9MDT

Crystal Structure Pyrophosphate-fructose 6-phosphate 1-phosphotransferase 1 (Pfk1) from Trichomonas vaginalis (ATP/Pyrophosphate complex)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003872	molecular_function	6-phosphofructokinase activity
A	0005737	cellular_component	cytoplasm
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006096	biological_process	glycolytic process
A	0008443	molecular_function	phosphofructokinase activity
A	0009749	biological_process	response to glucose
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0046835	biological_process	carbohydrate phosphorylation
A	0046872	molecular_function	metal ion binding
A	0047334	molecular_function	diphosphate-fructose-6-phosphate 1-phosphotransferase activity
A	0061615	biological_process	glycolytic process through fructose-6-phosphate
B	0003872	molecular_function	6-phosphofructokinase activity
B	0005737	cellular_component	cytoplasm
B	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006096	biological_process	glycolytic process
B	0008443	molecular_function	phosphofructokinase activity
B	0009749	biological_process	response to glucose
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0046835	biological_process	carbohydrate phosphorylation
B	0046872	molecular_function	metal ion binding
B	0047334	molecular_function	diphosphate-fructose-6-phosphate 1-phosphotransferase activity
B	0061615	biological_process	glycolytic process through fructose-6-phosphate
C	0003872	molecular_function	6-phosphofructokinase activity
C	0005737	cellular_component	cytoplasm
C	0006002	biological_process	fructose 6-phosphate metabolic process
C	0006096	biological_process	glycolytic process
C	0008443	molecular_function	phosphofructokinase activity
C	0009749	biological_process	response to glucose
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0046835	biological_process	carbohydrate phosphorylation
C	0046872	molecular_function	metal ion binding
C	0047334	molecular_function	diphosphate-fructose-6-phosphate 1-phosphotransferase activity
C	0061615	biological_process	glycolytic process through fructose-6-phosphate
D	0003872	molecular_function	6-phosphofructokinase activity
D	0005737	cellular_component	cytoplasm
D	0006002	biological_process	fructose 6-phosphate metabolic process
D	0006096	biological_process	glycolytic process
D	0008443	molecular_function	phosphofructokinase activity
D	0009749	biological_process	response to glucose
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0046835	biological_process	carbohydrate phosphorylation
D	0046872	molecular_function	metal ion binding
D	0047334	molecular_function	diphosphate-fructose-6-phosphate 1-phosphotransferase activity
D	0061615	biological_process	glycolytic process through fructose-6-phosphate

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01979

Chain	Residue	Details
A	ASP142
B	ASP142
C	ASP142
D	ASP142

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01979

Chain	Residue	Details
A	GLY15
B	MET186
B	GLU247
B	TYR308
C	GLY15
C	ASP114
C	THR140
C	MET186
C	GLU247
C	TYR308
D	GLY15
A	ASP114
D	ASP114
D	THR140
D	MET186
D	GLU247
D	TYR308
A	THR140
A	MET186
A	GLU247
A	TYR308
B	GLY15
B	ASP114
B	THR140

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: 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 => ECO:0000255|HAMAP-Rule:MF_01979

Chain	Residue	Details
A	ASP115
B	ASP115
C	ASP115
D	ASP115

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site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi => ECO:0000255|HAMAP-Rule:MF_01979

Chain	Residue	Details
A	LYS139
B	LYS139
C	LYS139
D	LYS139

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