A0A0D2H344 · A0A0D2H344_9EURO
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids811 (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 | 26 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 89-90 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 119-122 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 120 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 165-167 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 167 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 202 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 209-211 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 265 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 293 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 299-302 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HIQR | ||||||
Binding site | 484 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 541-545 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 579 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 586-588 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: QGG | ||||||
Binding site | 646 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 672 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 678-681 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HYQQ | ||||||
Binding site | 754 | 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Herpotrichiellaceae > Fonsecaea
Accessions
- Primary accessionA0A0D2H344
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-391 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MAFGRNTTPSASSVGPRRVGIMTSGGDSQGMNGVVRAVVRMSIHMGCEAYAILEGYEGLVRGGDAIRRMHWEDVRGYLSLGGTLIGTRRCREFFERAGRVKAAKNLILKGISGLVVCGGDGSLTGADRFRAEWPSLLDELVQTRQLTPSQVEPYRHLNVCGLVGSIDNDFSGTDATIGCYSSLQRICEMVDAVFDTAASHARGFVIEVMGRHCGWLALMASIATGADYVFIPEKPPGADWADEMCEIVTSHRNLGKRRTIIIIAEGATDIELNKITADQVVETLSEKLDLDTRKTVLGHIQRGGLASYYDRWLATLQGVEAVKALLEATPDTPSPVITVRENKILRSDLQECVRLTKSAAAAVKEKDWTRAMKLRDVEFKDYFDSYKLTTS | ||||||
Domain | 18-325 | Phosphofructokinase | ||||
Sequence: RVGIMTSGGDSQGMNGVVRAVVRMSIHMGCEAYAILEGYEGLVRGGDAIRRMHWEDVRGYLSLGGTLIGTRRCREFFERAGRVKAAKNLILKGISGLVVCGGDGSLTGADRFRAEWPSLLDELVQTRQLTPSQVEPYRHLNVCGLVGSIDNDFSGTDATIGCYSSLQRICEMVDAVFDTAASHARGFVIEVMGRHCGWLALMASIATGADYVFIPEKPPGADWADEMCEIVTSHRNLGKRRTIIIIAEGATDIELNKITADQVVETLSEKLDLDTRKTVLGHIQRGGLASYYDRWLATLQGVEAVKAL | ||||||
Domain | 408-704 | Phosphofructokinase | ||||
Sequence: RIAIIHVGAPAAGMNPATRAAVAYCLSRGHTPLAIYNGFPGLQRHHDDKPVGSVRELKWIDVDDWVNQGGSELGTNRSLPSEDLAQTAYCFDLYEFDALFLIGGFEAFTSASQIRNNRDKYPSFRIPLLVLPATISNNVPGTEYSLGSDTCLNTLVGFCDVIRQSASASRRRVFVVDTQGGKSGYLATMTGLAVGASAVYTPEAGINMRMLLRDIDFIREDFQNDRGAARAGKIILRNERASQTYTAQMIADVINVEAQGRFDARAAVPAHYQQGMKPSPIDRIRSFKLAIKCMQFL | ||||||
Region | 408-811 | C-terminal regulatory PFK domain 2 | ||||
Sequence: RIAIIHVGAPAAGMNPATRAAVAYCLSRGHTPLAIYNGFPGLQRHHDDKPVGSVRELKWIDVDDWVNQGGSELGTNRSLPSEDLAQTAYCFDLYEFDALFLIGGFEAFTSASQIRNNRDKYPSFRIPLLVLPATISNNVPGTEYSLGSDTCLNTLVGFCDVIRQSASASRRRVFVVDTQGGKSGYLATMTGLAVGASAVYTPEAGINMRMLLRDIDFIREDFQNDRGAARAGKIILRNERASQTYTAQMIADVINVEAQGRFDARAAVPAHYQQGMKPSPIDRIRSFKLAIKCMQFLEENFAGKDPDEINANPLNAAIIGIQGSEAVFSPMGSDLGLEATETDWSSRRQLNEYWRPVEAVIDILSGRPTDLDGTADYATLPETPGEAFVSVAPSRAITPRPQIL |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length811
- Mass (Da)88,866
- Last updated2015-04-29 v1
- ChecksumAEE632776F917D80
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KN846969 EMBL· GenBank· DDBJ | KIW85285.1 EMBL· GenBank· DDBJ | Genomic DNA |