Reviewed,
UniProtKB/Swiss-Prot P32811 (PHSH_SOLTU)
Last modified
June 16, 2009.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Alpha-glucan phosphorylase, H isozyme EC=2.4.1.1 Alternative name(s): Starch phosphorylase H |
| Organism | Solanum tuberosum (Potato) |
| Taxonomic identifier | 4113 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum |
Protein attributes
| Sequence length | 838 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. |
| Catalytic activity | (1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. |
| Cofactor | Pyridoxal phosphate. |
| Subcellular location | |
| Sequence similarities | Belongs to the glycogen phosphorylase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism |
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | Allosteric enzyme Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | phosphorylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| [1] | "Potato tuber type H phosphorylase isozyme. Molecular cloning, nucleotide sequence, and expression of a full-length cDNA in Escherichia coli." Mori H., Tanizawa K., Fukui T. J. Biol. Chem. 266:18446-18453(1991) [PubMed: 1917968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| M69038 mRNA. Translation: AAA33809.1. | |
| PIR | A40995. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1YGP based on UniProtKB P06738. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GT35. Glycosyltransferase Family 35. |
Enzyme and pathway databases | |
| BRENDA | 2.4.1.1. 296. |
Family and domain databases | |
| InterPro | IPR011833. Glycg_phsphrylas. IPR000811. Glyco_trans_35. [Graphical view] |
| PANTHER | PTHR11468. Glyco_trans_35. 1 hit. |
| Pfam | PF00343. Phosphorylase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000460. Pprylas_GlgP. 1 hit. |
| TIGRFAMs | TIGR02093. P_ylase. 1 hit. |
| PROSITE | PS00102. PHOSPHORYLASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PHSH_SOLTU | ||||||||
| Accession | Primary (citable) accession number: P32811 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


