Q5R9C1 · F263_PONAB
- Protein6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
- GenePFKFB3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids514 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Catalyzes both the synthesis and degradation of fructose 2,6-bisphosphate.
Catalytic activity
- beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 42-50 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLPARGKTY | ||||||
Binding site | 75 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 99 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 125 | |||||
Sequence: D | ||||||
Binding site | 127 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 133 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 155 | |||||
Sequence: C | ||||||
Binding site | 164-169 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NIMEVK | ||||||
Binding site | 169 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 190 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 194 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 253 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 253 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 254 | Tele-phosphohistidine intermediate | ||||
Sequence: H | ||||||
Binding site | 260 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 260 | Transition state stabilizer | ||||
Sequence: N | ||||||
Binding site | 266 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 323 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 334 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 345-348 | ATP (UniProtKB | ChEBI) | ||||
Sequence: YALR | ||||||
Binding site | 348 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 352 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 363 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Site | 388 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 389 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 389-393 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QAVLR | ||||||
Binding site | 393 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 425 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 6-phosphofructo-2-kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | fructose-2,6-bisphosphate 2-phosphatase activity | |
Biological Process | fructose 2,6-bisphosphate metabolic process | |
Biological Process | fructose metabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended name6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
- Short names6PF-2-K/Fru-2,6-P2ase 3; PFK/FBPase 3
- Alternative names
Including 2 domains:
- Recommended name6-phosphofructo-2-kinase
- EC number
- Recommended nameFructose-2,6-bisphosphatase
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pongo
Accessions
- Primary accessionQ5R9C1
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000345149 | 1-514 | 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 | |||
Sequence: MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQPLLGQACLT | ||||||
Modified residue | 461 | Phosphoserine; by AMPK and PKA | ||||
Sequence: S | ||||||
Modified residue | 463 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 467 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 471 | Phosphothreonine; by PKC | ||||
Sequence: T |
Post-translational modification
Phosphorylation by AMPK stimulates activity.
Keywords
- PTM
Interaction
Subunit
Homodimer. Forms a heterodimer with PFKFB2 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-245 | 6-phosphofructo-2-kinase | ||||
Sequence: MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQ | ||||||
Region | 246-514 | Fructose-2,6-bisphosphatase | ||||
Sequence: PRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQPLLGQACLT | ||||||
Region | 444-475 | Disordered | ||||
Sequence: ERSEDAKKGPNPLMRRNSVTPLASPEPTKKPR |
Sequence similarities
In the C-terminal section; belongs to the phosphoglycerate mutase family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q5R9C1-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length514
- Mass (Da)58,876
- Last updated2008-07-22 v2
- Checksum18FD1D267306853D
Q5R9C1-2
- Name2
Q5R9C1-3
- Name3
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A6D2XVH3 | A0A6D2XVH3_PONAB | PFKFB3 | 526 | ||
A0A2J8VK41 | A0A2J8VK41_PONAB | PFKFB3 | 568 | ||
A0A2J8VK47 | A0A2J8VK47_PONAB | PFKFB3 | 534 | ||
A0A2J8VK48 | A0A2J8VK48_PONAB | PFKFB3 | 455 | ||
A0A2J8VK62 | A0A2J8VK62_PONAB | PFKFB3 | 520 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_034919 | 3-26 | in isoform 2 and isoform 3 | |||
Sequence: LELTQSRVQKIWVPVDHRPSLPRS → FRKA | ||||||
Sequence conflict | 37 | in Ref. 1; CAH92952 | ||||
Sequence: V → A | ||||||
Sequence conflict | 224 | in Ref. 1; CAH93512 | ||||
Sequence: V → A | ||||||
Sequence conflict | 326 | in Ref. 1; CAH91639 | ||||
Sequence: A → V | ||||||
Alternative sequence | VSP_034920 | 506-514 | in isoform 2 | |||
Sequence: PLLGQACLT → NMKGSRSSADSSRKH | ||||||
Alternative sequence | VSP_034921 | 514 | in isoform 3 | |||
Sequence: T → RTVCHIFSKFSPY |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR859468 EMBL· GenBank· DDBJ | CAH91639.1 EMBL· GenBank· DDBJ | mRNA | ||
CR860843 EMBL· GenBank· DDBJ | CAH92952.1 EMBL· GenBank· DDBJ | mRNA | ||
CR861456 EMBL· GenBank· DDBJ | CAH93512.1 EMBL· GenBank· DDBJ | mRNA |