Q3AK74 (FBSB_SYNSC) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 40.
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: D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase Short name=FBPase class 2/SBPase EC=3.1.3.11 EC=3.1.3.37 | ||
| Gene names |
| ||
| Organism | Synechococcus sp. (strain CC9605) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 110662 [NCBI] | ||
| Taxonomic lineage | Bacteria › Cyanobacteria › Chroococcales › Synechococcus |
Protein attributes
| Sequence length | 334 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the hydrolysis of fructose 1,6-bisphosphate (Fru 1,6-P2) and sedoheptulose 1,7-bisphosphate (Sed 1,7-P2) to fructose 6-phosphate and sedoheptulose 7-phosphate, respectively By similarity. |
| Catalytic activity | D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. Sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate. |
| Cofactor | Manganese By similarity. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the FBPase class 2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calvin cycle Carbohydrate metabolism |
| Ligand | Manganese Metal-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycerol metabolic process Inferred from electronic annotation. Source: InterPro reductive pentose-phosphate cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | fructose 1,6-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW sedoheptulose-bisphosphatase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 334 | 334 | D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase | PRO_0000342728 | |||||
Regions | |||||||||
| Region | 88 – 90 | 3 | Substrate binding By similarity | ||||||
| Region | 164 – 166 | 3 | Substrate binding By similarity | ||||||
| Region | 186 – 188 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 33 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 57 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 85 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 88 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 213 | 1 | Manganese 2 By similarity | ||||||
| Binding site | 119 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Complete sequence of Synechococcus sp. CC9605." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CC9605. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000110 Genomic DNA. Translation: ABB35008.1. |
| RefSeq | YP_381563.1. NC_007516.1. |
3D structure databases | |
| ProteinModelPortal | Q3AK74. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q3AK74. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3736457. |
| GenomeReviews | Gene locus Syncc9605_1253 in contig CP000110_GR. |
| KEGG | syd:Syncc9605_1253. |
| NMPDR | fig|110662.3.peg.222. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1494. |
| HOGENOM | HBG284837. |
| OMA | TSEWADM. |
| PhylomeDB | Q3AK74. |
| ProtClustDB | PRK09479. |
Enzyme and pathway databases | |
| BioCyc | SSP1131:SYNCC9605_1253-MONOMER. |
Family and domain databases | |
| InterPro | IPR004464. FBPase_class-2/SBPase. [Graphical view] |
| KO | K11532. |
| Pfam | PF03320. FBPase_glpX. 1 hit. [Graphical view] |
| PIRSF | PIRSF004532. GlpX. 1 hit. |
| TIGRFAMs | TIGR00330. GlpX. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | FBSB_SYNSC | ||||||||
| Accession | Primary (citable) accession number: Q3AK74 | ||||||||
| Entry history |
| ||||||||
| 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 |

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