Q9TZL8 · PFKA1_CAEEL
- ProteinATP-dependent 6-phosphofructokinase 1
- Genepfk-1.1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids814 (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
- ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + 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 | 55 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 118-119 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RS | ||||||
Binding site | 148-151 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 149 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 194-196 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 196 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 231 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 238-240 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 294 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 322 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 328-331 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 505 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: K | ||||||
Binding site | 563-567 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 601 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 608-610 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 664 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 690 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 696-699 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQQ | ||||||
Binding site | 771 | 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 | |
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 1
- EC number
- Short namesATP-PFK 1 ; Phosphofructokinase 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ9TZL8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000429718 | 1-814 | ATP-dependent 6-phosphofructokinase 1 | |||
Sequence: MDADASTITPEELDFIRQRALRRFDSIVPTAGREGTEIASDIFKGRTLAIYTSGGDSQGMNSAVRSITRMAIYCGCKVYLIYEGYEGMIEGGDFIKEATWNTVSDIIQQGGTIIGSARSSEFRTREGRLKAATNLINRGIGRLVCIGGDGSLTGANTFRLEWTDLVQELVKNQRVTAAAAKKIPYIQIVGLVGSIDNDFCGTDMTIGTDSALQRIISSIDAVVATAQSHQRAFVIEVMGRHCGYLALVAALASEADFCFIPEWPAPENWRDVLCDKLSQMRSEGQRLNIIIVAEGAIDRDGKAITAEDVKTAVKEKLKYDTRVTILGHVQRGGAPSAFDRLLGCRMGAEAVFALMEMTEESEPCVISIDGNVMVRVPLLKCVERTQMVQKAMADKDWTTAVMLRGRSFQRNLETYKLLTKMRTVEKDNLSEGHKFNVAVINVGAPAGGMNAAVRSYVRMALYHQCTVYGIEDSFEGLANGSFKQFKWSDVTNWAMNGGSFLGTQKSLPTEKTMPQLAAQLKKHNIQALLLVGGFEAYHSTIILAENREKYPEFCIPMCVIPCTISNNVPGTMVSLGSDTAINEICQMIDKIKQSATGTKRRVFIVETMGGYCGYLATLSALSSGADNAYIFEEPFTVQDLSDDVDVILSKMEVGAKRYLVVRNEWADKNLTTDFVQNLFDSEGKKNFTTRVNVLGHVQQGGSPTPFDRNMGTKLAARALEFLLIQLKENLTADNKVIAKSAHTATLLGLKGRKVVFTPVQDLKKETDFEHRLPSEQWWMALRPLLRVLARHRSTVESSAILESVEEESADSHMF |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-420 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MDADASTITPEELDFIRQRALRRFDSIVPTAGREGTEIASDIFKGRTLAIYTSGGDSQGMNSAVRSITRMAIYCGCKVYLIYEGYEGMIEGGDFIKEATWNTVSDIIQQGGTIIGSARSSEFRTREGRLKAATNLINRGIGRLVCIGGDGSLTGANTFRLEWTDLVQELVKNQRVTAAAAKKIPYIQIVGLVGSIDNDFCGTDMTIGTDSALQRIISSIDAVVATAQSHQRAFVIEVMGRHCGYLALVAALASEADFCFIPEWPAPENWRDVLCDKLSQMRSEGQRLNIIIVAEGAIDRDGKAITAEDVKTAVKEKLKYDTRVTILGHVQRGGAPSAFDRLLGCRMGAEAVFALMEMTEESEPCVISIDGNVMVRVPLLKCVERTQMVQKAMADKDWTTAVMLRGRSFQRNLETYKLLTK | ||||||
Region | 421-435 | Interdomain linker | ||||
Sequence: MRTVEKDNLSEGHKF | ||||||
Region | 436-814 | C-terminal regulatory PFK domain 2 | ||||
Sequence: NVAVINVGAPAGGMNAAVRSYVRMALYHQCTVYGIEDSFEGLANGSFKQFKWSDVTNWAMNGGSFLGTQKSLPTEKTMPQLAAQLKKHNIQALLLVGGFEAYHSTIILAENREKYPEFCIPMCVIPCTISNNVPGTMVSLGSDTAINEICQMIDKIKQSATGTKRRVFIVETMGGYCGYLATLSALSSGADNAYIFEEPFTVQDLSDDVDVILSKMEVGAKRYLVVRNEWADKNLTTDFVQNLFDSEGKKNFTTRVNVLGHVQQGGSPTPFDRNMGTKLAARALEFLLIQLKENLTADNKVIAKSAHTATLLGLKGRKVVFTPVQDLKKETDFEHRLPSEQWWMALRPLLRVLARHRSTVESSAILESVEEESADSHMF |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length814
- Mass (Da)89,734
- Last updated2001-10-01 v2
- ChecksumDA829E8969EDF1CE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FO081433 EMBL· GenBank· DDBJ | CCD71595.1 EMBL· GenBank· DDBJ | Genomic DNA |