A0A1D1VWQ7 · A0A1D1VWQ7_RAMVA
- ProteinATP-dependent 6-phosphofructokinase
- GeneRvY_15952-1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids819 (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 | 67 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 130-131 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 160-163 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 161 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 206-208 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 208 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 243 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 250-252 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 306 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 334 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 340-343 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 516 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 573-577 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 611 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 618-620 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 674 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 700 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 706-709 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQQ | ||||||
Binding site | 775 | 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
- EC number
- Short namesATP-PFK ; Phosphofructokinase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Tardigrada > Eutardigrada > Parachela > Hypsibioidea > Ramazzottiidae > Ramazzottius
Accessions
- Primary accessionA0A1D1VWQ7
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-432 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MATGEDMEAQEMRKMKSLERFERRESVTTDPAPKIVALRGGIESDALRLMKPSTWLGKAVGVYCSGGDSQGMNAAVRGVVRMALYVGAKVFFIHEGYVGMVEGGKLIQEATWESVSGIIQKGGTIIGSARCAEFRQRAGRLNAAYNLVSRGICNIVCIGGDGSLTGANLFRQEWQSLLQELVDNARITPEQQEKYNFLNIVGLVGSIDNDFCGTDMTIGTDSALHRIVECIDAITTTAQSHQRTFVLEVMGRHCGYLALVGALACEADWVFIPEWPPEENWPESMCKKLAQEREMGHRLNIVIVSEGAIDRTGKPITSEQVKNVIVDRLKQDCRITVLGHVQRGGNASAFDRVLGTRMGAEAVFALMDATPETEACVISIDGNQAVRTNLMQCVERTQMVAKAMADKNWDLAVKLRGRSFVRNLTTYKMLTK | ||||||
Domain | 60-365 | Phosphofructokinase | ||||
Sequence: VGVYCSGGDSQGMNAAVRGVVRMALYVGAKVFFIHEGYVGMVEGGKLIQEATWESVSGIIQKGGTIIGSARCAEFRQRAGRLNAAYNLVSRGICNIVCIGGDGSLTGANLFRQEWQSLLQELVDNARITPEQQEKYNFLNIVGLVGSIDNDFCGTDMTIGTDSALHRIVECIDAITTTAQSHQRTFVLEVMGRHCGYLALVGALACEADWVFIPEWPPEENWPESMCKKLAQEREMGHRLNIVIVSEGAIDRTGKPITSEQVKNVIVDRLKQDCRITVLGHVQRGGNASAFDRVLGTRMGAEAVFA | ||||||
Region | 433-446 | Interdomain linker | ||||
Sequence: LKAPEKPGAKDKQR | ||||||
Region | 447-819 | C-terminal regulatory PFK domain 2 | ||||
Sequence: NLAVMCIGAPCGGINAATRSFVRNSQYHGYRTFAVYDGIEGLAAGSIKELTWMDVSGWNGEGGALLGIKRTLAGDYLPACAESLKKFEIEGLVIIGGFEAYHSALQFAEGRKNYPDLRIPIIVVPATISNNVPGTDFCLGADTAINEICEICDRLKQSAIGTRRRVFVIETMGGYCGYLATMAGIAAGADAAYIFEEQVSIDDLRNDVRHLTAKMATNVQRGLIIRNEFAHANYSLDFVRRMYAEEGKDIFSCREAVLGHVQQGGRPTPFDRNLGTKLAARAIEYMDEMITKGNLGNEPTSCALLGMIKRQVNLTPVQALATQTDFLHRIPRTQWWMILRPLLRIMAKHASVYVSEIEDATDDPDAGTRSVLG | ||||||
Domain | 448-731 | Phosphofructokinase | ||||
Sequence: LAVMCIGAPCGGINAATRSFVRNSQYHGYRTFAVYDGIEGLAAGSIKELTWMDVSGWNGEGGALLGIKRTLAGDYLPACAESLKKFEIEGLVIIGGFEAYHSALQFAEGRKNYPDLRIPIIVVPATISNNVPGTDFCLGADTAINEICEICDRLKQSAIGTRRRVFVIETMGGYCGYLATMAGIAAGADAAYIFEEQVSIDDLRNDVRHLTAKMATNVQRGLIIRNEFAHANYSLDFVRRMYAEEGKDIFSCREAVLGHVQQGGRPTPFDRNLGTKLAARAIEY |
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
- Length819
- Mass (Da)89,872
- Last updated2016-11-30 v1
- Checksum6FEB5866DA21FE35
Keywords
- Technical term