ID A0A1L8F9Y5_XENLA Unreviewed; 856 AA.
AC A0A1L8F9Y5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=pygl.L {ECO:0000313|RefSeq:XP_018086036.1,
GN ECO:0000313|Xenbase:XB-GENE-17336338};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018086036.1};
RN [1] {ECO:0000313|RefSeq:XP_018086036.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018086036.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018086036.1};
RG RefSeq;
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|ARBA:ARBA00037413,
CC 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|ARBA:ARBA00036074};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733;
CC Evidence={ECO:0000256|ARBA:ARBA00036074};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR RefSeq; XP_018086036.1; XM_018230547.2.
DR AlphaFoldDB; A0A1L8F9Y5; -.
DR STRING; 8355.A0A1L8F9Y5; -.
DR PaxDb; 8355-A0A1L8F9Y5; -.
DR GeneID; 108698772; -.
DR KEGG; xla:108698772; -.
DR AGR; Xenbase:XB-GENE-17336338; -.
DR CTD; 108698772; -.
DR Xenbase; XB-GENE-17336338; pygl.L.
DR OMA; HCACSVA; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 108698772; Expressed in kidney and 19 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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:SF26; GLYCOGEN PHOSPHORYLASE, LIVER 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}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 856 AA; 98004 MW; 7F7B5CD148A927B2 CRC64;
MAKPLTDQEK RKQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATVR DYYFALAHTV
RDHLVGRWIR TQQYYYEKDP KRTYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDI
EELEEMEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IKDGWQIEEA
DDWLRHGNPW EKARPEFMLP VHFYGRVEST KTGPRWVDTQ VVLAMPYDTP VPGYMNNTVN
TMRLWSARAP NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAASLQDIIR RFKASKLGCR DSVRTAFDSF PDKVAIQLND THPALGIPEL MRIFLDIEKL
PWDKAWEITK KTFAYTNHTV LPEALERWPV DLVEKLLPRH LQIIYEINQK HLDKISSLFP
EDLGRIRRMS LIEEDGVKRI NMAHLCIVGS HAVNGVAKIH SDIVKNEVFK DFSELEPNKF
QNKTNGITPR RWLLLCNPGL AELIAEKIGE DYVKDLSQLT QLKKFVDDNS FIRDISKAKE
ENKLKFAQFL EKEYRMKINP ASMFDVHVKR IHEYKRQLLN CLHIITMYNR IKANPSKNFV
PRTVIIGGKA APGYHMAKMI IKLITSVGDI VNNDPAVGNK LKVLYLENYR VSLAEKVIPA
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENIF IFGMRVEDVA
ELDKKGYNAQ EYYEKLPELK KVIDQIKSGF FSPAKPDLFK EIVNMLFNHD RFKVFADYEA
YIKCQEKVSD LYKTPKEWTK MVIKNIAASG KFSSDRTIKE YALDIWGVEP SDLKIPPPNE
PRDVADDAGA AGKAKA
//
