1PSD,1YBA,1SC6,1YBA


Conserved Protein Domain Family
ACT_3PGDH

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cd04901: ACT_3PGDH 
Click on image for an interactive view with Cn3D
C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria
The C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In Escherichia coli, the SerA 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. In the homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. Members of this CD belong to the superfamily of ACT regulatory domains.
Statistics
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PSSM-Id: 153173
View PSSM: cd04901
Aligned: 53 rows
Threshold Bit Score: 81.0148
Threshold Setting Gi: 49480110
Created: 18-Aug-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
L-serineACT domain
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:L-serine binding site [chemical binding site]
Evidence:
  • Structure:1YBA; active conformation of E. coli 3PGDH homotetramer in the absence of serine; the four L-serine binding sites are highlighted.
    View structure with Cn3D
  • Structure:1PSD_A; E. coli 3PGDH homodimer, contacts of one monomer with a single L-serine at 3.5 A.
    View structure with Cn3D
  • Citation:PMID 7719856
  • Comment:The bound serine inhibitor spans the ACT-ACT interface forming hydrogen bond with conserved residues (generally His and Asn) of one subunit with a second Asn of the adjacent subunit.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1            # #                 #                                               
1PSD_A      338 RLMHIHENRPGVLTALNKIFAeqGVNIAAQYLQTSaqMGYVVIDIEAde--dVAEKALQAMKAIpGTIRARLL 408 Escherichia coli
1YBA_D      339 RLXHIHENRPGVLTALNKIFAeqGVNIAAQYLQTSaqXGYVVIDIEAde--dVAEKALQAXKAIpGTIRARLL 409 Escherichia coli
NP_784030   315 RFTVIHENVPNMVSQITAKLAaaNLNITTMANAAKhqIAYTIIDVDDlq-qpQQADLIAELSKIpAVSRVRLL 386 Lactobacillus plantarum...
NP_266760   321 RVTLINKNVPNVVAQISLAVAaeNINIANIVNRGQgdYAYTLLDLDEkd-egKLAALVSRFEAAdNIIRVRLI 392 Lactococcus lactis subs...
ZP_00538167 316 RLTIAHQNIPNMVGQIASVLAteQINIANMINGSKdgIAYTIIDIDNh---lDETISLEQLNAIpGVLKTRLL 385 Exiguobacterium sp. 255-15
ZP_00233239 325 RIGICHKNIPNMVGQITTELGkySLNILDMINRSKneYAYTLIDIDKet-qaNLEQLKQDLLAVqGVLRVRVI 396 Listeria monocytogenes ...
YP_037345   317 RITIMHQNVPNMVGQITGCLAehHINIADMINRSKhsWAYTMIDIDNgiddiIKENIVENISKItGVVAVRMI 389 Bacillus thuringiensis ...
ZP_00531765 319 RIAISNSNVPKMVGQITSVLAdsGINIVDMLNKSRgdIAYNLLDLGTe----VGKDIADKIKKIeGVLAVRIM 387 Chlorobium phaeobactero...
YP_903847   317 RLAITHKNIPNMVGQISTTIAdsGANIVDMLNKSKgdIAYTLVDLEHe----ISPSVFNNLKQVkDILTVRGL 385 Candidatus Ruthia magni...
YP_534996   316 RLTLIHQNVPNMVGRITTILAkeEINIDNMINRSRgkIAYTMIDAADis-egKLKELKKELLEIpEVIRVRAL 387 Lactobacillus salivariu...

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