1B57,1DOS,1GVF


Conserved Protein Domain Family
FTBP_aldolase_II

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cd00453: FTBP_aldolase_II 
Click on image for an interactive view with Cn3D
Fructose/tagarose-bisphosphate aldolase class II. This family includes fructose-1,6-bisphosphate (FBP) and tagarose 1,6-bisphosphate (TBP) aldolases. FBP-aldolase is homodimeric and used in gluconeogenesis and glycolysis; the enzyme controls the condensation of dihydroxyacetone phosphate with glyceraldehyde-3-phosphate to yield fructose-1,6-bisphosphate. TBP-aldolase is tetrameric and produces tagarose-1,6-bisphosphate. There is an absolute requirement for a divalent metal ion, usually zinc, and in addition the enzymes are activated by monovalent cations such as Na+. Although structurally similar, the class I aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Statistics
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PSSM-Id: 238255
Aligned: 3 rows
Threshold Bit Score: 450.798
Created: 6-Mar-2002
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 20 residues -Click on image for an interactive view with Cn3D
Feature 1:active site
Evidence:
  • Comment:substrate (phosphoglycolohydroxamate, PGH) binding causes a conformational change in the mobile loop of the enzyme.
  • Structure:1DOS_A; substrate free; open conformation
  • Comment:the mobile loop closes over the active site after substrate binding.
  • Structure:1B57_A; substrate bound; closed conformation
  • Citation:PMID 9878448

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                       #                                                             
1B57_A     17 VQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQFSngGASFIAgkgvksdvpqgaailgaISGAHHVHQM 96  Escherichia coli
1DOS_A     17 VQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQFSngGASFIAgkgvksdvpqgaailgaISGAHHVHQM 96  Escherichia coli
1GVF_A      6 TKYLLQDAQANGYAVPAFNIHNAETIQAILEVCSEMRSPVILAGTp-GTFKHIa---------------lEEIYALCSAY 69  Escherichia coli
Feature 1                 ##                                 #                             # #
1B57_A     97 AEhygVPVILHTDHCakklLPWIDGLLDAGekhfaatgkplFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELG 176 Escherichia coli
1DOS_A     97 AEhygVPVILHTDHCakklLPWIDGLLDAGekhfaatgkplFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELG 176 Escherichia coli
1GVF_A     70 STtynMPLALHLDHHe--sLDDIRRKVHAG-----------VRSAMIDGSHFPFAENVKLVKSVVDFCHSQDCSVEAELG 136 Escherichia coli
Feature 1       ####                                          ### #                           
1B57_A    177 CTGGEEDGvdnshmdasalyTQPEDVDYAYTELskisprFTIAASFGNVHGVYkpgnVVLTPTILRDSQEyvskkhnlph 256 Escherichia coli
1DOS_A    177 CTGGEEDGvdnshmdasalyTQPEDVDYAYTELskisprFTIAASFGNVHGVYkagnVVLTPTILRDSQEyvskkhnlph 256 Escherichia coli
1GVF_A    137 RLGGVEDDmsvda--esaflTDPQEAKRFVELTg----vDSLAVAIGTAHGLYsk-tPKIDFQRLAEIREvv-------- 201 Escherichia coli
Feature 1            ## #                  # ##                                               
1B57_A    257 nsLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYkaneaylqgqlgnpkgedqpnkkyyDPRVWLRA 336 Escherichia coli
1DOS_A    257 nsLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYkaneaylqgqlgnpkgedqpnkkyyDPRVWLRA 336 Escherichia coli
1GVF_A    202 -dVPLVLHGASDVPDEFVRRTIELGVTKVNVATELKIAFAGAVKAWFaenp------------------qgnDPRYYMRV 262 Escherichia coli
Feature 1                         
1B57_A    337 GQTSMIARLekafqeLNAID 356 Escherichia coli
1DOS_A    337 GQTSMIARLekafqeLNAID 356 Escherichia coli
1GVF_A    263 GMDAMKEVVrnkinvCGSAN 282 Escherichia coli

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