1PSU,1J1Y,1O0I,1Q4S,1SBK,1SH8,1VH9,1YOC,1ZKI


Conserved Protein Domain Family
PaaI_thioesterase

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cd03443: PaaI_thioesterase 
Click on image for an interactive view with Cn3D
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).
Statistics
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PSSM-Id: 239527
Aligned: 456 rows
Threshold Bit Score: 47.5526
Created: 4-Apr-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:CoenzymeA binding site [chemical binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                     #                                         #      #
1PSU_A       21 ALGIDIISXDEGFAVVTXTVTaqXLNGHQSCHGGQLFSLADTAFAYACnsq----------------glaAVASACTIDF 84  Escherichia coli
1Q4S_A       33 TVGFVIDEMTPERATASVEVTdtLRQRWGLVHGGAYCALAEMLATEATvavvh------------ekgmmAVGQSNHTSF 100 Arthrobacter sp.
AAF11582     26 TVGVQITDVGLGWASGECPDTppFRNHLGTIHAGAQFLLAEAVSGAAFagafvq----------yvgeavPLIEKLETHY 95  Deinococcus radi...
CAD73154     39 AVQWKVTSVTEGGCESVLPLTkaSTNQHGTHQAALISLSADYTGGLALttllrgvplagihrcndedsasLWLAAMDVKY 118 Rhodopirellula b...
NP_902156    40 TAGLRFEQVGHDRLTVSIRNRkkVQNHIRGVHAAAMALLAETSTGFVVgmnmp-------------ddklMLLKSMKVNY 106 Chromobacterium ...
CAG69829     49 TANIRYLEVDQHHVTVRLENQrnMQNHIKGIHAAAMALLAETATGFLTglhvp-------------dnriLLIKSLHVDY 115 Acinetobacter sp...
ZP_00400450  21 FLGPRVLELDEQGCAVKIPLRwqSRNHLGSMYFGALCAGADIAGGLVAarliyt----------khkgvtLIFADLKADF 90  Anaeromyxobacter...
ZP_00653812  74 TTGIYYETVEPNQVVVSLNNTkaVQNHIGSVHAVAITLLAETATGFILglnlp-------------adrvLLIKSYSVNF 140 Psychrobacter cr...
AAZ54123     22 ILGVEFVELAEERAVMRLPDNpdHYDHTQNQHAGALIVLAETTSGAAVfnalgd----------rlklalPVSLDARVDH 91  Thermobifida fus...
ZP_00774227  39 TTSIDVVATNGRQVEYRMKNRkkVQNHIGSVHAAAMALLAESATGFIVginlp-------------gdklPLIKCMNLNY 105 Pseudoalteromona...
Feature 1       ###                                                           
1PSU_A       85 LRPGfagdTLTATAQVRHQ------------GKQTGVYDIEIVNqq---qKTVALFRGKSHR 131 Escherichia coli
1Q4S_A      101 FRPVke-gHVRAEAVRIHA------------GSTTWFWDVSLRDda---gRLCAVSSMSIAV 146 Arthrobacter sp.
AAF11582     96 VGRAv--gDLTARAEIDPAalpaayaeyqadGRARLPVKVTVKDge---dKPVMEAQAHWYL 152 Deinococcus radiodurans R1
CAD73154    119 RNPSt--gHLTATCDIPANiartvq-qryfnGKRVLVTLPVVFTsn---gELVAEAEMRYFA 174 Rhodopirellula baltica SH 1
NP_902156   107 VKRSq--gDMKAVATLTPQ------------QIQSMYEQEKGEVlv---eVLVTDESGESPI 151 Chromobacterium violaceum ATCC 12472
CAG69829    116 LKVVq--gGLTATATLSKE------------QQDYIADQEKGELli---pVTVTDDSGIEPI 160 Acinetobacter sp. ADP1
ZP_00400450  91 LKRAd--gDVVFRSRDGARvteavreadrtgERVTVPVEVVATVpdkygdEPVARFTLGLSL 150 Anaeromyxobacter dehalogenans 2CP-C
ZP_00653812 141 YRPIkk-gQMAAIASLSDEqrld----ilntPKGEMIIPCVIHDresdsdRDPIVVEMTWAW 197 Psychrobacter cryohalolentis K5
AAZ54123     92 RQPFs--gPVVAEAVLGEEwrtalt-eleagGQPEFPVDVALRAen---gSTTGTATITWML 147 Thermobifida fusca YX
ZP_00774227 106 VKRAt--gDMKAIATLTDEqial----lqerEKGEINVQVKVTDat---gIEPVECEMIWAW 158 Pseudoalteromonas atlantica T6c

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