2J0X,2J0W,2CDQ,2J0X


Conserved Protein Domain Family
ACT_AKiii-LysC-EC-like_1
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cd04912: ACT_AKiii-LysC-EC-like_1 
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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) and plants, (Zea mays Ask1, Ask2, and Arabidopsis thaliana AK1). Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. Like the A. thaliana AK1 (AK1-AT), the E. coli AKIII (LysC) has two bound feedback allosteric inhibitor lysine molecules at the dimer interface located between the ACT1 domain of two subunits. The lysine-sensitive plant isoenzyme is synergistically inhibited by S-adenosylmethionine. A homolog of this group appears to be the Saccharomyces cerevisiae AK (Hom3) which clusters with this group as well. Members of this CD belong to the superfamily of ACT regulatory domains.
Links
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Statistics
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PSSM-Id: 153184
Aligned: 29 rows
Threshold Bit Score: 89.182
Created: 19-Sep-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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allostericdimer interface
Conserved site includes 10 residues -Click on image for an interactive view with Cn3D
Feature 1:allosteric regulatory binding pocket
Evidence:
  • Structure:2CDQ; Arabidopsis AK1 dimer with bound lysine; contacts of ACT1 domains with lysine.
    - View structure with Cn3D
  • Structure:2J0X; E. coli aspartokinase AKIII dimer, in the inactive T-state with bound lysine; contacts of ACT1 domains with lysine.
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  • 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.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                 #  # ###            ###    ##                                         
2J0X_A      308 QTLLTLHSLNMLHSRGFLAEVFGILARHNISVDLITTSEVSVALTLDTtgstst--------gdtllTQSLLMELSALCR 379 Escherichia coli
2CDQ_A      341 VTMLDIASTRMLGQVGFLAKVFSIFEELGISVDVVATSEVSISLTLDPsklwsr-------eliqqeLDHVVEELEKIAV 413 thale cress
NP_010972   362 IFVINIHSNKKTLSHGFLAQIFTILDKYKLVVDLISTSEVHVSMALPIpdad-----------slksLRQAEEKLRILGS 430 baker's yeast
CAH08580    304 ITAIKIKSSRMLLAHGFLRKVFEIFESYQTSIDMICTSEVGVSVSVDNtk----------------hLNEILDDLKKYGT 367 Bacteroides frag...
NP_906237   307 ITVIKVKSSNKLLSWHFMRKLFEIFEFYQEPVDMVATSEVGVSLTIDNdk----------------nLPDIVRALSDIGD 370 Porphyromonas gi...
ZP_00591577 321 QCIVNFRSNRMLGRHGFLIEFFNVFARAGVSVEMISTSEVSVSLTVSDta----------------aVDGLVRELAGMGE 384 Prosthecochloris...
ZP_01059529 303 ITAIKIKSNRMLGAHGFLRTIFEVFDRHETSIDMITTSEVAISLTIDDtr----------------nLKAIITELSVIAE 366 Flavobacterium s...
YP_590558   313 TKILNIRAPRLLINHGFLRSLFEVFEKHSLSPDLVNTSEVSVSVALDGtr----------------dVKALVSDLKRLGQ 376 Acidobacteria ba...
O60163      358 IMVINIQSNRKISAHGFLASIFAILDKYKLAVDLITTSEVHVSMALYEesd-------------dgnMHEAFVELRRLGT 424 fission yeast
EAL92034    386 ILVINVHSNKRSLSHGFFAGIFSVLDRWRLSIDLISTSEVHVSMALHSempllngvgrdeyqiidedLKGALNDLQKYGT 465 Aspergillus fumi...

Feature 1            
2J0X_A      380 VEVEE 384 Escherichia coli
2CDQ_A      414 VNLLK 418 thale cress
NP_010972   431 VDITK 435 baker's yeast
CAH08580    368 VTVDK 372 Bacteroides fragilis NCTC 9343
NP_906237   371 VTVDK 375 Porphyromonas gingivalis W83
ZP_00591577 385 VELEH 389 Prosthecochloris aestuarii DSM 271
ZP_01059529 367 VTVEE 371 Flavobacterium sp. MED217
YP_590558   377 VDVEN 381 Acidobacteria bacterium Ellin345
O60163      425 LDILH 429 fission yeast
EAL92034    466 VDIIP 470 Aspergillus fumigatus Af293

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