A0A0B4KFI7 · A0A0B4KFI7_DROME
- ProteinATP-dependent 6-phosphofructokinase
- GenePfk
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids922 (go to sequence)
- Protein existenceEvidence at protein level
- 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 | 224-225 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 254-257 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 255 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 300-302 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 302 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 337 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 344-346 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 400 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 428 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 434-437 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 614 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 671-675 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 709 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 716-718 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 772 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 798 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 804-807 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 879 | 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 | cytoplasm | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionA0A0B4KFI7
Proteomes
Organism-specific databases
Subcellular Location
Expression
Gene expression databases
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-526 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MHSIKFRVFTKLKPICSIVWRFLEINGRIPICRHFHGPTTFRLEISNKTPPIRQKLTFPNIGIQCTRSHHLCCPRDISGNTLLSVKFNCKRHCIKLRSDSGDQKNDSPGEKNIQKDKSAQRCGKPINNLHNGFLNAVNYSEKNAVKKKKSAPKRKCGKSVDELRKCLRTMQDVIDFVHPVKPFVYFIREGYQGMVDGGDCIQEANWASVSSIIHRGGTIIGSARCQDFRERQGRLKAANNLIQRGITNLVVIGGDGSLTGANLFRQEWSSLLDELVKNKTITTEQQEKFNVLHIVGLVGSIDNDFCGTDMTIGTDTALHRIIEAIDAISSTAYSHQRTFIMEVMGRHCGYLSVVAGIISEADYVFLPESPPQADWPDRLVLKLEQERSAGQRLNIVIVAEGAMDREGHPITAEDVKKVIDERLKHDARITVLGHVQRGGNPSAFDRILACRMGAEATLALMEATKDSVPVVISLDGNQAVRVPLMECVERTQAVAKAMAEKRWADAVKLRGRSFERNLETYKMLTR | ||||||
Compositional bias | 99-118 | Basic and acidic residues | ||||
Sequence: DSGDQKNDSPGEKNIQKDKS | ||||||
Region | 99-121 | Disordered | ||||
Sequence: DSGDQKNDSPGEKNIQKDKSAQR | ||||||
Domain | 184-458 | Phosphofructokinase | ||||
Sequence: VYFIREGYQGMVDGGDCIQEANWASVSSIIHRGGTIIGSARCQDFRERQGRLKAANNLIQRGITNLVVIGGDGSLTGANLFRQEWSSLLDELVKNKTITTEQQEKFNVLHIVGLVGSIDNDFCGTDMTIGTDTALHRIIEAIDAISSTAYSHQRTFIMEVMGRHCGYLSVVAGIISEADYVFLPESPPQADWPDRLVLKLEQERSAGQRLNIVIVAEGAMDREGHPITAEDVKKVIDERLKHDARITVLGHVQRGGNPSAFDRILACRMGAEATL | ||||||
Domain | 545-830 | Phosphofructokinase | ||||
Sequence: RLAVMHIGAPACGMNAAVRSFVRNAIYRGDVVYGINDGVEGLIAGNVRELGWSDVSGWVGQGGAYLGTKRTLPEGKFKEIAARLKEFKIQGLLIIGGFESYHAAGQIADQRDNYPQFCIPIVVIPSTISNNVPGTEFSLGCDTGLNEITEICDRIRQSAQGTKRRVFVIETMGGYCGYLATLAGLAGGADAAYIYEEKFSIKDLQQDVYHMASKMAEGVSRGLILRNEKASENYSTDFIYRLYSEEGKGLFTCRMNILGHMQQGGSPTPFDRNMGTKMAAKCVDWL | ||||||
Region | 545-922 | C-terminal regulatory PFK domain 2 | ||||
Sequence: RLAVMHIGAPACGMNAAVRSFVRNAIYRGDVVYGINDGVEGLIAGNVRELGWSDVSGWVGQGGAYLGTKRTLPEGKFKEIAARLKEFKIQGLLIIGGFESYHAAGQIADQRDNYPQFCIPIVVIPSTISNNVPGTEFSLGCDTGLNEITEICDRIRQSAQGTKRRVFVIETMGGYCGYLATLAGLAGGADAAYIYEEKFSIKDLQQDVYHMASKMAEGVSRGLILRNEKASENYSTDFIYRLYSEEGKGLFTCRMNILGHMQQGGSPTPFDRNMGTKMAAKCVDWLAAQIKANIDANGVVNCKSPDTATLLGIVSRQYRFSPLVDLIAETNFDQRIPKKQWWLRLRPLLRILAKHDSAYEEEGMYITVEEECDTDAVA |
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
- Length922
- Mass (Da)102,483
- Last updated2015-04-01 v1
- ChecksumD10E63DC1CC0263B
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P52034 | PFKA_DROME | Pfk | 788 | ||
A0A0B4K7L1 | A0A0B4K7L1_DROME | Pfk | 950 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 99-118 | Basic and acidic residues | ||||
Sequence: DSGDQKNDSPGEKNIQKDKS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE013599 EMBL· GenBank· DDBJ | AGB93380.1 EMBL· GenBank· DDBJ | Genomic DNA |