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9MED

Crystal Structure Pyrophosphate-fructose 6-phosphate 1-phosphotransferase 1 (Pfk1) from Trichomonas vaginalis (AMP/beta-D-Glucose-6-phosphate complex)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003872molecular_function6-phosphofructokinase activity
A0005737cellular_componentcytoplasm
A0006002biological_processfructose 6-phosphate metabolic process
A0006096biological_processglycolytic process
A0008443molecular_functionphosphofructokinase activity
A0009749biological_processresponse to glucose
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
A0047334molecular_functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
A0061615biological_processglycolytic process through fructose-6-phosphate
B0003872molecular_function6-phosphofructokinase activity
B0005737cellular_componentcytoplasm
B0006002biological_processfructose 6-phosphate metabolic process
B0006096biological_processglycolytic process
B0008443molecular_functionphosphofructokinase activity
B0009749biological_processresponse to glucose
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0046835biological_processcarbohydrate phosphorylation
B0046872molecular_functionmetal ion binding
B0047334molecular_functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
B0061615biological_processglycolytic process through fructose-6-phosphate
C0003872molecular_function6-phosphofructokinase activity
C0005737cellular_componentcytoplasm
C0006002biological_processfructose 6-phosphate metabolic process
C0006096biological_processglycolytic process
C0008443molecular_functionphosphofructokinase activity
C0009749biological_processresponse to glucose
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0046835biological_processcarbohydrate phosphorylation
C0046872molecular_functionmetal ion binding
C0047334molecular_functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
C0061615biological_processglycolytic process through fructose-6-phosphate
D0003872molecular_function6-phosphofructokinase activity
D0005737cellular_componentcytoplasm
D0006002biological_processfructose 6-phosphate metabolic process
D0006096biological_processglycolytic process
D0008443molecular_functionphosphofructokinase activity
D0009749biological_processresponse to glucose
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0046835biological_processcarbohydrate phosphorylation
D0046872molecular_functionmetal ion binding
D0047334molecular_functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
D0061615biological_processglycolytic process through fructose-6-phosphate
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP","evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi","evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-07-23

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