTPGHSAVEWLRApkNRVLITGDECYFIEHCIegtglpnsaasSVRNNREFLHYVE 257 Leptospira fainei ...
KIA72934  156 GRLKLFSGETSPA-PGIRLVEVGGHTPGQSIVYVPTSe-GDVLLASDAVHFYEELErdmpf--taisDLPAMYEAFSFIR 231 Arthrobacter sp. M...
ABQ29014  150 GRIKLVGPRHEFR-PGVELIELPGHSPGQMSLVIARPd-GPVILSSDAVHYYEELEkdrpf--tvmsGLLDMYRSLDAIR 225 Acidiphilium crypt...
AJE49187  151 GRLRIIAEDGAFA-EGLDHILIGGHAPGQMALRIETRr-GPVLLASDAVHLFEEMEgerpf--fvfhDMRRMLRGLRTCR 226 Celeribacter sp. P73
EHI39502  153 ERLELVDESGEVGtSGARITRYAGHTPGQVVTDIDIDh-KKVLLAADAVHYYDEIRrkrpf--ylftDLEQMLDSYDSLR 229 Rhodococcus opacus...
AGZ41416  151 GRLRPFDDEADLA-PGVRVIRLGGHTPGQSVVTVETTd-GVVLLASDSVHYYEEFErsmpf--tqvsGLVDMYAAFERIR 226 Actinoplanes friul...
KJC64843  159 DRLRLIDAETEIF-PGITVYPVGGHCPGELVVRVETAg-SSFILASDAAHFYEQIEnewpf--faftDIQEMRDGLTFIN 234 Agreia bicolorata
EHI39511  155 GRVHFVDGPETIL-PGITVTPIRGHTPGQMITEVKSGy-LNIVLASDALHFYEEKDrdrpf--wiycDLEGMYEGYERLN 230 Rhodococcus opacus...
Feature 1                   #  
3DHA_A    226 EVVKKe-KPIIFFGHDI 241 Bacillus thuringiensis serovar kurstaki
3DHB_A    226 EVVKKe-KPIIFFGHDI 241 Bacillus thuringiensis serovar kurstaki
EPG73904  258 LLAEQ--GTKIFTSHDP 272 Leptospira fainei serovar Hurstbridge str. BUT 6
KIA72934  232 EEASNh-GLTVVAGHDP 247 Arthrobacter sp. MWB30
ABQ29014  226 VMRETp-GAVLVPGHDP 241 Acidiphilium cryptum JF-5
AJE49187  227 RLAGS--DDRLVPGHDP 241 Celeribacter sp. P73
EHI39502  230 LLDERp-DVDVIPGHDP 245 Rhodococcus opacus PD630
AGZ41416  227 TMLATgeVRHLVPGHDP 243 Actinoplanes friuliensis DSM 7358
KJC64843  235 ALAAEt-GSTVVPGHDG 250 Agreia bicolorata
EHI39511  231 ELAEQp-DTVVVAGHDP 246 Rhodococcus opacus PD630

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