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Reviewed, UniProtKB/Swiss-Prot O18751 (PYGM_SHEEP)

Last modified October 13, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 · 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
OrganismOvis aries (Sheep)
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

Sequence length842 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Catalytic activity

(1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.

Cofactor

Pyridoxal phosphate.

Subunit structure

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 842841Glycogen phosphorylase, muscle form
PRO_0000188534

Sites

Binding site761AMP By similarity
Site1091Involved in the association of subunits By similarity
Site1431Involved in the association of subunits By similarity
Site1561May be involved in allosteric control By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue151Phosphoserine; by PHK; in form phosphorylase A By similarity
Modified residue3161N6-acetyllysine By similarity
Modified residue4731Phosphotyrosine By similarity
Modified residue6811N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O18751-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E0EDEE3591DFA81C

FASTA84297,307
        10         20         30         40         50         60 
MSRPLTDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAYTV 

        70         80         90        100        110        120 
RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YIGRTLQNTM VNLALENACD EATYQLGLDM 

       130        140        150        160        170        180 
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA 

       190        200        210        220        230        240 
DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN 

       250        260        270        280        290        300 
TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 

       310        320        330        340        350        360 
VAATLQDIIR RFKSSKFGCL DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDQERL 

       370        380        390        400        410        420 
EWEKAWEVTV KTCAYTNHTV LPEALERWPV HLIETLLPRH LQIIYEINQR FLNRVAAAFP 

       430        440        450        460        470        480 
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF 

       490        500        510        520        530        540 
QNKTNGITPR RWLVMCNPGL AEVIAERIGE EYIADLDQLR KLLSYVDDES FIRDVAKVKQ 

       550        560        570        580        590        600 
ENKLKFSAYL EKEYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKKEPNKFFV 

       610        620        630        640        650        660 
PRTVMIGGKA APGYHMAKMI IRLITAIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA 

       670        680        690        700        710        720 
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVE 

       730        740        750        760        770        780 
RLDQKGYNAQ EYYDRIPELR HIIDQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYEE 

       790        800        810        820        830        840 
YVKCQERVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP TRQRMPAPDE 


KI 

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References

[1]"A splice-site mutation causing ovine McArdle's disease."
Tan P., Allen J.G., Wilton S.D., Akkari P.A., Huxtable C.R., Laing N.G.
Neuromuscul. Disord. 7:336-342(1997) [PubMed: 9267848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Merino.
Tissue: Muscle.

Cross-references

Sequence databases

AF001899 mRNA. Translation: AAB68800.1.
RefSeqNP_001009192.1.
UniGeneOar.860

3D structure databases

HSSPHSSP built from PDB template 1A8I based on UniProtKB P00489.
SMRO18751. Positions 13-836.
ModBaseSearch...

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

Genome annotation databases

GeneID442998.

Organism-specific databases

CTD442998.

Phylogenomic databases

HOVERGENO18751.

Enzyme and pathway databases

BRENDA2.4.1.1. 271.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERPTHR11468. Glyco_trans_35. 1 hit.
PfamPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsTIGR02093. P_ylase. 1 hit.
PROSITEPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYGM_SHEEP
AccessionPrimary (citable) accession number: O18751
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: January 23, 2007
Last modified: October 13, 2009
This is version 71 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents