3IX1,4H67,3QSL


Conserved Protein Domain Family
PBP2_ThiY_THI5_like

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cd13564: PBP2_ThiY_THI5_like 
Click on image for an interactive view with Cn3D
Substrate binding domain of ABC-type transporter for thiamin biosynthetic pathway intermediates and similar proteins; the type 2 periplasmic binding protein fold.
ThiY is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ThiY/THI5 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Statistics
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PSSM-Id: 270282
Aligned: 4 rows
Threshold Bit Score: 272.453
Created: 27-Jun-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
chemical
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:chemical substrate binding site [chemical binding site]
Evidence:
  • Structure:3IX1; the periplasmic ThiY protein from Bacillus halodurans binds FAMP (N-Formyl-4-Amino-5-Aminomethyl-2-Methylpyrimidine), contacts at 4A.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1            #                               #                                        
3IX1_A      4 TVEVMLDWYpnavHTFLYVAIENGYFaeeGLDVDIVFPTNPTDPIQLTASGAIPLALSYqPDVILARskdLPVVSVASVv 83  Bacillus haloduran...
4H67_A      5 KITFLLNWQptpyHIPIFLAQTKGYFkeqGLDMAILEPTNPSDVTELIGSGKVDMGLKAmIHTLAAKargFPVTSVASLl 84  baker's yeast
3QSL_A     34 KVQIAVGGKpliyYLPLTIAEVKGFFkdeGLDVSIADFAGGSKALQAVVGGSADVVSGAfEHTLSLQakgQFYRAFALQg 113 Bordetella bronchi...
BAF33366   38 TTTVKVGLIpivdVAPLYLGQQKGIYskhGLKLEITTAQGGAAIVPGVASGQFQFGFSNvTSLMVAQsnnVPVKAVANAi 117 Streptomyces sp. N...
Feature 1               #                         #     #                                     
3IX1_A     84 r------sPLNHVMFLAeqdf--dspaDLVGLTVGYPGIp-VNEPILKTMVEAAGgdyeQVHLMDVgf--eLGASIVSGr 152 Bacillus haloduran...
4H67_A     85 d------ePFTGVLYLKgsgit-edfqSLKGKKIGYVGE--FGKIQIDELTKHYGmkpeDYTAVRCgm--nVAKYIIEGk 153 baker's yeast
3QSL_A    114 r------aPXIGVGVSKknlpgykgpaDLKGRKIGVTAPgsSTNXVVNFFLAKHGlkasDVSFIGVgagagAVTALRSGq 187 Bordetella bronchi...
BAF33366  118 astgvegkDFSGLTVKQdspi--kspkDLEGKKVAINTLknINETAVRASVRKAGgdpdKVKFVELaf-dqMPAALDSGq 194 Streptomyces sp. N...
Feature 1          ##    #                                        #                          
3IX1_A    153 ADAVVGTyinHEYPVLKHEgh-------dISYFNPVdygv-------peydELVLISNEayveeSGEVLAAFWRAALKG 217 Bacillus halodurans...
4H67_A    154 IDAGIGIe-cMQQVELEEYlakqgrpasdAKMLRIDklaclg----cccfcTVLYICNDeflkkNPEKVRKFLKAIKKA 227 baker's yeast
3QSL_A    188 IDAISNTd--PVVSXLETSg--------dIQIIVDTrtlkdtkeifggnxpAGCLYAPQafvdaNPNTAQALTNAIVRA 256 Bordetella bronchis...
BAF33366  195 IDAAQVVe--PALATIKSQgg-------rVIASPLVdvap--------dltVAMYFTSTqyaqqNPEVVKKFQAATAEA 256 Streptomyces sp. NL...

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