4I36

Crystal Structure of the Bacillus stearothermophilus Phosphofructokinase Mutant D12A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003872	molecular_function	6-phosphofructokinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005945	cellular_component	6-phosphofructokinase complex
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006096	biological_process	glycolytic process
A	0008443	molecular_function	phosphofructokinase activity
A	0016208	molecular_function	AMP binding
A	0016301	molecular_function	kinase activity
A	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0048029	molecular_function	monosaccharide binding
A	0061621	biological_process	canonical glycolysis
A	0070095	molecular_function	fructose-6-phosphate binding
B	0003872	molecular_function	6-phosphofructokinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005945	cellular_component	6-phosphofructokinase complex
B	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006096	biological_process	glycolytic process
B	0008443	molecular_function	phosphofructokinase activity
B	0016208	molecular_function	AMP binding
B	0016301	molecular_function	kinase activity
B	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0048029	molecular_function	monosaccharide binding
B	0061621	biological_process	canonical glycolysis
B	0070095	molecular_function	fructose-6-phosphate binding
C	0003872	molecular_function	6-phosphofructokinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005945	cellular_component	6-phosphofructokinase complex
C	0006002	biological_process	fructose 6-phosphate metabolic process
C	0006096	biological_process	glycolytic process
C	0008443	molecular_function	phosphofructokinase activity
C	0016208	molecular_function	AMP binding
C	0016301	molecular_function	kinase activity
C	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0048029	molecular_function	monosaccharide binding
C	0061621	biological_process	canonical glycolysis
C	0070095	molecular_function	fructose-6-phosphate binding
D	0003872	molecular_function	6-phosphofructokinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005945	cellular_component	6-phosphofructokinase complex
D	0006002	biological_process	fructose 6-phosphate metabolic process
D	0006096	biological_process	glycolytic process
D	0008443	molecular_function	phosphofructokinase activity
D	0016208	molecular_function	AMP binding
D	0016301	molecular_function	kinase activity
D	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0048029	molecular_function	monosaccharide binding
D	0061621	biological_process	canonical glycolysis
D	0070095	molecular_function	fructose-6-phosphate binding

Functional Information from PROSITE/UniProt

site_id	PS00433
Number of Residues	19
Details	PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGsptafDR

Chain	Residue	Details
A	ARG243-ARG261

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00339

Chain	Residue	Details
A	ASP127
B	ASP127
C	ASP127
D	ASP127

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339

Chain	Residue	Details
A	GLY11
A	GLY102
B	GLY11
B	GLY102
C	GLY11
C	GLY102
D	GLY11
D	GLY102

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:6115424

Chain	Residue	Details
A	ARG21
B	ARG162
C	ARG21
C	ASP59
C	ARG72
C	ASP103
C	ARG162
D	ARG21
D	ASP59
D	ARG72
D	ASP103
A	ASP59
D	ARG162
A	ARG72
A	ASP103
A	ARG162
B	ARG21
B	ASP59
B	ARG72
B	ASP103

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:12390023, ECO:0000269|PubMed:6115424

Chain	Residue	Details
A	THR125
C	MET169
C	GLU222
C	HIS249
D	THR125
D	MET169
D	GLU222
D	HIS249
A	MET169
A	GLU222
A	HIS249
B	THR125
B	MET169
B	GLU222
B	HIS249
C	THR125

---

site_id	SWS_FT_FI5
Number of Residues	16
Details	BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:6115424

Chain	Residue	Details
A	ARG154
C	GLY185
C	ARG211
C	LYS213
D	ARG154
D	GLY185
D	ARG211
D	LYS213
A	GLY185
A	ARG211
A	LYS213
B	ARG154
B	GLY185
B	ARG211
B	LYS213
C	ARG154

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:12390023, ECO:0000269|PubMed:6115424

Chain	Residue	Details
A	ARG243
B	ARG243
C	ARG243
D	ARG243

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