2CDQ,2CDQ


Conserved Protein Domain Family
ACT_AK1-AT_2

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cd04918: ACT_AK1-AT_2 
Click on image for an interactive view with Cn3D
ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, plant aspartate kinase 1 (AK1)
This CD includes the second of two ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, plant aspartate kinase 1 (AK1), which can be synergistically inhibited by S-adenosylmethionine (SAM). This isoenzyme is found in higher plants, Arabidopsis thaliana (AT) and Zea mays, and also in Chlorophyta. In its inactive state, Arabidopsis AK1 binds the effectors lysine and SAM (two molecules each) at the interface of two ACT1 domain subunits. The second ACT domain (ACT2), this CD, does not interact with an effector. Members of this CD belong to the superfamily of ACT regulatory domains.
Statistics
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PSSM-Id: 153190
View PSSM: cd04918
Aligned: 4 rows
Threshold Bit Score: 120.761
Threshold Setting Gi: 116000390
Created: 4-Apr-2007
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
dimer interface
Conserved site includes 18 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:
  • Structure:2CDQ; Arabidopsis thaliana aspartate kinase dimer; contacts of ACT domain 2 from one monomer, with the other monomer at 3.5A.
    View structure with Cn3D
  • Comment:ACT domain 2 does not bind effectors.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1              ##  #   #   #      ############ #                       
2CDQ_A    420 RAIISLIGNVQHSSLILERAFHVLYtkGVNVQMISQGASKVNISFIVNEAEAEGCVQALHKSFFE 484 thale cress
2CDQ_B    420 RAIISLIGNVQHSSLILERAFHVLYtkGVNVQMISQGASKVNISFIVNEAEAEGCVQALHKSFFE 484 thale cress
ABO09875  489 RSIISLIGNVQRSSLILEKAFNVLRrnGVNVQMISQGASKVNISLVVNDSEAKQCVQALHSAFFE 553 Zea mays
CAL50070  359 HSIISLIGNVERNNEIMERAFRALGskDIKVKMVSQGASKTNISLLVNDSQGADAARAIHAEFFE 423 Ostreococcus tauri

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