A0A026WQT5 · A0A026WQT5_OOCBI
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids789 (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 | 28 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 91-92 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 121-124 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 122 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 167-169 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 169 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 204 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 211-213 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 267 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 295 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 301-304 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 478 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 536-540 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 574 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 581-583 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 637 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 663 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 669-672 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 744 | 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
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Formicoidea > Formicidae > Dorylinae > Ooceraea
Accessions
- Primary accessionA0A026WQT5
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-393 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MAEETPAQKFIKPGSHKGKGIAVFTSGGDSQGMNAAVRAVVRMGIYLGCRVYFIREGYQGMVDGGKNIEEATWSSVSCIIHRGGTVIGSARCKEFRERAGRRKAAKNLVNLGITNLVVIGGDGSLTGANLFKEEWSELLKELTESGEITAEQSEKYKQLHIVGLVGSIDNDFCGTDMTIGTDSALHRIIESIDAIVSTAYSHQRTFIMEVMGRHCGYLAIVGALAAEADYIFIPECPPPIDWPEKLCRKLEQERLTGQRLNIIIVAEGAVDRNGDPITADKVHKVVVEKLQQDTRVTVLGHVQRGGNPSAFDRVLGCRMGAEAVMALMEATPDTEACVVTLDGNQAVRLPLMECVRRTKAVAEAMAVKNWDLAVQLRGKGFERNLETYKMLTR | ||||||
Domain | 21-326 | Phosphofructokinase | ||||
Sequence: IAVFTSGGDSQGMNAAVRAVVRMGIYLGCRVYFIREGYQGMVDGGKNIEEATWSSVSCIIHRGGTVIGSARCKEFRERAGRRKAAKNLVNLGITNLVVIGGDGSLTGANLFKEEWSELLKELTESGEITAEQSEKYKQLHIVGLVGSIDNDFCGTDMTIGTDSALHRIIESIDAIVSTAYSHQRTFIMEVMGRHCGYLAIVGALAAEADYIFIPECPPPIDWPEKLCRKLEQERLTGQRLNIIIVAEGAVDRNGDPITADKVHKVVVEKLQQDTRVTVLGHVQRGGNPSAFDRVLGCRMGAEAVMA | ||||||
Region | 409-789 | C-terminal regulatory PFK domain 2 | ||||
Sequence: TLAVMHIGSPSCGMNAAVRSFVRNCIYRGDKVYGIGDGVLGLIAGRFKLMDWPSVTGWVAEGGAKLGTKRAPPQEDQLPLIAQKLKEFEIQALLIIGGFEGYQTGLTFFKARDKYEEFRIPIAMIPATISNNVPGTEFSLGCDTALNEISEICDRIRQSAQGTKRRVFIIETMGGFCGYLATVAGLAGGADAAYIYEEKFNIKDLNQDVIAMAAKMSEGVERGLIIRNESANENYNTEFMYRLFSEEGKGLFSCRRNILGHMQQGGSPTPFDRNLGTKMGSKAVEWFSDQLRKCTSPDGKTVTTAADSAVMLGIIRRQYRYTPFTELIEVTDFEHRIPTYQWWMKLRPLLKVLAKHESTYEEEGLYITIEEMDEQKDPPLV | ||||||
Domain | 410-694 | Phosphofructokinase | ||||
Sequence: LAVMHIGSPSCGMNAAVRSFVRNCIYRGDKVYGIGDGVLGLIAGRFKLMDWPSVTGWVAEGGAKLGTKRAPPQEDQLPLIAQKLKEFEIQALLIIGGFEGYQTGLTFFKARDKYEEFRIPIAMIPATISNNVPGTEFSLGCDTALNEISEICDRIRQSAQGTKRRVFIIETMGGFCGYLATVAGLAGGADAAYIYEEKFNIKDLNQDVIAMAAKMSEGVERGLIIRNESANENYNTEFMYRLFSEEGKGLFSCRRNILGHMQQGGSPTPFDRNLGTKMGSKAVEW |
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
- Length789
- Mass (Da)87,181
- Last updated2014-07-09 v1
- Checksum024CA81433B48DBF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KK107128 EMBL· GenBank· DDBJ | EZA58407.1 EMBL· GenBank· DDBJ | Genomic DNA |