ID Q5BZM8_SCHJA Unreviewed; 167 AA.
AC Q5BZM8;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 2.
DT 22-FEB-2023, entry version 43.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
DE Flags: Fragment;
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182 {ECO:0000313|EMBL:AAX27147.2};
RN [1] {ECO:0000313|EMBL:AAX27147.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16617374; DOI=10.1371/journal.ppat.0020029;
RA Liu F., Lu J., Hu W., Wang S.Y., Cui S.J., Chi M., Yan Q., Wang X.R.,
RA Song H.D., Xu X.N., Wang J.J., Zhang X.L., Zhang X., Wang Z.Q., Xue C.L.,
RA Brindley P.J., McManus D.P., Yang P.Y., Feng Z., Chen Z., Han Z.G.;
RT "New perspectives on host-parasite interplay by comparative transcriptomic
RT and proteomic analyses of Schistosoma japonicum.";
RL PLoS Pathog. 2:268-281(2006).
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|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; AY811258; AAX27147.2; -; mRNA.
DR AlphaFoldDB; Q5BZM8; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
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:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR000811; Glyco_trans_35.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000587};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT NON_TER 167
FT /evidence="ECO:0000313|EMBL:AAX27147.2"
SQ SEQUENCE 167 AA; 19062 MW; C5E733C4C9822336 CRC64;
MVYFLSMEFF MGRTLKNTML NVDVAEALDE SMYQLGLDIE ELEEMECDAG LGNGGLGRLA
ACFLDSMATI GLPAYGYGIR YENGAFHQKI KDGWQIEEPD EWLLYGNPWE KERPECTRIV
QFYGRVVRND LDQCEWVDTA TICALPYEVP IPGYCNQTCN TLRLWAA
//
