Reviewed,
UniProtKB/Swiss-Prot Q9Z1N1 (F16P2_RAT)
Last modified
January 19, 2010.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Fructose-1,6-bisphosphatase isozyme 2 Short name=FBPase 2 EC=3.1.3.11 Alternative name(s): D-fructose-1,6-bisphosphate 1-phosphohydrolase 2 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 339 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level. |
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. Fructose-2,6-biphosphate acts as competitive inhibitor By similarity. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the FBPase class 1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Gluconeogenesis |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Technical term | Allosteric enzyme |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis Inferred from direct assay. Source: RGD |
| Molecular function | fructose 1,6-bisphosphate 1-phosphatase activity Inferred from direct assay. Source: RGD 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 339 | 339 | Fructose-1,6-bisphosphatase isozyme 2 | PRO_0000200507 | |||||
Regions | |||||||||
| Nucleotide binding | 18 – 22 | 5 | AMP By similarity | ||||||
| Nucleotide binding | 28 – 32 | 5 | AMP By similarity | ||||||
| Nucleotide binding | 113 – 114 | 2 | AMP By similarity | ||||||
| Region | 122 – 125 | 4 | Substrate binding By similarity | ||||||
| Region | 213 – 216 | 4 | Substrate binding By similarity | ||||||
| Region | 244 – 249 | 6 | Substrate binding By similarity | ||||||
| Region | 275 – 277 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 69 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 98 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 98 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 119 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 119 | 1 | Magnesium 3 By similarity | ||||||
| Metal binding | 121 | 1 | Magnesium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 122 | 1 | Magnesium 3 By similarity | ||||||
| Metal binding | 281 | 1 | Magnesium 3 By similarity | ||||||
| Binding site | 141 | 1 | AMP By similarity | ||||||
| Binding site | 265 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 216 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning and expression of rat muscle fructose-1,6-bisphosphatase cDNA." Al-Robaiy S., Eschrich K. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ005046 mRNA. Translation: CAA06313.1. |
| IPI | IPI00209038. |
| RefSeq | NP_446168.1. |
| UniGene | Rn.15319 |
3D structure databases | |
| SMR | Q9Z1N1. Positions 7-337. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9Z1N1. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000023865; ENSRNOP00000023865; ENSRNOG00000017637; Rattus norvegicus. [Genome view] |
| GeneID | 114508. |
| KEGG | rno:114508. |
| UCSC | NM_053716. rat. |
Organism-specific databases | |
| CTD | 114508. |
| RGD | 620930. Fbp2. |
Phylogenomic databases | |
| eggNOG | roNOG08567. |
| HOVERGEN | Q9Z1N1. |
| InParanoid | Q9Z1N1. |
| PhylomeDB | Q9Z1N1. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.11. 248. |
Gene expression databases | |
| ArrayExpress | Q9Z1N1. |
| Genevestigator | Q9Z1N1. |
| GermOnline | ENSRNOG00000017637. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000146. Fructose_bisphosphatase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view] |
| PANTHER | PTHR11556. In_FB_phphtase. 1 hit. |
| Pfam | PF00316. FBPase. 1 hit. [Graphical view] |
| PRINTS | PR00115. F16BPHPHTASE. |
| PROSITE | PS00124. FBPASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 618609. |
Entry information
| Entry name | F16P2_RAT | ||||||||
| Accession | Primary (citable) accession number: Q9Z1N1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


