A0A0N4Z0F0 · A0A0N4Z0F0_PARTI
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids820 (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 | 60 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 123-124 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 153-156 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 154 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 199-201 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 201 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 236 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 243-245 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 299 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 327 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 333-336 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 513 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: K | ||||||
Binding site | 571-575 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 609 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 616-618 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 672 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 698 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 704-707 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HAQQ | ||||||
Binding site | 780 | 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
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Tylenchina > Panagrolaimomorpha > Strongyloidoidea > Strongyloididae > Parastrongyloides
Accessions
- Primary accessionA0A0N4Z0F0
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-425 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MENSNNGSEDELGDLPKVCIQGKKSVYRKDSIIPVMGKEGHRIERNIYEGSNLAVFTSGGDAPGMNAAVRSVVRMGIYLGCKVYFIYEGYQGMVDGDEYIKEATWNSVSDIIQKGGTIIGSARCKDFRTKEGRLKACLNLIKKDITNLVCIGGDGSLTGANTFRIEWPELVKELVILEKITLDEARKNSNIQIVGLVGSIDNDFCGTDMTIGTDTALQRIIEATDSVVSTAQSHQRAFVIEVMGRHCGYLALVASLASEADFCFIPEWPPTVNWREVLCKKLAQMRSDGQRLNIIIVAEGAIDLAGEPITADMIKKVVQENLKYDIRTTVLGHVQRGGNPSAFDRLLGTRMGAEAVLALMEMTPESHPSVISIDGNQIVRVPLMKCVERTQAVQKAMDNKDFSRAVELRGRSFQRNLETYRLLTK | ||||||
Domain | 53-358 | Phosphofructokinase | ||||
Sequence: LAVFTSGGDAPGMNAAVRSVVRMGIYLGCKVYFIYEGYQGMVDGDEYIKEATWNSVSDIIQKGGTIIGSARCKDFRTKEGRLKACLNLIKKDITNLVCIGGDGSLTGANTFRIEWPELVKELVILEKITLDEARKNSNIQIVGLVGSIDNDFCGTDMTIGTDTALQRIIEATDSVVSTAQSHQRAFVIEVMGRHCGYLALVASLASEADFCFIPEWPPTVNWREVLCKKLAQMRSDGQRLNIIIVAEGAIDLAGEPITADMIKKVVQENLKYDIRTTVLGHVQRGGNPSAFDRLLGTRMGAEAVLA | ||||||
Domain | 444-729 | Phosphofructokinase | ||||
Sequence: NIAVMNIGAPAGGMNAAVRSCVRMGLYNHCKVFAVYDSFEGLAKGDFKEMQWSDVSGWVMHGGSFLGTQKQLPNEHNLPRINEQLEKYNIHSLIMIGGFEAYNSAIILHESRNKYSNLRIPICVIPCTISNNVPGTSFSLGSDTSVNQICEFIDKIKQSATGTKRRVFLIETMGGYCGYLATVTALASGADNAYIYEEKFDIDDIKDDCEVIKHKMESGIQRYLIVRNEKANKNYTTEFIMHLFNEEGKGVFSTRVNVLGHAQQGGNSSVFDRNMGTKLAAKAIDH | ||||||
Region | 444-820 | C-terminal regulatory PFK domain 2 | ||||
Sequence: NIAVMNIGAPAGGMNAAVRSCVRMGLYNHCKVFAVYDSFEGLAKGDFKEMQWSDVSGWVMHGGSFLGTQKQLPNEHNLPRINEQLEKYNIHSLIMIGGFEAYNSAIILHESRNKYSNLRIPICVIPCTISNNVPGTSFSLGSDTSVNQICEFIDKIKQSATGTKRRVFLIETMGGYCGYLATVTALASGADNAYIYEEKFDIDDIKDDCEVIKHKMESGIQRYLIVRNEKANKNYTTEFIMHLFNEEGKGVFSTRVNVLGHAQQGGNSSVFDRNMGTKLAAKAIDHVLEQMKETINTATNEKNAVHEDTCTLLGLRGRKYEFTSVINLIEETNFDVRLPKNQWWLKLRPLLRILAKHNSSYVVEAEEDSDTEDSKKL | ||||||
Coiled coil | 724-751 | |||||
Sequence: AKAIDHVLEQMKETINTATNEKNAVHED |
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
Family and domain databases
Sequence
- Sequence statusComplete
- Length820
- Mass (Da)91,341
- Last updated2015-12-09 v1
- Checksum2AA97ADE9946C1E8