ID   PYGB_BOVIN              Reviewed;         843 AA.
AC   Q3B7M9;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Glycogen phosphorylase, brain form;
DE            EC=2.4.1.1;
GN   Name=PYGB;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Glycogen phosphorylase that regulates glycogen mobilization.
CC       Phosphorylase is an important allosteric enzyme in carbohydrate
CC       metabolism. Enzymes from different sources differ in their regulatory
CC       mechanisms and in their natural substrates. However, all known
CC       phosphorylases share catalytic and structural properties.
CC       {ECO:0000250|UniProtKB:P11216}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activity of phosphorylase is controlled both by
CC       allosteric means (through the non-covalent binding of metabolites) and
CC       by covalent modification. Thus AMP allosterically activates, whereas
CC       ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase
CC       B (By similarity). {ECO:0000250|UniProtKB:P11216}.
CC   -!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
CC       enzymatically active phosphorylase A (By similarity).
CC       {ECO:0000250|UniProtKB:P11216}.
CC   -!- PTM: Phosphorylation of Ser-15 converts phosphorylase B
CC       (unphosphorylated) to phosphorylase A. {ECO:0000250|UniProtKB:P11217}.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; BC107536; AAI07537.1; -; mRNA.
DR   RefSeq; NP_001030347.1; NM_001035270.1.
DR   AlphaFoldDB; Q3B7M9; -.
DR   SMR; Q3B7M9; -.
DR   STRING; 9913.ENSBTAP00000006069; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PaxDb; Q3B7M9; -.
DR   PRIDE; Q3B7M9; -.
DR   GeneID; 505560; -.
DR   KEGG; bta:505560; -.
DR   CTD; 5834; -.
DR   eggNOG; KOG2099; Eukaryota.
DR   InParanoid; Q3B7M9; -.
DR   OrthoDB; 240595at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
DR   GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
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; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Allosteric enzyme; Carbohydrate metabolism;
KW   Glycogen metabolism; Glycosyltransferase; Phosphoprotein;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P11216"
FT   CHAIN           2..843
FT                   /note="Glycogen phosphorylase, brain form"
FT                   /id="PRO_0000239657"
FT   REGION          677..678
FT                   /note="Pyridoxal 5'-phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P11216"
FT   BINDING         43
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P11216"
FT   BINDING         197
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P11216"
FT   BINDING         310
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P11216"
FT   BINDING         569
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P11216"
FT   SITE            76
FT                   /note="Participates in a stacking interaction with the
FT                   adenine ring of AMP"
FT                   /evidence="ECO:0000250|UniProtKB:P11216"
FT   SITE            109
FT                   /note="Involved in the association of subunits"
FT                   /evidence="ECO:0000250"
FT   SITE            143
FT                   /note="Involved in the association of subunits"
FT                   /evidence="ECO:0000250"
FT   SITE            156
FT                   /note="May be involved in allosteric control"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P11216"
FT   MOD_RES         15
FT                   /note="Phosphoserine; by PHK; in form phosphorylase A"
FT                   /evidence="ECO:0000250|UniProtKB:P53534"
FT   MOD_RES         197
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CI94"
FT   MOD_RES         473
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CI94"
FT   MOD_RES         681
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11216"
SQ   SEQUENCE   843 AA;  96340 MW;  A10C12C5C052A2CA CRC64;
     MAKPLTDGER RKQISVRGLA GLGDVAEVRK SFNRHLHFTL VKDRNVATRR DYYLALAHTV
     RDHLVGRWIR TQQRYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQNACD EAIYQLGLDL
     EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA
     DDWLRYGNPW EKARPEYMLP VHFYGRVEHS PEGVRWLDTQ VVLAMPYDTP VPGYKNDTVN
     TMRLWSAKAP NDFKLHDFNV GGYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
     VAATLQDIIR RFKSSKFGCR DPVRTSFETF PDKVAIQLND THPALAIPEL MRILVDVEKV
     DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LDIIYAINQR HLDHVAALFP
     GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVRQSVFK DFYELEPEKF
     QNKTNGITPR RWLLLCNPGL AETIVERIGE GFLTDLSQLK KLLPLVGDEA LIRDVAQVKQ
     ENKVKFSAFL EKQYGVKVNP SSMFDVHVKR IHEYKRQLLN CLHVVTLYNR IKKDPTQAFV
     PRTVMIGGKA APGYHMAKKI IKLVTSIGNI VNHDPIVGDR LKVIFLENYR VSLAEKVIPA
     ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGAENLF IFGLRVEDVE
     ALDRKGYNAH EYYDRLPELR QAVDQINGGF FSPREPDCFK DVVNMLLNHD RFKVFADYEA
     YVACQARVDQ LYRNPKEWTK KVIRNIACSG KFSSDRTITE YAHDIWGAEP PALQTPPPSL
     PRD