Q5MIB5 (PYGL_SHEEP) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 28, 2011.
Version 42.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glycogen phosphorylase, liver form EC=2.4.1.1 | ||
| Gene names |
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| Organism | Ovis aries (Sheep) | ||
| Taxonomic identifier | 9940 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis |
Protein attributes
| Sequence length | 851 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)
| 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 By similarity. |
| Catalytic activity | (1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Enzyme regulation | Activity of phosphorylase is controlled both by allosteric means (through the noncovalent binding of metabolites) and by covalent modification. Thus AMP allosterically activates, whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase B By similarity. |
| Subunit structure | Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A. Interacts with PPP1R3B By similarity. |
| Post-translational modification | Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A By similarity. |
| Sequence similarities | Belongs to the glycogen phosphorylase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Glycogen metabolism |
| Ligand | Nucleotide-binding Pyridoxal phosphate |
| Molecular function | Glycosyltransferase Transferase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Allosteric enzyme |
| Gene Ontology (GO) | |
| Biological process | glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorylase activityInferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| 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 – 851 | 850 | Glycogen phosphorylase, liver form | PRO_0000188527 | |||||
Sites | |||||||||
| Binding site | 76 | 1 | AMP By similarity | ||||||
| Site | 109 | 1 | Involved in the association of subunits By similarity | ||||||
| Site | 143 | 1 | Involved in the association of subunits By similarity | ||||||
| Site | 156 | 1 | May be involved in allosteric control By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 15 | 1 | Phosphoserine; by PHK; in form phosphorylase A By similarity | ||||||
| Modified residue | 75 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 76 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 681 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Characterization of ovine brain and liver glycogen phosphorylases." Walker K.R., Blechynden L.M., Binz N., Laing N.G. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY827551 mRNA. Translation: AAV87309.1. |
| RefSeq | NP_001020032.1. NM_001024861.1. |
| UniGene | Oar.3181. |
3D structure databases | |
| ProteinModelPortal | Q5MIB5. |
| SMR | Q5MIB5. Positions 6-838. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GT35. Glycosyltransferase Family 35. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 554320. |
Organism-specific databases | |
| CTD | 5836. |
Phylogenomic databases | |
| HOVERGEN | HBG006848. |
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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYGL_SHEEP | ||||||||
| Accession | Primary (citable) accession number: Q5MIB5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |