T1FP07 · T1FP07_HELRO
- ProteinATP-dependent 6-phosphofructokinase
- Gene20210554
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids799 (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
- beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + 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 | 44 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 107-108 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 137-140 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 138 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 183-185 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 185 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 220 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 227-229 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 283 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 311 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 317-320 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 491 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 549-553 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 587 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 594-596 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 650 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 676 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 682-685 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 757 | 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 > Spiralia > Lophotrochozoa > Annelida > Clitellata > Hirudinea > Rhynchobdellida > Glossiphoniidae > Helobdella
Accessions
- Primary accessionT1FP07
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-409 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MDDSAALGKIQKSQSICVTAGTEGKKIEKDCYSGCVIGVFTSGGDSQGMNAATRAIVRMGIYVGCKVYLIKEGYQGMVDGGSNIVLADWKSVSNIIQSGGTIIGSARCADFRERPGRLQAAYNLLERGITNLVCIGGDGSLTGANLFRIEWSSLLEELVKTGRITSQKAQECAHLNVVGLVGSIDNDFCGTDMTIGTDSALHRIIEAIDNINTTASSHQRCFVMEVMGRHCGYLALVAALASEADWVFIPESPPEKGWEDKLCEKLAQERSLGQRLNIIIVSEGAIDEEGRPITADQIKDLISKRLKYDTRVTILGHVQRGGNPSAFDRLLGCRMGAEAVLALMEATPFTPACVISLNGNQIVRVPLMECVARTKEVQAAMDKKEFQKAVELRGRDFVANLESFRTLAR | ||||||
Domain | 37-342 | Phosphofructokinase | ||||
Sequence: IGVFTSGGDSQGMNAATRAIVRMGIYVGCKVYLIKEGYQGMVDGGSNIVLADWKSVSNIIQSGGTIIGSARCADFRERPGRLQAAYNLLERGITNLVCIGGDGSLTGANLFRIEWSSLLEELVKTGRITSQKAQECAHLNVVGLVGSIDNDFCGTDMTIGTDSALHRIIEAIDNINTTASSHQRCFVMEVMGRHCGYLALVAALASEADWVFIPESPPEKGWEDKLCEKLAQERSLGQRLNIIIVSEGAIDEEGRPITADQIKDLISKRLKYDTRVTILGHVQRGGNPSAFDRLLGCRMGAEAVLA | ||||||
Region | 422-799 | C-terminal regulatory PFK domain 2 | ||||
Sequence: NLAVVFVGAPACGMNAAVRSFVRIGITKGFRILGIKNGFEGLVNNEVVSLSWTDVHGWSGSGGARLKTNRTTPSKVGLDRVADKLRHFSIHGLLIIGGFEAFESILQLTEARSAYREFCIPMSMVPATISNNIPGTDFSLGSDTSLNAIVEIADRIKQSASGTRNRVFVLETMGGHCGYLATLSALASGADAAYIFEEPFNITDLQGDVNHLASKIRGGVKRGMVMRNEKANENYTSDFITRLYQEEGRNIFQCRLNVLGHMQQGGQPSPFDRNMGTKMAAKCAELLAKQVEENKTPEGSVFTNSSDTATLLGLQKKRSLFTPVLELKEKTDFQHRISKEVWWCKLRPLLRILAMHNSIYEVEGQENDGFDDLDKLYL | ||||||
Domain | 423-708 | Phosphofructokinase | ||||
Sequence: LAVVFVGAPACGMNAAVRSFVRIGITKGFRILGIKNGFEGLVNNEVVSLSWTDVHGWSGSGGARLKTNRTTPSKVGLDRVADKLRHFSIHGLLIIGGFEAFESILQLTEARSAYREFCIPMSMVPATISNNIPGTDFSLGSDTSLNAIVEIADRIKQSASGTRNRVFVLETMGGHCGYLATLSALASGADAAYIFEEPFNITDLQGDVNHLASKIRGGVKRGMVMRNEKANENYTSDFITRLYQEEGRNIFQCRLNVLGHMQQGGQPSPFDRNMGTKMAAKCAELL |
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
- Length799
- Mass (Da)87,224
- Last updated2013-10-16 v1
- Checksum00EB1757B6F66F7B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AMQM01001367 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KB097495 EMBL· GenBank· DDBJ | ESN96243.1 EMBL· GenBank· DDBJ | Genomic DNA |