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Reviewed, UniProtKB/Swiss-Prot P00489 (PYGM_RABIT)

Last modified November 25, 2008. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycogen phosphorylase, muscle form
    EC=2.4.1.1
Alternative name(s):
    Myophosphorylase
Gene names
Name: PYGM
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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.

Subunit structure

Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A.

Post-translational modification

Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A.

Sequence similarities

Belongs to the glycogen phosphorylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 843842Glycogen phosphorylase, muscle form
PRO_0000188532

Sites

Binding site761AMP
Binding site6811Pyridoxal phosphate (covalent)
Site1091Involved in the association of subunits
Site1431Involved in the association of subunits
Site1561Can be labeled by an AMP analog; may be involved in allosteric regulation

Amino acid modifications

Modified residue21N-acetylserine
Modified residue151Phosphoserine; by PHK; in form phosphorylase A
Modified residue4731Phosphotyrosine By similarity

Experimental info

Sequence conflict31 – 333NFN → DFD AA sequence Ref.2
Sequence conflict431D → N AA sequence Ref.2
Sequence conflict56 – 583LAH → HAL AA sequence Ref.2
Sequence conflict891E → Q AA sequence Ref.2
Sequence conflict1131T → D AA sequence Ref.2
Sequence conflict3091Missing AA sequence Ref.2
Sequence conflict578 – 5792LL → FF in CAA26833. Ref.6
Sequence conflict6101A → P in BAA00027 and CAA27816. Ref.1
Sequence conflict7131G → C in CAA26833. Ref.6

Secondary structure

................................................................................................................................................ 843
Helix Strand Turn

Details...