O08333 (K6PF1_STRCO) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 94.
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 1 EC=2.7.1.11 Alternative name(s): ATP-PFK Phosphofructokinase 1 Phosphohexokinase 1 | ||||||||
| Gene names |
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| Organism | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP] | ||||||||
| Taxonomic identifier | 100226 [NCBI] | ||||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › ![]() |
Protein attributes
| Sequence length | 342 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339 |
| Enzyme regulation | Allosterically inhibited by phosphoenolpyruvate. HAMAP-Rule MF_00339 |
| Pathway | Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339 |
| Subunit structure | Homotetramer By similarity. HAMAP-Rule MF_00339 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00339. |
| Sequence similarities | Belongs to the phosphofructokinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Allosteric enzyme Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | fructose 6-phosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysisInferred from electronic annotation. Source: HAMAP |
| Cellular_component | 6-phosphofructokinase complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | 6-phosphofructokinase activity Inferred from electronic annotation. Source: HAMAP 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 – 342 | 342 | 6-phosphofructokinase 1 HAMAP-Rule MF_00339 | PRO_0000111986 | |||||
Regions | |||||||||
| Nucleotide binding | 20 – 24 | 5 | ATP By similarity | ||||||
| Nucleotide binding | 155 – 159 | 5 | ATP By similarity | ||||||
| Nucleotide binding | 172 – 188 | 17 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 128 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 186 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Binding site | 163 | 1 | Substrate By similarity | ||||||
| Binding site | 266 | 1 | Substrate By similarity | ||||||
| Binding site | 272 | 1 | Substrate By similarity | ||||||
| Binding site | 275 | 1 | Substrate By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of ATP-dependent phosphofructokinase as a regulatory step in the glycolytic pathway of the actinomycete Streptomyces coelicolor A3(2)." Alves A.M.C.R., Euverink G.J.W., Bibb M.J., Dijkhuizen L. Appl. Environ. Microbiol. 63:956-961(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: A3(2) / 1109. |
| [2] | "Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. Hopwood D.A.Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U51728 Genomic DNA. Translation: AAC45135.1. AL939111 Genomic DNA. Translation: CAB51967.1. |
| PIR | T35500. |
| RefSeq | NP_626376.1. NC_003888.3. |
3D structure databases | |
| ProteinModelPortal | O08333. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 100226.SCO2119. |
PTM databases | |
| PhosSite | P1007943. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB51967; CAB51967; CAB51967. |
| GeneID | 1097553. |
| KEGG | sco:SCO2119. |
| PATRIC | 23733890. VBIStrCoe124346_2154. |
Phylogenomic databases | |
| eggNOG | COG0205. |
| HOGENOM | HOG000248869. |
| KO | K00850. |
| OMA | TVPLERY. |
| ProtClustDB | PRK03202. |
Enzyme and pathway databases | |
| UniPathway | UPA00109; UER00182. |
Family and domain databases | |
| HAMAP | MF_00339. Phosphofructokinase. |
| InterPro | IPR012003. ATP_PFK_prok. IPR012829. PFK. IPR022953. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. IPR000023. Phosphofructokinase_dom. [Graphical view] |
| Pfam | PF00365. PFK. 1 hit. [Graphical view] |
| PIRSF | PIRSF000532. ATP_PFK_prok. 1 hit. |
| PRINTS | PR00476. PHFRCTKINASE. |
| SUPFAM | SSF53784. Ppfruckinase. 1 hit. |
| TIGRFAMs | TIGR02483. PFK_mixed. 1 hit. |
| PROSITE | PS00433. PHOSPHOFRUCTOKINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | K6PF1_STRCO | ||||||||
| Accession | Primary (citable) accession number: O08333 | ||||||||
| 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
