Reviewed,
UniProtKB/Swiss-Prot Q05079 (F16P_KLULA)
Last modified
June 16, 2009.
Version 59.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Fructose-1,6-bisphosphatase Short name=FBPase EC=3.1.3.11 Alternative name(s): D-fructose-1,6-bisphosphate 1-phosphohydrolase | ||||
| Gene names |
| ||||
| Organism | Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome] | ||||
| Taxonomic identifier | 28985 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces |
Protein attributes
| Sequence length | 355 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. |
| Cofactor | Binds 3 magnesium ions per subunit By similarity. |
| Enzyme regulation | Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate By similarity. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the FBPase class 1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| Technical term | Allosteric enzyme Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | fructose 1,6-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC magnesium 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Probable | ||||||
| Chain | 2 – 355 | 354 | Fructose-1,6-bisphosphatase | PRO_0000200509 | |||||
Regions | |||||||||
| Nucleotide binding | 37 – 41 | 5 | AMP By similarity | ||||||
| Nucleotide binding | 121 – 122 | 2 | AMP By similarity | ||||||
| Region | 130 – 133 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 78 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 107 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 107 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 127 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 127 | 1 | Magnesium 3 By similarity | ||||||
| Metal binding | 129 | 1 | Magnesium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 130 | 1 | Magnesium 3 By similarity | ||||||
| Metal binding | 300 | 1 | Magnesium 3 By similarity | ||||||
| Binding site | 230 | 1 | Substrate By similarity | ||||||
| Binding site | 264 | 1 | Substrate By similarity | ||||||
| Binding site | 284 | 1 | Substrate By similarity | ||||||
| Binding site | 294 | 1 | Substrate By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Fructose-1,6-bisphosphatase of the yeast Kluyveromyces lactis." Zaror I., Marcus F., Moyer D.L., Tung J., Shuster J.R. Eur. J. Biochem. 212:193-199(1993) [PubMed: 8383039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SD11. |
| [2] | "Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.  Souciet J.-L.Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37. |
Cross-references
Sequence databases | |
|---|---|
| X70181 Genomic DNA. Translation: CAA49728.1. CR382125 Genomic DNA. Translation: CAG99090.1. | |
| PIR | S29397. |
| RefSeq | XP_454003.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FBH based on UniProtKB P00636. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2894286. |
| KEGG | kla:KLLA0E01210g. |
Phylogenomic databases | |
| HOGENOM | Q05079. |
| OMA | Q05079. MADQAPF. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.11. 74088. |
Family and domain databases | |
| InterPro | IPR000146. Fructose_bisphosphatase. IPR017955. IMPase/FBPase. [Graphical view] |
| PANTHER | PTHR11556. In_FB_phphtase. 1 hit. |
| Pfam | PF00316. FBPase. 1 hit. [Graphical view] |
| PRINTS | PR00115. FBPHPHTASE. PR00377. INFBPHPHTASE. |
| ProDom | PD001491. In_FB_phphtase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00124. FBPASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | F16P_KLULA | ||||||||
| Accession | Primary (citable) accession number: Q05079 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
