Q9V2Z7 (K6PF_PYRFU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 78.
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: ADP-specific phosphofructokinase EC=2.7.1.146 Alternative name(s): ADP-dependent phosphofructokinase Short name=ADP-Pfk | ||||||
| Gene names |
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| Organism | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 186497 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › ![]() |
Protein attributes
| Sequence length | 454 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate using ADP as the phosphate donor. As a phosphoryl group donor, ADP can be replaced by GDP, ATP, and GTP to a limited extent. HAMAP-Rule MF_00561 |
| Catalytic activity | ADP + D-fructose 6-phosphate = AMP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00561 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Enzyme regulation | Inhibited by AMP and ATP. HAMAP-Rule MF_00561 |
| Pathway | |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Sequence similarities | Belongs to the carbohydrate kinase PfkC family. Contains 1 ADPK (ADP-dependent kinase) domain. |
| Biophysicochemical properties | Kinetic parameters: The kinetic parameters were measured at 50 degrees Celsius. KM=2.3 mM for fructose 6-phosphate KM=0.11 mM for ADP Vmax=194 µmol/min/mg enzyme with fructose 6-phosphate as substrate Vmax=150 µmol/min/mg enzyme with ADP as substrate pH dependence: Optimum pH is 6.5. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | fructose metabolic process Inferred from electronic annotation. Source: InterPro glycolysisInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ADP-specific phosphofructokinase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: HAMAP phosphofructokinase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 454 | 454 | ADP-specific phosphofructokinase HAMAP-Rule MF_00561 | PRO_0000184766 | |||||
Regions | |||||||||
| Domain | 1 – 452 | 452 | ADPK | ||||||
Sites | |||||||||
| Active site | 436 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 263 | 1 | Magnesium By similarity | ||||||
| Metal binding | 293 | 1 | Magnesium By similarity | ||||||
| Metal binding | 436 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus." Tuininga J.E., Verhees C.H., van der Oost J., Kengen S.W.M., Stams A.J.M., de Vos W.M. J. Biol. Chem. 274:21023-21028(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1. |
| [2] | "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF127909 Genomic DNA. Translation: AAD48400.1. AE009950 Genomic DNA. Translation: AAL81908.1. |
| RefSeq | NP_579513.1. NC_003413.1. |
3D structure databases | |
| ProteinModelPortal | Q9V2Z7. |
| SMR | Q9V2Z7. Positions 8-453. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 186497.PF1784. |
Proteomic databases | |
| PRIDE | Q9V2Z7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAL81908; AAL81908; PF1784. |
| GeneID | 1469663. |
| KEGG | pfu:PF1784. |
Phylogenomic databases | |
| eggNOG | COG4809. |
| HOGENOM | HOG000254055. |
| KO | K00918. |
| OMA | HLEFASI. |
| ProtClustDB | PRK03979. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-11808. |
| UniPathway | UPA00109. |
Family and domain databases | |
| HAMAP | MF_00561. ADP_PFKinase. |
| InterPro | IPR007666. ADP_PFK/GK. IPR015990. ADP_PFK/GK_arc. IPR011790. ADP_PFK_arc. [Graphical view] |
| PANTHER | PTHR21208. PTHR21208. 1 hit. |
| Pfam | PF04587. ADP_PFK_GK. 1 hit. [Graphical view] |
| PIRSF | PIRSF015883. ADP-Pfk_glckin. 1 hit. |
| TIGRFAMs | TIGR02045. P_fruct_ADP. 1 hit. |
| PROSITE | PS51255. ADPK. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | K6PF_PYRFU | ||||||||
| Accession | Primary (citable) accession number: Q9V2Z7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
