P47859 (K6PP_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 88.
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-phosphofructokinase type C EC=2.7.1.11 Alternative name(s): Phosphofructo-1-kinase isozyme C Short name=PFK-C Phosphofructokinase 1 Phosphohexokinase | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) [Reference proteome] | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus![]() |
Protein attributes
| Sequence length | 791 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP By similarity. |
| Catalytic activity | ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. |
| Cofactor | Magnesium. |
| Enzyme regulation | Allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate. |
| Pathway | |
| Post-translational modification | GlcNAcylation decreases enzyme activity By similarity. |
| Sequence similarities | Belongs to the phosphofructokinase family. Two domains subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Domain | Repeat |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Acetylation Glycoprotein Phosphoprotein |
| Technical term | Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | fructose 6-phosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysisInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | 6-phosphofructokinase complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | 6-phosphofructokinase activity Inferred from direct assay PubMed 18632794. Source: UniProtKB ATP bindingInferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 791 | 791 | 6-phosphofructokinase type C | PRO_0000112026 | |||||
Regions | |||||||||
| Nucleotide binding | 44 – 48 | 5 | ATP By similarity | ||||||
| Nucleotide binding | 202 – 206 | 5 | ATP By similarity | ||||||
| Nucleotide binding | 219 – 235 | 17 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 175 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 233 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Binding site | 210 | 1 | Substrate By similarity | ||||||
| Binding site | 301 | 1 | Substrate By similarity | ||||||
| Binding site | 307 | 1 | Substrate By similarity | ||||||
| Binding site | 310 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 12 | 1 | Phosphoserine; by PKA Ref.2 | ||||||
| Modified residue | 386 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 395 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 486 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 651 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 688 | 1 | N6-acetyllysine By similarity | ||||||
| Glycosylation | 540 | 1 | O-linked (GlcNAc...) By similarity | ||||||
Sequences
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References
| [1] | "Structure and expression of the cDNA for the C isozyme of phosphofructo-1-kinase from rabbit brain." Li Y., Valaitis A.P., Latshaw S.P., Kwiatkowska D., Tripathi R.L., Campbell M.C., Kemp R.G. J. Biol. Chem. 269:5781-5787(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Brain. |
| [2] | "The sites of phosphorylation of rabbit brain phosphofructo-1-kinase by cyclic AMP-dependent protein kinase." Valaitis A.P., Foe L.G., Kwiatkowska D., Latshaw S.P., Kemp R.G. Biochim. Biophys. Acta 995:187-194(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 5-17, PHOSPHORYLATION AT SER-12. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U01154 mRNA. Translation: AAA17707.1. |
| PIR | A53206. |
| RefSeq | NP_001076217.1. NM_001082748.1. |
| UniGene | Ocu.6209. |
3D structure databases | |
| ProteinModelPortal | P47859. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9986.ENSOCUP00000009500. |
Proteomic databases | |
| PRIDE | P47859. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100009526. |
Organism-specific databases | |
| CTD | 5214. |
Phylogenomic databases | |
| eggNOG | COG0205. |
| HOGENOM | HOG000200154. |
| HOVERGEN | HBG000976. |
| OrthoDB | EOG4NS39Z. |
Enzyme and pathway databases | |
| UniPathway | UPA00109; UER00182. |
Family and domain databases | |
| InterPro | IPR009161. 6-phosphofructokinase_euk. IPR022953. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. IPR000023. Phosphofructokinase_dom. [Graphical view] |
| Pfam | PF00365. PFK. 2 hits. [Graphical view] |
| PIRSF | PIRSF000533. ATP_PFK_euk. 1 hit. |
| PRINTS | PR00476. PHFRCTKINASE. |
| SUPFAM | SSF53784. Ppfruckinase. 2 hits. |
| TIGRFAMs | TIGR02478. 6PF1K_euk. 1 hit. |
| PROSITE | PS00433. PHOSPHOFRUCTOKINASE. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | K6PP_RABIT | ||||||||
| Accession | Primary (citable) accession number: P47859 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
