ID   PYGB_PONAB              Reviewed;         843 AA.
AC   Q5R5M6;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Glycogen phosphorylase, brain form;
DE            EC=2.4.1.1;
GN   Name=PYGB;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR860831; CAH92940.1; -; mRNA.
DR   RefSeq; NP_001126731.1; NM_001133259.1.
DR   AlphaFoldDB; Q5R5M6; -.
DR   SMR; Q5R5M6; -.
DR   STRING; 9601.ENSPPYP00000012049; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   GeneID; 100173733; -.
DR   KEGG; pon:100173733; -.
DR   CTD; 5834; -.
DR   eggNOG; KOG2099; Eukaryota.
DR   InParanoid; Q5R5M6; -.
DR   OrthoDB; 240595at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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   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_0000188537"
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;  96616 MW;  4FB84484C04D0FCB CRC64;
     MAKPLTDSEK RKQISVRGLA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYLFALAHTV
     RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQNACD EAIYQLGLDL
     EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA
     DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PDGVKWLDTQ VVLAMPYDTP VPGYKNNTVN
     TMRLWSAKAP NDFKLQDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
     VAATLQDIIR RFKSSKFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL MRILVDVEKV
     DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LEIIYAINQR HLDHVAALFP
     GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVKQSVFK DFYELEPEKF
     QNKTNGITPR RWLLLCNPGL ADTIVEKIGE EFLTDLSQLK KLLPLVNDEV FIRDVAKVKQ
     ENKLKFSAFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVVTLYNR IKRDPAKAFV
     PRTVMIGGKA APGYHMAKLI IKLVTSIGDV VNHDPVVGDR LKVIFLENYR VSLAEKVIPA
     ADLSQQISTA GAEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGAENLF IFGLQVEDVE
     ALDRKGYNAR EYYDHLPELK QAVDQISSGF FSPKEPNCFK DIVNMLMHHD RFKVFADYEA
     YMQCQAQVDQ LYRNPKEWTK KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNV
     PRD