A0A9Q5I2V3 · A0A9Q5I2V3_SANBA
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids826 (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 | 15 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 137-138 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RS | ||||||
Binding site | 167-170 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 168 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 213-215 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 215 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 250 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 257-259 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 314 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 342 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 348-351 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HTQR | ||||||
Binding site | 523 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 580-584 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 618 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 625-627 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: QGG | ||||||
Binding site | 685 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 711 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 792 | 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 | 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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Hymenochaetales > Hymenochaetaceae > Sanghuangporus
Accessions
- Primary accessionA0A9Q5I2V3
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-440 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MSKIKRKIAVLTSGGDSAGMNACVRAVVKYGIIRGCEVYVVREGYEGLVRGNVDAPKRKVAFNDSNNDKHHHGDDSAEDKLINNLRFGDGNLLKEGEGDAIEHPGGRSLKGRYIIRVGWDDVRAWFAEGGTLIGTARSAAFRTKEGRLAAANNLITEGIDSIVVCGGDGSLTGADVFRAEWPSLVNELRQSNTITSEQAERYAHLNIAGTVGSIDNDMSMTDITIGAYTALHRICESIDNINSTAFSHSRAFVVEVMGRHCGWLALMAGVSAGADFIFIPERPPVADPWEDDMCKNIQNHRDIGKRKTIVIVAEGAIDANLNPIRAEYVKDVLTERLGLDTRVTCLGHTQRGGRPCAYDRLLPTMQGVEAVDALLESTPESPSYMIAIHENKISRVPLVEAVAQTRAVAKAISEKDFERAMSYRDPEFREMLDGFVAVSS | ||||||
Domain | 7-56 | Phosphofructokinase | ||||
Sequence: KIAVLTSGGDSAGMNACVRAVVKYGIIRGCEVYVVREGYEGLVRGNVDAP | ||||||
Domain | 113-374 | Phosphofructokinase | ||||
Sequence: YIIRVGWDDVRAWFAEGGTLIGTARSAAFRTKEGRLAAANNLITEGIDSIVVCGGDGSLTGADVFRAEWPSLVNELRQSNTITSEQAERYAHLNIAGTVGSIDNDMSMTDITIGAYTALHRICESIDNINSTAFSHSRAFVVEVMGRHCGWLALMAGVSAGADFIFIPERPPVADPWEDDMCKNIQNHRDIGKRKTIVIVAEGAIDANLNPIRAEYVKDVLTERLGLDTRVTCLGHTQRGGRPCAYDRLLPTMQGVEAVDAL | ||||||
Domain | 454-742 | Phosphofructokinase | ||||
Sequence: RVAIINMGAPAGGMNAATRTATRYCIRRGHKPIAIYNGFRGLLEDNVEDLSWLRVDNWMTRGGSELGTNRTLPDIDLGAVASQFQKHRFDAFFLIGGFEAFRSLQILEEARGLYPAFHIPMVCVPATISNNVPVTDYSLGCDTSLNALVEACDAIKQSASASRNRVFVVETQGGKCGYIATMGALATGAVCYYTPEDGITLDGLRKDVEFLKLRYSLDEKGKAEGRLILRNEASSNVFTTDFIQKMLQEEGGSLFDSRMASLGHTLQGGIPSPMDRARAVRFSLKCMAF | ||||||
Region | 454-826 | C-terminal regulatory PFK domain 2 | ||||
Sequence: RVAIINMGAPAGGMNAATRTATRYCIRRGHKPIAIYNGFRGLLEDNVEDLSWLRVDNWMTRGGSELGTNRTLPDIDLGAVASQFQKHRFDAFFLIGGFEAFRSLQILEEARGLYPAFHIPMVCVPATISNNVPVTDYSLGCDTSLNALVEACDAIKQSASASRNRVFVVETQGGKCGYIATMGALATGAVCYYTPEDGITLDGLRKDVEFLKLRYSLDEKGKAEGRLILRNEASSNVFTTDFIQKMLQEEGGSLFDSRMASLGHTLQGGIPSPMDRARAVRFSLKCMAFLERHHISLLAQPELKRKAPEESAAVITIQRNEVGFTPVKCMLARADVKNRRGNKTWWEEYKPMVSMLGGRTALVEEEVDPKLKK |
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length826
- Mass (Da)90,842
- Last updated2023-09-13 v1
- ChecksumC9ABC0765257C237
Keywords
- Technical term