Q28901 (F263_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 Short name=6PF-2-K/Fru-2,6-P2ase 3 Short name=PFK/FBPase 3 Alternative name(s): 6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme Including the following 2 domains:
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| Gene names |
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| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 463 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Synthesis and degradation of fructose 2,6-bisphosphate. |
| Catalytic activity | Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate. |
| Subunit structure | Homodimer By similarity. |
| Tissue specificity | Brain. |
| Post-translational modification | Phosphorylation by AMPK stimulates activity By similarity. |
| Sequence similarities | In the C-terminal section; belongs to the phosphoglycerate mutase family. |
| Sequence caution | The sequence AAB34145.2 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Hydrolase Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Multifunctional enzyme Reference proteome |
| Gene Ontology (GO) | |
| Biological process | fructose 2,6-bisphosphate metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | 6-phosphofructo-2-kinase activity Inferred from electronic annotation. Source: EC ATP bindingInferred from electronic annotation. Source: UniProtKB-KW fructose-2,6-bisphosphate 2-phosphatase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›463 | ›463 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 | PRO_0000179967 | |||||
Regions | |||||||||
| Nucleotide binding | 42 – 49 | 8 | ATP By similarity | ||||||
| Region | 1 – 246 | 246 | 6-phosphofructo-2-kinase | ||||||
| Region | 247 – ›463 | ›217 | Fructose-2,6-bisphosphatase | ||||||
Sites | |||||||||
| Active site | 125 | 1 | Potential | ||||||
| Active site | 155 | 1 | Potential | ||||||
| Active site | 255 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Active site | 324 | 1 | Potential | ||||||
| Active site | 389 | 1 | Proton donor By similarity | ||||||
| Binding site | 99 | 1 | Fructose-6-phosphate By similarity | ||||||
| Binding site | 191 | 1 | Fructose-6-phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 462 | 1 | Phosphoserine; by AMPK and PKA By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 463 | 1 | |||||||
Sequences
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References
| [1] | "Cloning and expression of a catalytic core bovine brain 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase." Ventura F., Ambrosio S., Bartrons R., El-Maghrabi M.R., Lange A.J., Pilkis S.J. Biochem. Biophys. Res. Commun. 209:1140-1148(1995) [PubMed: 7733968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | S77845 mRNA. Translation: AAB34145.2. Different initiation. |
| IPI | IPI00708598. |
| UniGene | Bt.12314. |
3D structure databases | |
| ProteinModelPortal | Q28901. |
| SMR | Q28901. Positions 3-462. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q28901. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| GeneTree | ENSGT00390000018751. |
| HOVERGEN | HBG005628. |
| InParanoid | Q28901. |
| OrthoDB | EOG4G4GQ4. |
| PhylomeDB | Q28901. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.46. 908. |
Family and domain databases | |
| InterPro | IPR003094. 6Pfruct_kin. IPR013079. 6Phosfructo_kin. IPR016260. Bifunct_6PFK/fruc_bisP_Ptase. IPR013078. His_Pase_superF_clade-1. IPR001345. PG/BPGM_mutase_AS. [Graphical view] |
| PANTHER | PTHR10606. 6Pfruct_kin. 1 hit. |
| Pfam | PF01591. 6PF2K. 1 hit. PF00300. His_Phos_1. 1 hit. [Graphical view] |
| PIRSF | PIRSF000709. 6PFK_2-Ptase. 1 hit. |
| PRINTS | PR00991. 6PFRUCTKNASE. |
| SMART | SM00855. PGAM. 1 hit. [Graphical view] |
| PROSITE | PS00175. PG_MUTASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | F263_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q28901 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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