5HR5
Bovine Heart 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase (PFKFB2)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0003873 | molecular_function | 6-phosphofructo-2-kinase activity |
A | 0004331 | molecular_function | fructose-2,6-bisphosphate 2-phosphatase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006000 | biological_process | fructose metabolic process |
A | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
A | 0006096 | biological_process | glycolytic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046835 | biological_process | carbohydrate phosphorylation |
Functional Information from PROSITE/UniProt
site_id | PS00175 |
Number of Residues | 10 |
Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEsEfN |
Chain | Residue | Details |
A | LEU255-ASN264 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000255 |
Chain | Residue | Details |
A | ASP129 | |
A | CYS159 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250|UniProtKB:Q16875 |
Chain | Residue | Details |
A | NEP258 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q16875 |
Chain | Residue | Details |
A | GLU327 |
site_id | SWS_FT_FI4 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q16875 |
Chain | Residue | Details |
A | GLY46 | |
A | ARG257 | |
A | ASN264 | |
A | GLY270 | |
A | TYR338 | |
A | ARG352 | |
A | LYS356 | |
A | TYR367 | |
A | GLN393 | |
A | TYR429 | |
A | ARG79 | |
A | ARG103 | |
A | THR131 | |
A | ARG137 | |
A | ASN168 | |
A | LYS173 | |
A | ARG194 | |
A | TYR198 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07953 |
Chain | Residue | Details |
A | PHE349 | |
A | ARG397 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:Q16875 |
Chain | Residue | Details |
A | ARG257 | |
A | ASN264 | |
A | HIS392 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:O60825 |
Chain | Residue | Details |
A | SER2 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:2846551 |
Chain | Residue | Details |
A | SER467 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O60825 |
Chain | Residue | Details |
A | THR469 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by AMPK and PKC => ECO:0000269|PubMed:2846551 |
Chain | Residue | Details |
A | THR476 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O60825 |
Chain | Residue | Details |
A | SER484 | |
A | SER494 |