ID A0A059D8I8_EUCGR Unreviewed; 957 AA.
AC A0A059D8I8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=EUGRSUZ_B03166 {ECO:0000313|EMBL:KCW86515.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW86515.1};
RN [1] {ECO:0000313|EMBL:KCW86515.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW86515.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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|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 -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; KK198754; KCW86515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059D8I8; -.
DR STRING; 71139.A0A059D8I8; -.
DR EnsemblPlants; KCW86515; KCW86515; EUGRSUZ_B03166.
DR Gramene; KCW86515; KCW86515; EUGRSUZ_B03166.
DR InParanoid; A0A059D8I8; -.
DR OMA; AFNTGDH; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
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:SF27; ALPHA-1,4 GLUCAN PHOSPHORYLASE L-2 ISOZYME, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 2.
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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 520..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 802
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 957 AA; 108464 MW; 75B30E60B817E756 CRC64;
MAASPFSANC TLPKSIAHSK SVHSSKGCDF GARVTKLFFL QHPRLVCSRR NFYVRNVASD
QKQELKEPLA DEVPGTLDTS VPDSASIASS IKYHAEFTPS FSPEKFELPK AYFATAESVR
DTLIINWNAT YHYYEKLNVK QAYYLSMEYL QGRALLNAIG NLELSGAYAE ALRKLGHNLE
DVASQERDAA LGNGGLGRLA SCFLDSLATL NYPAWGYGLR YKYGLFKQNI TKDGQEEVAE
NWLEMGNPWE IVRNDVSYPV KFYGEVISGP DGSKEWVGGE NIVALAYDVP VPGYKTKTTI
NLRLWSTKVA SEEFDLCAFN AGDHATAYAA LKNAEKICYI LYPGDESIEG KTLRLKQQYT
LCSASLQDII TRFERRSGDV VDWGKLPEKV AVQMNDTHPT LCIPELIRIL MDVKKLSWEE
AWNITKRTVA YTNHTVLPEA LEKWSLELMQ DLLPRHVEII KKIDEELVQT IIDEYGQEDL
DLLQQKLKEM RILANVELPG TVLELLVKPE EDPIEEVDTA IEESKLVDEV DQPEEEDDPE
EKKVIPEPDP ELPKMVRMAN LCVAGGFAVN GVAEIHSEIV KEEVFNDFFK LWPEKFQNKT
NGVTPRRWIR FCNPNLSEII TKWTGTDDWT INTEKLAILR KFADNEDLQS EWREAKRRNK
IKVAAFLKEK TGYVVSPDAM FDVQVKRIHE YKRQLLNILG IVHRYKKMKE MTPEERKTRF
VPRVCIFGGK AFATYVQAKR IVKFITDVGA TVNHDPEIGD LLKVVFVPDY NVSVAEVLIP
GSELSQHIST AGMEASGTSN MKFAMNGCVL IGTLDGANVE IREEVGEDNF FLFGARAPEI
AGLRKERAEG KFVPDARFEE VKAYVRSGVF GPYNYEELMG SLEGNEGYGR ADYFLVGKDF
PSYMECQEKV DEAYRDQKQR WTKMSILNTA GSYKFSSDRT IHEYARDIWG IEPVVLP
//