ID A0A8C5PF44_9ANUR Unreviewed; 845 AA.
AC A0A8C5PF44;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
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:ENSLLEP00000018512.1};
OS Leptobrachium leishanense (Leishan spiny toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pelobatoidea; Megophryidae; Leptobrachium.
OX NCBI_TaxID=445787 {ECO:0000313|Ensembl:ENSLLEP00000018512.1, ECO:0000313|Proteomes:UP000694569};
RN [1] {ECO:0000313|Ensembl:ENSLLEP00000018512.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSLLEP00000018512.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) 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 -!- 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:0000256|ARBA:ARBA00045394}.
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|ARBA:ARBA00001275,
CC 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; A0A8C5PF44; -.
DR Ensembl; ENSLLET00000019240.1; ENSLLEP00000018512.1; ENSLLEG00000010829.1.
DR GeneTree; ENSGT00950000183148; -.
DR OrthoDB; 9215500at2759; -.
DR Proteomes; UP000694569; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:TreeGrafter.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR FunFam; 3.40.50.2000:FF:000005; Alpha-1,4 glucan phosphorylase; 1.
DR FunFam; 3.40.50.2000:FF:000153; Alpha-1,4 glucan phosphorylase; 1.
DR FunFam; 3.40.50.2000:FF:000197; Alpha-1,4 glucan 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000694569};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 683
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 845 AA; 97163 MW; 241AE40D68DF111F CRC64;
MATPLTDSDK RKQISVRGIA GLGDVAEVRK SFNRHLHFTL VKDRNVSTPR DYYFALAHTV
RDHLVGRWIR TQQYYYEKDP KRIYYLSLEF YMGRTLQNTM LNLGLQHACD EAVYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQR IMNGWQVEEA
DDWLRYGNPW EKARPEYMLP VHFYGRVEHT AEGTKWVDTQ IVLAMPYDTP VPGYKNNTVN
TMRLWSAKAP NEFNLQEFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCR DPVRTAFDTF PDKVAIQLND THPALAIPEL MRILVDIETL
DWDKAWDITK RTCAYTNHTV LPEALERWPV HLFEKLLPRH LEIIYAINQK HLDVRTVAVI
YPGDMDRLRR MSVIEEGDCK RINMAHLCVI GAHAVNGVAR IHSEIVKNTV FKDFYDLEPS
KFQNKTNGIT PRRWLMLCNP GLSDILAEKI GEDFVTDLSQ LKKLLDFVDD EMFVHDVAKV
KQENKLKFST YLEAQYKVKI NPSSMFDVQV KRIHEYKRQL LNCLHIITLY NRIKKDPSKT
FVPRTVMIGG KAAPGYHMAK MIIKLITSVG SIINNDPVIG DRLKVIYLEN YRVSLAEKVI
PASDLSQQIS TAGTEASGTG NMKFMLNGAL TIGTMDGANV EMAEEAGEEN LFIFGMRVED
VEALDKKGYN AKEYCDRIPE LRQAMDQIRD GHFSPREPDL FKDVVNMLMH NDRFKVFADY
EAYISCQEKV DRLYMNPREW TRKVIRNIAC SGKFSSDRTI SEYATEIWGV EPSAVKIPPP
NIPRD
//
