A0AAI9WZK5 · A0AAI9WZK5_9ASCO
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids959 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 200 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 264-265 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 294-297 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 295 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 340-342 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 342 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 377 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 384-386 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 441 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 469 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 475-478 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 652 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 710-714 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 748 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 755-757 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: QGG | ||||||
Binding site | 841 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: K | ||||||
Binding site | 847-850 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQQ | ||||||
Binding site | 928 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R |
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 > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida
Accessions
- Primary accessionA0AAI9WZK5
Proteomes
Subcellular Location
Interaction
Subunit
Heterooctamer of 4 alpha and 4 beta chains.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-567 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MSSIINGSSTVPLIAGSQELLDDALIFYTNVLDFSEHSKKDNCVFLANRDQVVIELKLDPKKGNSAREVKERRKEILSKLNIVDWRSLDTTFVFKVGNLVDTIEILNSFKYTLQITPNELYPNEAYCVDPLGYIIGFTACNEPLTVVPPLQKANPKTDTSYLPSAMMSTTGSFSKLSESLQLSTNSLKPRRNIAIMTSGGDAPGMNASVRAVVRAAIFRGCKAFAIKEGYEGLVRGGEKYITEMKWQDVRGFLSDGGTNIGTARCMEFKKREGRLKGCRHLIEAGIDALIVCGGDGSLTGADLFRSEWPSLIAELKEQKEISEEQYEKHKHLYICGMVGSIDNDMATTDSTIGCYSALERICRAVDYIDATANSHSRAFVVEVMGRHCGWLALMAGIATSADYILIPEKPASSQDWQDQMTTIVKNHRAKGKRKTIVIVAEGAITLDLTPISSEDVKNVLVDRLGLDTRITTLGHVQRGGTAVAFDRILATVQGVEAVKAVLELEPDTPSPLIAIDENKICRRPLVEAVKITKSVAAAIAEKDFEKAMSLRDSEFKEHLSNFIAMNS | ||||||
Domain | 192-500 | Phosphofructokinase | ||||
Sequence: NIAIMTSGGDAPGMNASVRAVVRAAIFRGCKAFAIKEGYEGLVRGGEKYITEMKWQDVRGFLSDGGTNIGTARCMEFKKREGRLKGCRHLIEAGIDALIVCGGDGSLTGADLFRSEWPSLIAELKEQKEISEEQYEKHKHLYICGMVGSIDNDMATTDSTIGCYSALERICRAVDYIDATANSHSRAFVVEVMGRHCGWLALMAGIATSADYILIPEKPASSQDWQDQMTTIVKNHRAKGKRKTIVIVAEGAITLDLTPISSEDVKNVLVDRLGLDTRITTLGHVQRGGTAVAFDRILATVQGVEAVKA | ||||||
Region | 568-581 | Interdomain linker | ||||
Sequence: ACHDEPTLPLTKRK | ||||||
Region | 582-959 | C-terminal regulatory PFK domain 2 | ||||
Sequence: TIAIINIGAPAGGMNSATYAMATYCMSRGHTPYAIHNGFSGLSRHESVKSINWLDIEGWNSVGGSDIGTNRKTPEETDIGMIAHYFEKYKFDGLIIVGGFEAFISLHQLEKSRPMYPAFRIPMVLIPATISNNIPGTEYSLGADTCLNALMNYCDIIKQSASATRGRAFVIEAQGGNSGYIATYASLVSGAQASYVPEEGIHLTQLQMDIDSLREAFALEKSTTKTGKLIIKSSNASQVLTPQVLADIINAECKGEFDVKTAIPGHVQQGGLPSPIDRTRADRFAIKAVQFIEDHCDLMEPVRYAIDFSQDGKKYTETAAVLCLKGSHLRFSSIRRLYNFETELSKRMPKKVFWSKTRSIADDLVGRNRYKPVEEISH | ||||||
Domain | 583-873 | Phosphofructokinase | ||||
Sequence: IAIINIGAPAGGMNSATYAMATYCMSRGHTPYAIHNGFSGLSRHESVKSINWLDIEGWNSVGGSDIGTNRKTPEETDIGMIAHYFEKYKFDGLIIVGGFEAFISLHQLEKSRPMYPAFRIPMVLIPATISNNIPGTEYSLGADTCLNALMNYCDIIKQSASATRGRAFVIEAQGGNSGYIATYASLVSGAQASYVPEEGIHLTQLQMDIDSLREAFALEKSTTKTGKLIIKSSNASQVLTPQVLADIINAECKGEFDVKTAIPGHVQQGGLPSPIDRTRADRFAIKAVQFI |
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
- Length959
- Mass (Da)105,486
- Last updated2024-07-24 v1
- Checksum6FF568F94A343859