2J0W,2J0X,2J0X


Conserved Protein Domain Family
ACT_AKiii-LysC-EC_1

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cd04932: ACT_AKiii-LysC-EC_1 
Click on image for an interactive view with Cn3D
ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII
This CD includes the first of two ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in bacteria (Escherichia coli (EC) LysC). Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. The E. coli AKIII (LysC) binds two feedback allosteric inhibitor lysine molecules at the dimer interface located between the ACT1 domain of two subunits. Members of this CD belong to the superfamily of ACT regulatory domains.
Statistics
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PSSM-Id: 153204
View PSSM: cd04932
Aligned: 10 rows
Threshold Bit Score: 112.124
Threshold Setting Gi: 114794887
Created: 30-Mar-2007
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1: lysine allosteric regulatory site
Evidence:
  • Structure:2J0X; E. coli aspartokinase AKIII dimer, in the inactive T-state with bound lysine; contacts of ACT1 domains with lysine.
    View structure with Cn3D
  • Comment:defined by 3.5 Angstrom distance.
  • Comment:two feedback allosteric inhibitor lysine molecules are bound at the dimer interface located between the ACT1 domains of two subunits.
  • Comment:E. coli AKIII (2J0W) in the active R-state binds aspartate and ADP in the catalytic domain.
  • Comment:Comparison of R- and T-state AKIII indicates that binding of lysine to the regulatory ACT1 domain in R-state AKIII instigates a series of changes that release a "latch" from the catalytic domain, which in turn undergoes large rotational rearrangements, promoting tetramer formation and completion of the transition to the T-state.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                 #  #  ##            ###    ##                                      
2J0W_A      308 QTLLTLHSLNMLHSRGFLAEVFGILARHNISVDLITTSEVSVALTLDTTgststgdtlLTQSLLMELSALCRVEVEE 384 Escherichia coli
2J0X_A      308 QTLLTLHSLNMLHSRGFLAEVFGILARHNISVDLITTSEVSVALTLDTTgststgdtlLTQSLLMELSALCRVEVEE 384 Escherichia coli
2J0X_B      308 QTLLTLHSLNMLHSRGFLAEVFGILARHNISVDLITTSEVSVALTLDTTgststgdtlLTQSLLMELSALCRVEVEE 384 Escherichia coli
NP_873799   309 QTLVTLSSLAMLHAQEFLASVFSILAKYQVSVDIITTSEVSITLTLDKTdstastaqiLSDALVHELSQFCHIKIEN 385 Haemophilus ducreyi...
YP_268734   317 QTLVTVKSPAMLHASGFLAKVFGVLAKHELSIDLITTSEISVALTFDNPsgst--qslITNAVVAELEQLCEVSVEH 391 Colwellia psychrery...
ZP_01110754 310 QVMVTVKTPKMMYAQGFLQQVFAIIAKHKLSVDLVTTSEISVSFTLDNPansv--aqrLNKETIAELETICDVKVEK 384 Alteromonas macleod...
ZP_01135933 308 QILLTLKSPEMLLASGFLARVFTILSEYNISVDLVTTSEISVALTLDNApnas--rpeLDQACLQRLSEFCHVTVEN 382 Pseudoalteromonas t...
NP_967151   319 QVLVTLSTPEMLYAHGFLFQIFKIFNDHKVSIDAITTSEISVSVTLDDSt-------lLNKNLIKDLSQIADVQVEE 388 Bdellovibrio bacter...
ZP_01450574 310 QVMVTVKTPKMMYAQGFLAKVFEIIAKHELSVDLVTTSEISVSFTLDNPpnsv--aerLNRVTIEELQDICDVTVER 384 alpha proteobacteri...
YP_899336   308 QTLLTIKSFNMFGSQGFLVKVFSILANHNIAVDLVSTSEVSVAITLDKLgshsmgddlVTPELLKDLESIGNVNIKV 384 Francisella tularen...

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