Conserved Protein Domain Family
ACT_AK-Hom3_2

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cd04919: ACT_AK-Hom3_2 
ACT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3
This CD includes the second of two ACT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae, and other related ACT domains. AK is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single AK, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies shown that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size. Members of this CD belong to the superfamily of ACT regulatory domains.
Statistics
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PSSM-Id: 153191
View PSSM: cd04919
Aligned: 4 rows
Threshold Bit Score: 124.169
Threshold Setting Gi: 21622337
Created: 15-Sep-2005
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
putative
Feature 1:putative threonine allosteric regulatory residues
Evidence:
  • Comment:The G-452-D Saccharomyces cerevisiae HOM3-R2 mutant contains an AK activity insensitive to inhibition by threonine.
  • Comment:The S-472-Y point mutation involved in HOM3 regulation.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                    #                   #                              
NP_010972 437 LSIVSLVGKHMKQYIGIAGTMFTTLAEeGINIEMISQGANEINISCVINESDSIKALQCIHAKLLS 502 baker's yeast
EAK81622  556 MAILSLVGKHMRNMVGVAGRMFTVLADgNVNIEMISQGASEINISCVLHEKLAVKALNLIHYSVLE 621 Ustilago maydis 521
18202097  431 LAILSLVGKHMRNTTGYAGRMFCKLAEaQINIEMISQGASEINISCVIDEKMAVKALNVIHKELLE 496 fission yeast
CAD36978  454 LAILSLVGAEMKNMIGISGKMFSTLGDhRINIEMISQGASEINISCVIDARDAERAMNILHTNLFT 519 Neurospora crassa

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