K7FNM8 · K7FNM8_PELSI
- ProteinATP-dependent 6-phosphofructokinase
- GenePFKM
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids872 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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 | 117 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 180-181 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 210-213 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 211 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 256-258 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 258 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 293 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 300-302 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 356 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 384 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 390-393 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 562 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 619-623 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TVSNN | ||||||
Binding site | 657 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 664-666 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 720 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 746 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 752-755 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 826 | 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 | apical plasma membrane | |
Cellular Component | nucleus | |
Cellular Component | sperm principal piece | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Molecular Function | fructose binding | |
Molecular Function | fructose-6-phosphate binding | |
Molecular Function | identical protein binding | |
Molecular Function | kinase binding | |
Molecular Function | metal ion binding | |
Biological Process | canonical glycolysis | |
Biological Process | fructose 1,6-bisphosphate metabolic process | |
Biological Process | fructose 6-phosphate metabolic process | |
Biological Process | glucose homeostasis | |
Biological Process | glycogen catabolic process | |
Biological Process | glycolysis from storage polysaccharide through glucose-1-phosphate | |
Biological Process | muscle cell cellular homeostasis | |
Biological Process | positive regulation of insulin secretion | |
Biological Process | positive regulation of transcription by RNA polymerase II |
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 > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Testudinata > Testudines > Cryptodira > Trionychia > Trionychidae > Pelodiscus
Accessions
- Primary accessionK7FNM8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 60-79 | Helical | ||||
Sequence: LFISVSLAFAVFFFFSFFPF |
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-482 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MRFKPFQCKAVPFTSASKRQAWERQLLQQADIMSINTREEGWHFPVMWTSLDLSVIGSKLFISVSLAFAVFFFFSFFPFSQNKKEPPAKKMLQPKEKHEHTHNLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGAKVYFVHEGYQGLVDGGDNIKEATWESVSMMLQLGGTVIGSARCQDFRTREGRLKAARNLVKRGITNLCVIGGDGSLTGADTFRAEWSNLLMELVKTGGITAEETKNSSHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALITALACGADWVFIPESPPEDDWEEHLCRRLTETRGRGSRLNIIIVAEGAINKQGKPITSEDIKNLVVKRLGYDTRVTILGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTTAMNEGRFEDAVKLRGRSFQNNWNVYKLLAH | ||||||
Domain | 110-415 | Phosphofructokinase | ||||
Sequence: IAVLTSGGDAQGMNAAVRAVVRVGIFTGAKVYFVHEGYQGLVDGGDNIKEATWESVSMMLQLGGTVIGSARCQDFRTREGRLKAARNLVKRGITNLCVIGGDGSLTGADTFRAEWSNLLMELVKTGGITAEETKNSSHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALITALACGADWVFIPESPPEDDWEEHLCRRLTETRGRGSRLNIIIVAEGAINKQGKPITSEDIKNLVVKRLGYDTRVTILGHVQRGGTPSAFDRILGSRMGVEAVMA | ||||||
Region | 493-872 | C-terminal regulatory PFK domain 2 | ||||
Sequence: NLAVMNVGAPAAGMNAAVRAAVRIGLIHGHKMLAVHDGFEGLAHGQVEEIVWGGVGGWTGLGGSKLGTKRTLPKKYFEEISATISTFNIHGLIVIGGFEAFTGSLELVEGRSKYEELCIPLCVIPATVSNNVPGSDFSIGADTALNTITMTCDRIKQSAAGTKRRVFIIETMGGFCGYLATMAGLASGADAAYIYEDPFTIRDLQVNVEHLTEKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFESRKNVLGHMQQGGTPTPFDRNFGTKMGAKSVVWLTGKIKECSRHGRIFANTLDSACLLGMRRRSLVFQPLAELENQTDFEHRIPKQQWWLKLRPILKILAKYKIDLDTSEKAHLEHVARKGLPVEANI | ||||||
Domain | 494-777 | Phosphofructokinase | ||||
Sequence: LAVMNVGAPAAGMNAAVRAAVRIGLIHGHKMLAVHDGFEGLAHGQVEEIVWGGVGGWTGLGGSKLGTKRTLPKKYFEEISATISTFNIHGLIVIGGFEAFTGSLELVEGRSKYEELCIPLCVIPATVSNNVPGSDFSIGADTALNTITMTCDRIKQSAAGTKRRVFIIETMGGFCGYLATMAGLASGADAAYIYEDPFTIRDLQVNVEHLTEKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFESRKNVLGHMQQGGTPTPFDRNFGTKMGAKSVVW |
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
- Length872
- Mass (Da)95,785
- Last updated2013-01-09 v1
- Checksum8F88CE74552D5AB8
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
K7FNL7 | K7FNL7_PELSI | PFKM | 782 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AGCU01201673 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AGCU01201674 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AGCU01201675 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |