Q4MVY3 (K6PF_BACCE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 35.
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 Short name=Phosphofructokinase EC=2.7.1.11 Alternative name(s): Phosphohexokinase | ||||||
| Gene names |
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| Organism | Bacillus cereus | ||||||
| Taxonomic identifier | 1396 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group![]() |
Protein attributes
| Sequence length | 319 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 |
| 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. |
| Subcellular location | Cytoplasm By similarity. |
| Induction | By salt stress. Ref.2 |
| Sequence similarities | Belongs to the phosphofructokinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis Stress response |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Allosteric enzyme Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | fructose 6-phosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysisInferred from electronic annotation. Source: HAMAP response to stressInferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 319 | 319 | 6-phosphofructokinase HAMAP-Rule MF_00339 | PRO_0000271249 | |||||
Regions | |||||||||
| Nucleotide binding | 21 – 25 | 5 | ATP By similarity | ||||||
| Nucleotide binding | 154 – 158 | 5 | ATP By similarity | ||||||
| Nucleotide binding | 171 – 187 | 17 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 127 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 185 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 187 | 1 | Magnesium By similarity | ||||||
| Binding site | 162 | 1 | Substrate By similarity | ||||||
| Binding site | 243 | 1 | Substrate By similarity | ||||||
| Binding site | 249 | 1 | Substrate By similarity | ||||||
| Binding site | 252 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax." Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D., Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W., Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J., Peterson S.N., Weyant R.S. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G9241. |
| [2] | "Heat and salt stress in the food pathogen Bacillus cereus." Browne N., Dowds B.C.A. J. Appl. Microbiol. 91:1085-1094(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, INDUCTION. Strain: NCIMB 11796 / DSM 626. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AAEK01000003 Genomic DNA. Translation: EAL16121.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 6PFK based on UniProtKB P00512. |
| ProteinModelPortal | Q4MVY3. |
| SMR | Q4MVY3. Positions 1-319. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EAL16121; EAL16121; BCE_G9241_4679. |
| PATRIC | 24953657. VBIBacCer116370_0791. |
Enzyme and pathway databases | |
| UniPathway | UPA00109; UER00182. |
Family and domain databases | |
| HAMAP | MF_00339. Phosphofructokinase. |
| InterPro | IPR012003. ATP_PFK_prok. IPR012828. PFKA_ATP. 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 | TIGR02482. PFKA_ATP. 1 hit. |
| PROSITE | PS00433. PHOSPHOFRUCTOKINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | K6PF_BACCE | ||||||||
| Accession | Primary (citable) accession number: Q4MVY3 Secondary accession number(s): P83066 | ||||||||
| 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
