A2RV78 · A2RV78_XENLA
- ProteinATP-dependent 6-phosphofructokinase
- Genepfkp.S
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids786 (go to sequence)
- Protein existenceEvidence at transcript level
- 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: HVQR | ||||||
Binding site | 473 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 530-534 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TVSNN | ||||||
Binding site | 568 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 575-577 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 631 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 657 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 663-666 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 739 | 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 | cytoplasm | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
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 > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionA2RV78
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Keywords
- PTM
Expression
Gene expression databases
Interaction
Subunit
Homo- and heterotetramers.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-391 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MAQPDKRLFENLSGKGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVQAKVYFIYEGYQGMVDGGDNIEEVSWESVSSILQVGGTVIGSARCKSFRTREGRLQAANNLVQRGITNLCVIGGDGSLTGANLFREEWSGLLDELVQNGKIEAEATKQYAHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFIPEYPPEEGWEDTMCNKLSENRARKKRLNIIIVSEGAIDCHNKPITSDLVKDLVMKRLGFDTRVTILGHVQRGGTPSAFDRILASRMGVDCVLALLEATPETPACVVSLCGNQAVRLPLMECVQMTQEVQKAMDERRFDDAVRLRGRSFENNLNTYKLLSH | ||||||
Domain | 19-324 | Phosphofructokinase | ||||
Sequence: IGVLTSGGDAQGMNAAVRAVVRMGIYVQAKVYFIYEGYQGMVDGGDNIEEVSWESVSSILQVGGTVIGSARCKSFRTREGRLQAANNLVQRGITNLCVIGGDGSLTGANLFREEWSGLLDELVQNGKIEAEATKQYAHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFIPEYPPEEGWEDTMCNKLSENRARKKRLNIIIVSEGAIDCHNKPITSDLVKDLVMKRLGFDTRVTILGHVQRGGTPSAFDRILASRMGVDCVLA | ||||||
Domain | 404-689 | Phosphofructokinase | ||||
Sequence: NVAVLNVGAPAAGMNAAVRSAVRVGITEGHKMFAVNDGFEGFAKGQIKEIKWGDVGGYTGQGGSLLGTKRTLPAKYFDQIAEQLRTHKINALLVIGGFEAYLGLLEMVEGRGKYDEFCIPMVMVPATVSNNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEESFDIRELQANVEHLTEKMKTSIQRGLVLRNENSNENYTTDFIYQLYSEEGRGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISAKAVQWI | ||||||
Region | 404-786 | C-terminal regulatory PFK domain 2 | ||||
Sequence: NVAVLNVGAPAAGMNAAVRSAVRVGITEGHKMFAVNDGFEGFAKGQIKEIKWGDVGGYTGQGGSLLGTKRTLPAKYFDQIAEQLRTHKINALLVIGGFEAYLGLLEMVEGRGKYDEFCIPMVMVPATVSNNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEESFDIRELQANVEHLTEKMKTSIQRGLVLRNENSNENYTTDFIYQLYSEEGRGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISAKAVQWISKKLVETYRKDEGRVFANTDDSVCLLGMRRRNLLFQPVTQLKDETDFKHRIPKEQWWLKMRPLMKILAKYKTSYDISDAGKLEHVNMCRRTDEAVAI |
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
- Length786
- Mass (Da)86,641
- Last updated2007-03-06 v1
- ChecksumC4A3B826DDEE3965
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8J1L0B3 | A0A8J1L0B3_XENLA | pfkp.S | 835 | ||
A0A8J0VII5 | A0A8J0VII5_XENLA | pfkp.S | 786 | ||
A0A8J0VKV2 | A0A8J0VKV2_XENLA | pfkp.S | 784 | ||
A0A8J0VM01 | A0A8J0VM01_XENLA | pfkp.S | 784 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC133214 EMBL· GenBank· DDBJ | AAI33215.1 EMBL· GenBank· DDBJ | mRNA |