Reviewed,
UniProtKB/Swiss-Prot Q3SZB7 (F16P1_BOVIN)
Last modified
January 19, 2010.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Fructose-1,6-bisphosphatase 1 Short name=FBPase 1 EC=3.1.3.11 Alternative name(s): D-fructose-1,6-bisphosphate 1-phosphohydrolase 1 | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 338 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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. AMP binding affects the turnover of bound substrate and not the affinity for substrate. Fructose-2,6-biphosphate acts as competitive inhibitor. Fructose-2,6-biphosphate and AMP have synergistic effects 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 | Acetylation |
| Technical term | Allosteric enzyme |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis 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 By similarity | ||||||
| Chain | 2 – 338 | 337 | Fructose-1,6-bisphosphatase 1 | PRO_0000247322 | |||||
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 | ||||||
| Binding site | 265 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylthreonine By similarity | ||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC102974 mRNA. Translation: AAI02975.1. |
| IPI | IPI00704584. |
| RefSeq | NP_001029619.1. |
| UniGene | Bt.24314 |
3D structure databases | |
| SMR | Q3SZB7. Positions 7-338. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q3SZB7. |
Proteomic databases | |
| PRIDE | Q3SZB7. |
Genome annotation databases | |
| Ensembl | ENSBTAT00000012835; ENSBTAP00000012835; ENSBTAG00000009733; Bos taurus. [Genome view] |
| GeneID | 513483. |
| KEGG | bta:513483. |
Organism-specific databases | |
| CTD | 513483. |
Phylogenomic databases | |
| eggNOG | maNOG08767. |
| HOVERGEN | Q3SZB7. |
| InParanoid | Q3SZB7. |
| PhylomeDB | Q3SZB7. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.11. 251. |
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... |
Entry information
| Entry name | F16P1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q3SZB7 | ||||||||
| Entry history |
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| 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


