B2AT75 · B2AT75_PODAN
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids848 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic activity
- beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H+
Cofactor
Activity regulation
Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
Pathway
Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 78 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 141-142 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 171-174 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 172 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 217-219 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 219 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 254 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 261-263 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 317 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 347 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 353-356 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 536 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 594-598 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 632 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 639-641 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: QGG | ||||||
Binding site | 699 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 725 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 731-734 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 803 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 6-phosphofructokinase complex | |
Cellular Component | membrane | |
Cellular Component | mitochondrion | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Molecular Function | fructose-6-phosphate binding | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | monosaccharide binding | |
Biological Process | canonical glycolysis | |
Biological Process | fructose 1,6-bisphosphate metabolic process | |
Biological Process | fructose 6-phosphate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent 6-phosphofructokinase
- EC number
- Short namesATP-PFK ; Phosphofructokinase
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Podosporaceae > Podospora > Podospora anserina
Accessions
- Primary accessionB2AT75
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 9-28 | Helical | ||||
Sequence: LLRPFSIVIYPIWTLLAFFY |
Keywords
- Cellular component
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-445 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MPLPDTRFLLRPFSIVIYPIWTLLAFFYRHSPLRFLSSTLQPLFGLRNTTDIDPETPEPTSTTNMSAKKKIAIMTSGGDSPGMNGVVRACVRMAIHMGCDAYCIYEGYEGLVRGGDLIRKMNWYDVRGWLSEGGTLIGTARCMAFFERAGRLAAAKNMILHGIDALIICGGDGSLTGADRFRAEWPSLLDELAANGEFTTQELQPFRHLNIVGLVGSIDNDLSGTDATIGCYSALARICYAVDLIEATASSHSRAFVVEVMGRHCGWLALMAGVATGADFIFIPEKPREDNWREEMCSIVEHHRKIGKRKTIVIIAEGALDREGNKITPAMVKDLLADKDGLGLDTRITTLGHVQRGGTAVAYDRMLATLQGVEAVKAVLEATPETKTCVIAITENKIVRKPLMDAVQDTKKVAKAIERQDFEEAMGLRDAEFSEQYKSFMMTTA | ||||||
Domain | 70-378 | Phosphofructokinase | ||||
Sequence: KIAIMTSGGDSPGMNGVVRACVRMAIHMGCDAYCIYEGYEGLVRGGDLIRKMNWYDVRGWLSEGGTLIGTARCMAFFERAGRLAAAKNMILHGIDALIICGGDGSLTGADRFRAEWPSLLDELAANGEFTTQELQPFRHLNIVGLVGSIDNDLSGTDATIGCYSALARICYAVDLIEATASSHSRAFVVEVMGRHCGWLALMAGVATGADFIFIPEKPREDNWREEMCSIVEHHRKIGKRKTIVIIAEGALDREGNKITPAMVKDLLADKDGLGLDTRITTLGHVQRGGTAVAYDRMLATLQGVEAVKA | ||||||
Domain | 461-756 | Phosphofructokinase | ||||
Sequence: RIGFINVGAPAGGMNAAVRAGVAYCLSRGHEPMAIYNGFAGFARHHADNPGAVRPFNWLEVDGWASKGGSEIGTNRELPGESGMETIANLIEQYKFDALFLIGGFEAFHAVSQLRKARDQYPSLCIPMTLLPATISNNVPGTEYSLGSDTCLNELVEYCDKIKQSASATRRRVFVIETQGGRSGYVATLGGLGVGASAVYTPEEGVSLDMLAADVRHLKNVFAHDQGQSRAGRLILINEKASKVYNAKLIADILREESHGRFESREGIPGHMQQGGVPSPMDRCRAVRLAIRCIQH | ||||||
Region | 461-848 | C-terminal regulatory PFK domain 2 | ||||
Sequence: RIGFINVGAPAGGMNAAVRAGVAYCLSRGHEPMAIYNGFAGFARHHADNPGAVRPFNWLEVDGWASKGGSEIGTNRELPGESGMETIANLIEQYKFDALFLIGGFEAFHAVSQLRKARDQYPSLCIPMTLLPATISNNVPGTEYSLGSDTCLNELVEYCDKIKQSASATRRRVFVIETQGGRSGYVATLGGLGVGASAVYTPEEGVSLDMLAADVRHLKNVFAHDQGQSRAGRLILINEKASKVYNAKLIADILREESHGRFESREGIPGHMQQGGVPSPMDRCRAVRLAIRCIQHLEQFGRNVHNRVKVDPMSTTVIGIKGASVVFTPVKQVEEEETDWPNRRPKAAYWLGMKEIVDILGGRPKYELPESDLTGIKAKDVKRGIVPP |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length848
- Mass (Da)93,016
- Last updated2008-05-20 v1
- ChecksumECE40892D2B8A31A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU633899 EMBL· GenBank· DDBJ | CAP67598.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FO904936 EMBL· GenBank· DDBJ | CDP23859.1 EMBL· GenBank· DDBJ | Genomic DNA |