4PFK
PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003824 | molecular_function | catalytic activity |
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 | 0016740 | molecular_function | transferase activity |
A | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0046835 | biological_process | carbohydrate phosphorylation |
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 |
Functional Information from PROSITE/UniProt
site_id | PS00433 |
Number of Residues | 19 |
Details | PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGsptafDR |
Chain | Residue | Details |
A | ARG243-ARG261 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00339 |
Chain | Residue | Details |
A | ASP127 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339 |
Chain | Residue | Details |
A | GLY11 | |
A | GLY102 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:6115424 |
Chain | Residue | Details |
A | ARG21 | |
A | ASP59 | |
A | ARG72 | |
A | ASP103 | |
A | ARG162 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:12390023, ECO:0000269|PubMed:6115424 |
Chain | Residue | Details |
A | THR125 | |
A | MET169 | |
A | GLU222 | |
A | HIS249 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:6115424 |
Chain | Residue | Details |
A | ARG154 | |
A | GLY185 | |
A | ARG211 | |
A | LYS213 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:12390023, ECO:0000269|PubMed:6115424 |
Chain | Residue | Details |
A | ARG243 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1pfk |
Chain | Residue | Details |
A | GLY11 | |
A | ASP127 | |
A | THR125 | |
A | ARG72 | |
A | ARG171 |