Reviewed,
UniProtKB/Swiss-Prot Q46LG3 (FBSB_PROMT)
Last modified
June 16, 2009.
Version 20.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names 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 | Prochlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 59920 [NCBI] | ||
| Taxonomic lineage | Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus |
Protein attributes
| Sequence length | 334 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the FBPase class 2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calvin cycle Carbohydrate metabolism |
| 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 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_0000342722 | |||
Sequences
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References
| [1] | "Patterns and implications of gene gain and loss in the evolution of Prochlorococcus." Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W. PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000095 Genomic DNA. Translation: AAZ57665.1. | |
| RefSeq | YP_291368.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3605543. |
| GenomeReviews | Gene locus PMN2A_0173 in contig CP000095_GR. |
| KEGG | pmn:PMN2A_0173. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | Q46LG3. TSEWADM. |
Enzyme and pathway databases | |
| BioCyc | PMAR59920:PMN2A_0173-MON. |
Family and domain databases | |
| InterPro | IPR004464. GlpX. [Graphical view] |
| Pfam | PF03320. FBPase_glpX. 1 hit. [Graphical view] |
| PIRSF | PIRSF004532. GlpX. 1 hit. |
| ProDom | PD007014. GlpX. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00330. glpX. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | FBSB_PROMT | ||||||||
| Accession | Primary (citable) accession number: Q46LG3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


