A0A8M9PRJ5 · A0A8M9PRJ5_DANRE
- ProteinATP-dependent 6-phosphofructokinase
- Genepfkpb
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids787 (go to sequence)
- Protein existenceEvidence at protein 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 | 25 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 88-89 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 118-121 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 119 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 164-166 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 166 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 201 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 208-210 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 264 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 292 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 298-301 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 477 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 534-538 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TVSNN | ||||||
Binding site | 572 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 579-581 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 635 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 661 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 667-670 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 741 | 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 | membrane | |
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 > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionA0A8M9PRJ5
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Homo- and heterotetramers.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-390 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MPDTKKYIENLSGAGKCIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIHEGYQGMVDGGDNIKEASWESVSSMLQVGGTVIGSARCKDFRTHEGRLCAALNLVQRGITNLCVIGGDGSLTGANLFREEWSGLLDELVQSGQISEDAAQTHSALHIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVLIPERPPKDGWEEQMCQKLSENRADKKRLNIIIVAEGAIDQNNKPITTDHIKDLVVSRLGFDTRVTILGHVQRGGTPSAFDRILASRMGVEAVLALLEASPGTPACVVSLCGNQAVRVPLMECVQMTQEVQKAMDEKRFEEAVKLRGRSFENNLNTYKLLSH | ||||||
Domain | 18-323 | Phosphofructokinase | ||||
Sequence: IGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIHEGYQGMVDGGDNIKEASWESVSSMLQVGGTVIGSARCKDFRTHEGRLCAALNLVQRGITNLCVIGGDGSLTGANLFREEWSGLLDELVQSGQISEDAAQTHSALHIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVLIPERPPKDGWEEQMCQKLSENRADKKRLNIIIVAEGAIDQNNKPITTDHIKDLVVSRLGFDTRVTILGHVQRGGTPSAFDRILASRMGVEAVLA | ||||||
Domain | 408-693 | Phosphofructokinase | ||||
Sequence: NVAVLNVGAPAAGMNAAVRSAVRVGITEGHTMFAVSDGFEGFYKGQIKEIKWGDVGGWTGQGGSLLGTKRTLPAKHVDKIAEQMRIHNINALLVIGGFEAYLGLMELQAARSKHAELCVPMVMVPATVSNNIPGSDLSIGADTAINAITDTCDRIKQSASGTKRRVFIIETMGGYCGYLATVGGLAAGADAAYIYEEPFDIRDLQSNVEHLTEKMKTSIQRGLVLRNENSNENYTTDFIYQLYSEEGKGVFDCRKNVLGHMQQGGAPSPFDRNFGTKIAAKAMQWI | ||||||
Region | 408-787 | C-terminal regulatory PFK domain 2 | ||||
Sequence: NVAVLNVGAPAAGMNAAVRSAVRVGITEGHTMFAVSDGFEGFYKGQIKEIKWGDVGGWTGQGGSLLGTKRTLPAKHVDKIAEQMRIHNINALLVIGGFEAYLGLMELQAARSKHAELCVPMVMVPATVSNNIPGSDLSIGADTAINAITDTCDRIKQSASGTKRRVFIIETMGGYCGYLATVGGLAAGADAAYIYEEPFDIRDLQSNVEHLTEKMKTSIQRGLVLRNENSNENYTTDFIYQLYSEEGKGVFDCRKNVLGHMQQGGAPSPFDRNFGTKIAAKAMQWISKKLKEFYRDGRVFANTEDSACLLGMRRRALLFQPVVQLKDETDFVHRIPKEQWWLRLRPLMKILAKYKTSYDVSDSGQLEHIVRLRAKDSSAI |
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
- Length787
- Mass (Da)86,034
- Last updated2022-08-03 v1
- Checksum65D6298AEAD98FE0
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8M9PAY2 | A0A8M9PAY2_DANRE | pfkpb | 789 | ||
A0A8M9PJ31 | A0A8M9PJ31_DANRE | pfkpb | 784 | ||
X1WDM7 | X1WDM7_DANRE | pfkpb | 782 | ||
A0A8M9PQ30 | A0A8M9PQ30_DANRE | pfkpb | 784 | ||
A0A8M9PNB0 | A0A8M9PNB0_DANRE | pfkpb | 787 | ||
A0A8M9P1U9 | A0A8M9P1U9_DANRE | pfkpb | 782 | ||
A0A8M9PAZ4 | A0A8M9PAZ4_DANRE | pfkpb | 738 | ||
A0A8M2BAP4 | A0A8M2BAP4_DANRE | pfkpb | 782 | ||
A0A8M9PGE2 | A0A8M9PGE2_DANRE | pfkpb | 789 | ||
A0A8M9PGF5 | A0A8M9PGF5_DANRE | pfkpb | 782 | ||
A0A8M6YU07 | A0A8M6YU07_DANRE | pfkpb | 731 |
Keywords
- Technical term