Reviewed,
UniProtKB/Swiss-Prot Q06137 (YL345_YEAST)
Last modified
January 19, 2010.
Version 69.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase YLR345W Including the following 2 domains: 1- Recommended name: 6-phosphofructo-2-kinase EC=2.7.1.105 2- Recommended name: Fructose-2,6-bisphosphatase EC=3.1.3.46 | ||
| Gene names |
| ||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||
| Taxonomic identifier | 4932 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 509 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Synthesis and degradation of fructose 2,6-bisphosphate By similarity. |
| 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. |
| Subcellular location | |
| Induction | Expression is under the control of the RFX1 transcription factor. Ref.4 |
| Miscellaneous | Present with 3380 molecules/cell in log phase SD medium. Ref.3 |
| Sequence similarities | In the C-terminal section; belongs to the phosphoglycerate mutase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Hydrolase Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | fructose 2,6-bisphosphate metabolic process Ref.4 Non-traceable author statement. Source: SGD regulation of glycolysis Ref.4Non-traceable author statement. Source: SGD |
| Cellular component | cytoplasm Ref.2 Inferred from direct assay. Source: SGD |
| Molecular function | 6-phosphofructo-2-kinase activity Ref.4 Non-traceable author statement. Source: SGD ATP bindingInferred from electronic annotation. Source: UniProtKB-KW fructose-2,6-bisphosphate 2-phosphatase activityInferred from electronic annotation. Source: EC protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Q06146 | 1 | EBI-33827,EBI-36149 | ||
| MTR3 | P48240 | 3 | EBI-33827,EBI-1749 | |
| PRP45 | P28004 | 2 | EBI-33827,EBI-20640 | |
| RNR2 | P09938 | 1 | EBI-33827,EBI-15240 | |
| SFH1 | Q06168 | 3 | EBI-33827,EBI-35813 | |
| SIC1 | P38634 | 1 | EBI-33827,EBI-17127 | |
| TPS3 | P38426 | 1 | EBI-33827,EBI-19448 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 509 | 509 | Putative 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase YLR345W | PRO_0000268185 | |||||
Regions | |||||||||
| Nucleotide binding | 90 – 97 | 8 | ATP By similarity | ||||||
| Region | 6 – 291 | 286 | 6-phosphofructo-2-kinase By similarity | ||||||
| Region | 292 – 466 | 175 | Fructose-2,6-bisphosphatase By similarity | ||||||
Sites | |||||||||
| Active site | 173 | 1 | Potential | ||||||
| Active site | 459 | 1 | Proton donor By similarity | ||||||
| Binding site | 237 | 1 | Fructose-6-phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 6 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 75 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 104 | 1 | Phosphothreonine Ref.5 | ||||||
| Modified residue | 432 | 1 | Phosphoserine Ref.6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D.Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [2] | "Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [3] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [4] | "Identification of new genes regulated by the Crt1 transcription factor, an effector of the DNA damage checkpoint pathway in Saccharomyces cerevisiae." Zaim J., Speina E., Kierzek A.M. J. Biol. Chem. 280:28-37(2005) [PubMed: 15494396] [Abstract] Cited for: INDUCTION. |
| [5] | "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, MASS SPECTROMETRY. |
| [6] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-75 AND SER-432, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U19028 Genomic DNA. Translation: AAB67253.1. |
| PIR | S51348. |
| RefSeq | NP_013449.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2AXN based on UniProtKB Q16875. |
| SMR | Q06137. Positions 83-506. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-1500N. |
| IntAct | Q06137. 21 interactions. |
| STRING | Q06137. |
Proteomic databases | |
| PeptideAtlas | Q06137. |
Genome annotation databases | |
| Ensembl | YLR345W; YLR345W; YLR345W; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 851059. |
| KEGG | sce:YLR345W. |
| NMPDR | fig|4932.3.peg.4470. |
Organism-specific databases | |
| CYGD | YLR345w. |
| SGD | S000004337. YLR345W. |
Phylogenomic databases | |
| eggNOG | fuNOG04023. |
| HOGENOM | HBG395770. |
| OMA | SYHDLAV. |
| OrthoDB | EOG9TQNS1. |
| PhylomeDB | Q06137. |
Enzyme and pathway databases | |
| BRENDA | 2.7.1.105. 250. 3.1.3.46. 250. |
Gene expression databases | |
| ArrayExpress | Q06137. |
| Genevestigator | Q06137. |
| GermOnline | YLR345W. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR003094. 6Pfruct_kin. IPR013079. 6Phosfructo_kin. IPR016260. Bifunct_6PFK/fruc_bisP_Ptase. IPR013078. PG_mutase. [Graphical view] |
| PANTHER | PTHR10606. 6Pfruct_kin. 1 hit. |
| Pfam | PF01591. 6PF2K. 1 hit. PF00300. PGAM. 1 hit. [Graphical view] |
| PIRSF | PIRSF000709. 6PFK_2-Ptase. 1 hit. |
| PRINTS | PR00991. 6PFRUCTKNASE. |
| SMART | SM00855. PGAM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 967684. |
Entry information
| Entry name | YL345_YEAST | ||||||||
| Accession | Primary (citable) accession number: Q06137 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

Clusters with


