A0A6G0UH46 · A0A6G0UH46_9BILA
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids813 (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 | 57 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 120-121 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 150-153 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 151 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 196-198 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 198 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 233 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 240-242 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 296 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 324 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 330-333 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 508 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: K | ||||||
Binding site | 565-569 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 603 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 610-612 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 666 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 692 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 698-701 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HAQQ | ||||||
Binding site | 774 | 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Tylenchina > Panagrolaimomorpha > Panagrolaimoidea > Panagrolaimidae > Halicephalobus
Accessions
- Primary accessionA0A6G0UH46
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-422 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MADPPKEDELGPLREYPENARKVVRTDSIVPTVGREGSDIKRLIYKGRSMAVFTSGGDSQGMNAAIRSVVRMGLYVGCKVYLINEGYQGMVDGGENIWEADWNVVSDIIQKGGTIIGSARCKAFREREGRLKAAQNLLERSITNIVCIGGDGSLTGANTFRQEWPSLLQELVESGKITKEKAEQCSNIQIVGLVGSIDNDFCGTDMTIGTDTALQRIIDAIDAVVATAQSHQRAFVVEVMGRHCGYLGLVAALASEADFCFIPEWPPPTNWPEILCEKLTHTRSTGLRLNIIVVAEGAIDREGKPITSDMVKDVINKTLNYDTRVTVLGHVQRGGNPSAFDRLLGSRMGAEAVLALMEMTPESEPCVISIDGNQMVRVPLMECVHRTQAVQKAMDGKNWDIAVKLRGRSFQRNLDTYRLLTK | ||||||
Domain | 50-355 | Phosphofructokinase | ||||
Sequence: MAVFTSGGDSQGMNAAIRSVVRMGLYVGCKVYLINEGYQGMVDGGENIWEADWNVVSDIIQKGGTIIGSARCKAFREREGRLKAAQNLLERSITNIVCIGGDGSLTGANTFRQEWPSLLQELVESGKITKEKAEQCSNIQIVGLVGSIDNDFCGTDMTIGTDTALQRIIDAIDAVVATAQSHQRAFVVEVMGRHCGYLGLVAALASEADFCFIPEWPPPTNWPEILCEKLTHTRSTGLRLNIIVVAEGAIDREGKPITSDMVKDVINKTLNYDTRVTVLGHVQRGGNPSAFDRLLGSRMGAEAVLA | ||||||
Domain | 439-723 | Phosphofructokinase | ||||
Sequence: NVAVMNVGAPAGGMNAAVRSFVRMGLYHHCTVYGIHNSFEGLAAGEVKKMEWGDVANWVMHGGSKLGTQKQLPLKQLSKIAEMLKHFKIHALLIIGGFEAYNSVLELSRHRTKYEAFRIPMCVIPCTISNNIPGTSHSLGCDTAVNEICHMIDKIKQSATGTKRRVFIIETMGGYCGYLATISALASGADNAYIFEENFTVDDIKEDVSVILSKMQKGVQRYLIVRCENANRHYTTTFVQQLFQEEGKGGFSTRINVLGHAQQGGNPTPFDRNMGTKLAARALEY | ||||||
Region | 439-813 | C-terminal regulatory PFK domain 2 | ||||
Sequence: NVAVMNVGAPAGGMNAAVRSFVRMGLYHHCTVYGIHNSFEGLAAGEVKKMEWGDVANWVMHGGSKLGTQKQLPLKQLSKIAEMLKHFKIHALLIIGGFEAYNSVLELSRHRTKYEAFRIPMCVIPCTISNNIPGTSHSLGCDTAVNEICHMIDKIKQSATGTKRRVFIIETMGGYCGYLATISALASGADNAYIFEENFTVDDIKEDVSVILSKMQKGVQRYLIVRCENANRHYTTTFVQQLFQEEGKGGFSTRINVLGHAQQGGNPTPFDRNMGTKLAARALEYLVTQAKEFVDPVNGVLGATETDTATLLGLRGRRVVFTPVEELAEETDFEHRLPLDQWWLKLRPLLRILAKHNSTYYTEAMDVPEVVGEMD |
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
- Length813
- Mass (Da)89,770
- Last updated2020-08-12 v1
- Checksum2078D4CB6253C7E3
Keywords
- Technical term