ID   A0A0D9S0C3_CHLSB        Unreviewed;       695 AA.
AC   A0A0D9S0C3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   Name=PYGB {ECO:0000313|Ensembl:ENSCSAP00000014312.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014312.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000014312.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|RuleBase:RU000587}.
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:0000256|RuleBase:RU000587};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000587};
CC   -!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
CC       enzymatically active phosphorylase A. {ECO:0000256|ARBA:ARBA00038533}.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR   AlphaFoldDB; A0A0D9S0C3; -.
DR   STRING; 60711.ENSCSAP00000014312; -.
DR   Ensembl; ENSCSAT00000016397.1; ENSCSAP00000014312.1; ENSCSAG00000018301.1.
DR   eggNOG; KOG2099; Eukaryota.
DR   GeneTree; ENSGT00950000183148; -.
DR   OMA; WLKQANP; -.
DR   Proteomes; UP000029965; Unplaced.
DR   Bgee; ENSCSAG00000018301; Expressed in pituitary gland and 7 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   NCBIfam; TIGR02093; P_ylase; 1.
DR   PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11468:SF29; GLYCOGEN PHOSPHORYLASE, BRAIN FORM; 1.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000587};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU000587};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         533
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   695 AA;  79711 MW;  02F8DCE6C1A63286 CRC64;
     MATLGLAAYG YGIRYEFGIF NQKIVNGWQV EEADDWLRYG NPWEKARPEY MLPVHFYGRV
     EHTPDDVKWL DTQVVLAMPY DTPVPGYKNN TVNTMRLWSA KAPNDFKLQD FNVGDYIEAV
     LDRNLAENIS RVLYPNDNFF EGKELRLKQE YFVVAATLQD IIRRFKSSKF GCRDPVRTCF
     ETFPDKVAIQ LNDTHPALSI PELMRILVDV EKVDWDKAWE ITKKTCAYTN HTVLPEALER
     WPVSMFEKLL PRHLEIIYAI NQRHLDHVAA LFPGDVDRLR RMSVIEEGDC KRINMAHLCV
     IGSHAVNGVA RIHSEIVKQS VFKDFYELEP EKFQNKTNGI TPRRWLLLCN PGLADTIVEK
     IGEEFLTDLS QLKKLLPLVN DEAFIRDVAK VKQENKLKFS AFLEKEYKVK INPSSMFDVH
     VKRIHEYKRQ LLNCLHVITL YNRIKRDPAK AFVPRTVMIG GKAAPGYHMA KLIIKLVTSI
     GDVVNHDPVV GDRLKVFLEN YRVSLAEKVI PAADLSQQIS TAGTEASGTG NMKFMLNGAL
     TIGTMDGANV EMAEEAGAEN LFIFGLRVED VEALDRKGYN AREYYDRLPE LKQAVDQISS
     GFFSPKEPDC FKDVVNMLMH HDRFKVFADY EAYVQCQAQV DQLYRNPKGW TKKVIRNIAC
     SGKFSSDRTI TEYAREIWGV EPSDLQIPPP NIPRD
//