PYGM_BOVIN
ID PYGM_BOVIN Reviewed; 842 AA.
AC P79334;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Glycogen phosphorylase, muscle form {ECO:0000305|PubMed:8845714};
DE EC=2.4.1.1 {ECO:0000305|PubMed:8845714};
DE AltName: Full=Myophosphorylase;
GN Name=PYGM {ECO:0000250|UniProtKB:P11217};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT GSD-V TRP-490, DISEASE, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Skeletal muscle;
RX PubMed=8845714; DOI=10.1016/0960-8966(95)00014-3;
RA Tsujino S., Shanske S., Valberg S.J., Cardinet G.H. III, Smith B.P.,
RA DiMauro S.;
RT "Cloning of bovine muscle glycogen phosphorylase cDNA and identification of
RT a mutation in cattle with myophosphorylase deficiency, an animal model for
RT McArdle's disease.";
RL Neuromuscul. Disord. 6:19-26(1996).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000305|PubMed:8845714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000305|PubMed:8845714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733;
CC Evidence={ECO:0000305|PubMed:8845714};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P00489};
CC -!- ACTIVITY REGULATION: Allosterically regulated through the non-covalent
CC binding of metabolites, being activated by AMP and inhibited by ATP,
CC ADP, and glucose-6-phosphate. The activity is also controlled by post-
CC translational modifications including phosphorylation.
CC {ECO:0000250|UniProtKB:P11217}.
CC -!- SUBUNIT: Homodimer. Homotetramer; to form the enzymatically active
CC phosphorylase A. {ECO:0000250|UniProtKB:P11217}.
CC -!- PTM: Phosphorylation of Ser-15 converts phosphorylase B
CC (unphosphorylated) to phosphorylase A. {ECO:0000250|UniProtKB:P11217}.
CC -!- DISEASE: Note=Defects in PYGM are the cause of glycogen storage disease
CC V (GSD-V); also known as McArdle disease. {ECO:0000269|PubMed:8845714}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; S82859; AAB46846.1; -; mRNA.
DR RefSeq; NP_786980.1; NM_175786.2.
DR AlphaFoldDB; P79334; -.
DR SMR; P79334; -.
DR STRING; 9913.ENSBTAP00000001373; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR PaxDb; P79334; -.
DR PeptideAtlas; P79334; -.
DR PRIDE; P79334; -.
DR GeneID; 327664; -.
DR KEGG; bta:327664; -.
DR CTD; 5837; -.
DR eggNOG; KOG2099; Eukaryota.
DR InParanoid; P79334; -.
DR OrthoDB; 240595at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008184; F:glycogen phosphorylase activity; ISS:UniProtKB.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; ISS:UniProtKB.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; Carbohydrate metabolism; Disease variant;
KW Glycogen metabolism; Glycogen storage disease; Glycosyltransferase;
KW Nucleotide-binding; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT CHAIN 2..842
FT /note="Glycogen phosphorylase, muscle form"
FT /id="PRO_0000188528"
FT BINDING 43
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P11217"
FT BINDING 76
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT BINDING 310..319
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P11217"
FT SITE 109
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT SITE 143
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT SITE 156
FT /note="May be involved in allosteric control"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT MOD_RES 15
FT /note="Phosphoserine; by PHK; in form phosphorylase A"
FT /evidence="ECO:0000250|UniProtKB:P11217"
FT MOD_RES 204
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUB3"
FT MOD_RES 473
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUB3"
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
FT VARIANT 490
FT /note="R -> W (in GSD-V)"
FT /evidence="ECO:0000269|PubMed:8845714"
SQ SEQUENCE 842 AA; 97293 MW; DFCEF2D8ADBF878E CRC64;
MSRPLTDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAYTV
RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YIGRTLQNTM VNLALENACD EATYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA
DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN
TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCL DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDQERL
EWEKAWEVTV KTCAYTNHTV LPEALERWPV HLIETLLPRH LQIIYEINQR FLNRVAAAFP
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF
QNKTNGITPR RWLVMCNPGL AEIIAERIGE EYIADLDQLR KLLSYVDDES FIRDVAKVKQ
ENKLKFSAYL EKEYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKKEPNKFFV
PRTVMIGGKA APGYHMAKMI IKLITAIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVE
RLDQKGYNAQ EYYDRIPELR HVIDQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYEE
YIKCQERVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP TRQRMPAPDE
KI
