2CDQ,2J0X,2J0W,2J0X


Conserved Protein Domain Family
ACT_AK-like_1
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cd04890: ACT_AK-like_1 
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ACT domains found C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase)
This CD includes the first of two ACT domains found C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids, lysine, threonine, methionine, and isoleucine. This CD, includes the first ACT domain of the Escherichia coli (EC) isoenzyme, AKIII (LysC) and the Arabidopsis isoenzyme, asparate kinase 1, both enzymes monofunctional and involved in lysine synthesis, as well as the the first ACT domain of Bacillus subtilis (BS) isoenzyme, AKIII (YclM), and of the Saccharomyces cerevisiae AK (Hom3). Also included are the first ACT domains of the Methylomicrobium alcaliphilum AK, the first enzyme of the ectoine biosynthetic pathway. Members of this CD belong to the superfamily of ACT regulatory domains.
Links
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Statistics
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PSSM-Id: 153162
Aligned: 60 rows
Threshold Bit Score: 37.9126
Created: 26-Mar-2007
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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allosteric
Conserved site includes 7 residues -Click on image for an interactive view with Cn3D
Feature 1:allosteric regulatory binding residue
Evidence:
  • Structure:2CDQ; Arabidopsis AK1 dimer with bound lysine; contacts of ACT1 domains with lysine.
  • Structure:2J0X; E. coli aspartokinase AKIII dimer, in the inactive T-state with bound lysine; contacts of ACT1 domains with lysine.
  • Comment:defined by 3.5 Angstrom distance.
  • Comment:The Saccharomyces cerevisiae HOM3-ts31d mutant allele, having a Phe substituted for this Ser residue, encodes an aspartate kinase resistant to feedback-inhibition by threonine.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                      ###            ###    #                                 
2CDQ_A      342 TMLDIASTrml-gqVGFLAKVFSIFEelGISVDVVATSe--VSISLTLDpsklwsreliqqelDHVVEELE 409 thale cress
CAG35180    331 TCLEVHDTrmv-geVGFDMKIMEVLS--AHQVSYINKAtnaNTIGVIVYdnd---------ctEELLRDLR 389 Desulfotalea psychrophila...
ABA57537    331 FAIEFFEQdmv-gsSGYDTQLLALLE--RFKLKIVAKDtnaNTITHFVAssl--------kaiKRVTHAME 390 Nitrosococcus oceani ATCC...
NP_798098   325 FALHLFDQamvgkvDNVSYELMEIIS--DARVSLIGKEmnaNSITYYLGgss--------dslNKVLYKAE 385 Vibrio parahaemolyticus R...
YP_760351   330 FALEVFDQdmv-geKGYDSTILDALT--RHSIRIVSKCsnaNTITHYIEgsr--------kalKRATADIE 389 Hyphomonas neptunium ATCC...
ZP_01596487 332 FAVELFDQdmagdiDKFDVDILKVLR--QFHAHIIAKDinaNTITHYLAinl--------ktlKRVMRVLH 392 Marinomonas sp. MWYL1
ZP_01113085 331 YALNVFDQdmv-gePHQFLEIQQLVQ--EFNVPLLAKEhnaNTVTLYLDtgl--------kvvERIQARLE 390 Reinekea sp. MED297
ZP_01673421 331 TGIEVWDQdmv-grWDHDLEMLKHLA--AAKIRYLAKDtnaNTLTHYIAapl--------akiKRLTDNIK 390 Candidatus Desulfococcus ...
YP_390791   359 IALEVFDQemmgqqGSYEKVIIDATN--RLKCQVITKDfnaNTITIYLKasl--------kkvKRLAEQLK 419 Thiomicrospira crunogena ...
ZP_01168384 331 FGIEIFDQeml-gdAKYDIEISKLLA--QLKLYVINKDadaNSITYYVGgsr--------kmvNRAANLME 390 Oceanospirillum sp. MED92

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