2IQ8


Conserved Protein Domain Family
ACT_CM-PDT

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cd04905: ACT_CM-PDT 
Click on image for an interactive view with Cn3D
C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme
The C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme, found in plants, fungi, bacteria, and archaea. The P-protein of E. coli (CM-PDT, PheA) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains.
Statistics
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PSSM-Id: 153177
View PSSM: cd04905
Aligned: 148 rows
Threshold Bit Score: 64.0581
Threshold Setting Gi: 28199252
Created: 24-Aug-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
putative L-Phe
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:putative L-Phe binding site [chemical binding site]
Evidence:
  • Comment:Based on sequence similarity with PAH and 3PGDH and by mutational analyses, these two regions are predicted to be involved in L-Phe binding.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                      ####                ####                                         
2IQ8_A      188 SLXFLITPXHd--KPGLLASVLNTFAlfNINLSWIESRPLkt--------------qlGXYRFFVQADsa--iTTDIKKV 249 Staphylococcus a...
NP_014083   241 VNLLTFTTRQd--DPGSLVDVLNILKihSLNMCSINSRPFhlde----------hdrnWRYLFFIEYYtekntPKNKEKF 308 baker's yeast
CAG62499    245 VSLLTFTIKQd--DPGSLVEVLSVLKdfSLNMCSISSRPYllrseqisqqgenfrrrnWQYIFFIEFYieqdkEFDKDKF 322 Candida glabrata...
CAG99359    218 VNFVTFVINQd--DPGSLIDVLNVLReyKLNMCSISSRPFhnqvq---------serkWQYCFFIEFYgn--yGTDYELL 284 Kluyveromyces la...
AAK78199    191 YKTGIIISDAnadKPGTLWRVLNEFSvrDINLTSIISRPTkk--------------glGQYYFFIEVDgcyfkDNRLNEA 256 Clostridium acet...
NP_696546   204 ETIITFIPLVt--GPGVLADLLDVLRdaGLNMTSFISRPIkg--------------hdGTYSFIATLDaa-pwEPRFRTA 266 Bifidobacterium ...
AAS51740    230 IHLVAFTTDRq--GAGSLTDVLLVLKryGIDMRSITSRPFrrcs----------tsskWQYVFFVEYSde--lDVPWDSF 295 Ashbya gossypii ...
CAC12044    199 RHIILCVIPD---RPGSLHSLIGVLAsrGINMNMIYSRPLrd--------------tiWKYYFYIEFSg----KLDEDLL 257 Thermoplasma aci...
NP_779566   296 LAFSVYLPED---RPGSLQRLLHVFEqhGINLSSIHSSRTp----------------aGELHFRISFD-----PGSDRVA 351 Xylella fastidio...
ZP_01215543 193 KTTLVVKNDNd--CPGVLGNIINAFAaqKVNLTSIMSRPTks--------------qfGQYHFFIDIDgh-qqDENIKLA 255 Psychromonas sp....
Feature 1                         
2IQ8_A      250 IAILETlDFKVEXIGAFN 267 Staphylococcus aureus
NP_014083   309 YEDISDkSKQWCLWGTFP 326 baker's yeast
CAG62499    323 CDRIDAlCGDWCHWGRFP 340 Candida glabrata CBS138
CAG99359    285 AKRFDEnCAKWIHWGKFY 302 Kluyveromyces lactis NRRL Y-1140
AAK78199    257 VEAIKH-HSVVKVVGTYY 273 Clostridium acetobutylicum ATCC 824
NP_696546   267 LEEIAGhGDWAKTLAVYP 284 Bifidobacterium longum NCC2705
AAS51740    296 HAEVGAhCREWCHWGTFY 313 Ashbya gossypii ATCC 10895
CAC12044    258 LTMGKQ-SLRILYKGSFK 274 Thermoplasma acidophilum
NP_779566   352 LMRAAD-EIDMRRIGCVL 368 Xylella fastidiosa Temecula1
ZP_01215543 256 ILNIKN-DHVIRVLGSYP 272 Psychromonas sp. CNPT3

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