Reviewed,
UniProtKB/Swiss-Prot O02606 (PGM2_PARTE)
Last modified
June 16, 2009.
Version 51.
History...
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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: Phosphoglucomutase-2 Short name=PGM 2 EC=5.4.2.2 Alternative name(s): Glucose phosphomutase 2 Parafusin-2 Short name=Pf-2 | ||||
| Gene names |
| ||||
| Organism | Paramecium tetraurelia | ||||
| Taxonomic identifier | 5888 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Alveolata › Ciliophora › Intramacronucleata › Oligohymenophorea › Peniculida › Parameciidae › Paramecium |
Protein attributes
| Sequence length | 572 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | May be involved in membrane fusion in exocytosis By similarity. |
| Catalytic activity | Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Post-translational modification | Phosphorylated via a calcium-dependent protein kinase By similarity. |
| Sequence similarities | Belongs to the phosphohexose mutase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Isomerase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucomutase 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 – 572 | 572 | Phosphoglucomutase-2 | PRO_0000307834 | |||||
Sites | |||||||||
| Active site | 126 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 126 | 1 | Magnesium; via phosphate group By similarity | ||||||
| Metal binding | 308 | 1 | Magnesium By similarity | ||||||
| Metal binding | 310 | 1 | Magnesium By similarity | ||||||
| Metal binding | 312 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of isoforms of the exocytosis-sensitive phosphoprotein PP63/parafusin in Paramecium tetraurelia and demonstration of phosphoglucomutase activity." Hauser K., Kissmehl R., Linder J., Schultz J.E., Lottspeich F., Plattner H. Biochem. J. 323:289-296(1997) [PubMed: 9173895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Stock 51. |
| [2] | "Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia." Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R. Wincker P.Nature 444:171-178(2006) [PubMed: 17086204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Stock d4-2. |
Cross-references
Sequence databases | |
|---|---|
| Y09970 mRNA. Translation: CAA71089.1. CT868096 Genomic DNA. Translation: CAK70916.1. | |
| RefSeq | XP_001438313.1. |
| UniGene | Pte.8242 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1KFQ based on UniProtKB P47244. |
| SMR | O02606. Positions 3-572. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5024098. |
| KEGG | ptm:GSPATT00000627001. |
Enzyme and pathway databases | |
| BRENDA | 5.4.2.2. 21526. |
Family and domain databases | |
| InterPro | IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR005841. A-D-PHexomutase_N. [Graphical view] |
| Gene3D | G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 2 hits. |
| Pfam | PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view] |
| PRINTS | PR00509. PGMPMM. |
| PROSITE | PS00710. PGM_PMM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PGM2_PARTE | ||||||||
| Accession | Primary (citable) accession number: O02606 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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