ID U4UTB8_DENPD Unreviewed; 851 AA.
AC U4UTB8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=D910_10652 {ECO:0000313|EMBL:ERL93360.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL93360.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL93360.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
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 -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; KB632354; ERL93360.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UTB8; -.
DR STRING; 77166.U4UTB8; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
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:SF13; GLYCOGEN PHOSPHORYLASE, MUSCLE 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 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:UP000030742};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 682
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 851 AA; 97760 MW; B82CE8955428BA97 CRC64;
MSVPQSDVER RKQISVRGIA EVGDVTEIKK TFNRHVHYTL VKDRNVATPR DYYFALAHTV
RDHLVSRWIR TQQHYYEVDP KRVAYLSLEF YMGRTLSNTM INLGIQSPCD EALYQLGLDI
EELEEMEEDA GLGNGGLGRL AACFLDSMAT LGMAAYGYGI RYEYGIFAQR LVNGEQQEEP
DDWLRFGNPW EKARPEYMLP VNFYGKVIET PEGKKKWVDT QVVFALPYDN PVPGYRNNVV
NTLRLWSAKS PVDFDLKFFN DGDYIQAVLD RNLAENISRV LYPNDNFFEG KELRLKQEYF
MVAATLQDIV RRFKSAKFGS KEATRNDFDQ FPDKVAIQLN DTHPSLAIPE LMRLLVDVEG
LDWDKAWDIT RRTCGYTNHT VLPEALERWA VSHLQNILPR HLDIIYKINF HHLQDVEKKW
PGNLDKMRTM SLIEEDGAKR VNMAHLSIVG SHAVNGVAQL HSDIIKAGLF RDFYELNPEK
FQNKTNGVTP RRWVLLCNPG LSDLISERFG EDWIIHLEQL QQLRPLAKDP AFQRAVMKVK
QENKLRLAQL LEKDYGVKVN PASMFDVHVK RIHEYKRQLL NCMHIITMYN RIKKNPSAKF
TPRTVMIGGK AAPGYYTAKK IIKLINYVAN VVNNDPIVGD KLKVIYLENY RVTLAEKIIP
AADLSEQIST AGTEASGTGN MKFQLNGALT IGTLDGANVE MAEEMGRENI FIFGMTADEV
EALQRKGYNA YDYYNANPEL KQVVDQMQNG FFSPSNPDEF KDLADILLKY DRFFLLADYD
SYIKKQDEVS SIYQNQSKWL EMAIMNIATS GKFSSDRTII EYGRDIWGVE PNYEKLPDPA
VPKELALKEE Q
//
