P53534 · PYGB_RAT
- ProteinGlycogen phosphorylase, brain form
- GenePygb
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids838 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Glycogen phosphorylase that regulates glycogen mobilization (By similarity).
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
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
[(1→4)-α-D-glucosyl](n) RHEA-COMP:9584 + CHEBI:43474 = [(1→4)-α-D-glucosyl](n-1) RHEA-COMP:9586 + CHEBI:58601
Cofactor
Activity regulation
Activity of phosphorylase is controlled both by allosteric means (through the non-covalent binding of metabolites) and by covalent modification. Thus AMP allosterically activates, whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase B.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 43 | AMP (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Site | 76 | Participates in a stacking interaction with the adenine ring of AMP | |||
Site | 109 | Involved in the association of subunits | |||
Site | 143 | Involved in the association of subunits | |||
Site | 156 | May be involved in allosteric control | |||
Binding site | 197 | AMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Binding site | 310 | AMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Binding site | 569 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cytoplasm | |
Molecular Function | carbohydrate binding | |
Molecular Function | glycogen phosphorylase activity | |
Molecular Function | identical protein binding | |
Molecular Function | linear malto-oligosaccharide phosphorylase activity | |
Molecular Function | organic cyclic compound binding | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | SHG alpha-glucan phosphorylase activity | |
Biological Process | glycogen catabolic process | |
Biological Process | glycogen metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlycogen phosphorylase, brain form
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP53534
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Initiator methionine | 1 | Removed | |||
Modified residue | 2 | N-acetylalanine | |||
Chain | PRO_0000188538 | 2-838 | Glycogen phosphorylase, brain form | ||
Modified residue | 15 | Phosphoserine | |||
Modified residue | 197 | Phosphotyrosine | |||
Modified residue | 473 | Phosphotyrosine | |||
Modified residue | 524 | Phosphoserine | |||
Modified residue | 681 | N6-(pyridoxal phosphate)lysine | |||
Post-translational modification
Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 677-678 | Pyridoxal 5'-phosphate | |||
Sequence similarities
Belongs to the glycogen phosphorylase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length838
- Mass (Da)96,174
- Last updated2007-01-23 v3
- MD5 ChecksumB8020B8E513E6E4D24DBF8B35283AF31
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6GKE5 | A0A8I6GKE5_RAT | Pygb | 838 | ||
A0A8I6G9W3 | A0A8I6G9W3_RAT | Pygb | 775 | ||
G3V6Y6 | G3V6Y6_RAT | Pygb | 846 |
Features
Showing features for sequence conflict, non-terminal residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 589 | in Ref. 3; AAA40815 | |||
Non-terminal residue | 838 | ||||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L10668 EMBL· GenBank· DDBJ | AAA41252.1 EMBL· GenBank· DDBJ | mRNA | ||
M27726 EMBL· GenBank· DDBJ | AAA40815.1 EMBL· GenBank· DDBJ | mRNA |