ID A0A059AEY0_EUCGR Unreviewed; 962 AA.
AC A0A059AEY0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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_J01374 {ECO:0000313|EMBL:KCW51920.1};
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:KCW51920.1, ECO:0000313|Proteomes:UP000030711};
RN [1] {ECO:0000313|Proteomes:UP000030711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BRASUZ1 {ECO:0000313|Proteomes:UP000030711};
RX PubMed=24919147; DOI=10.1038/nature13308;
RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA van der Merwe K., Singh P., van Jaarsveld I., Silva-Junior O.B.,
RA Togawa R.C., Pappas M.R., Faria D.A., Sansaloni C.P., Petroli C.D.,
RA Yang X., Ranjan P., Tschaplinski T.J., Ye C.Y., Li T., Sterck L.,
RA Vanneste K., Murat F., Soler M., Clemente H.S., Saidi N., Cassan-Wang H.,
RA Dunand C., Hefer C.A., Bornberg-Bauer E., Kersting A.R., Vining K.,
RA Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.E., Liston A.,
RA Spatafora J.W., Dharmwardhana P., Raja R., Sullivan C., Romanel E.,
RA Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA Grima-Pettenati J., Salse J., Van de Peer Y., Rokhsar D.S., Schmutz J.;
RT "The genome of Eucalyptus grandis.";
RL Nature 510:356-362(2014).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK198762; KCW51920.1; -; Genomic_DNA.
DR RefSeq; XP_010032532.1; XM_010034230.2.
DR RefSeq; XP_018719565.1; XM_018864020.1.
DR AlphaFoldDB; A0A059AEY0; -.
DR STRING; 71139.A0A059AEY0; -.
DR EnsemblPlants; KCW51920; KCW51920; EUGRSUZ_J01374.
DR Gramene; KCW51920; KCW51920; EUGRSUZ_J01374.
DR eggNOG; KOG2099; Eukaryota.
DR InParanoid; A0A059AEY0; -.
DR OMA; WLKQANP; -.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000030711; Unassembled WGS sequence.
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:SF28; ALPHA-GLUCAN PHOSPHORYLASE 1; 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 Reference proteome {ECO:0000313|Proteomes:UP000030711};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 808
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 962 AA; 108725 MW; B78965AFEE7581B8 CRC64;
MATSQLAATT PPLPSGDERF PRRQDQRRLL GSGLGEKKLA LLFRTRDARP LRTRRPSAVK
SVSGESKQRL KDSPLEEEPG SPSPLKPDAA SIASSIKYHA EFTAPFSPDQ FELPKAFFAT
AQSVRDALII NWNATYDYCE KLNVKQAYYL SMEFLQGRAL LNAIGNLELT GAYAEALSKL
GHDLENVAAQ EADAALGNGG LGRLASCFLD SLATLNYPAW GYGLRYRYGL FKQRITKDGQ
EEVAESWLEM GNPWEVVRND VSYPVKFYGK VVSGSDGKRR WIGGEDIRAA AFDVPIPGYK
TKNTINLRLW STKVLSEEFD LSAFNAGEHT KANEALSNAE KICYILYPGD ESIEGKILRL
KQQYTLCSAS LQDIIARFEK LSGKHVKWED FPEKVAVQMN DTHPTLCIPE LMRILMDVKG
LSWKEAWNIT RRTVAYTNHT VLPEALEKWS LELMQKLLPR HVEIIEMIDE ELVGTIIAEC
GTENPGLLEK KLKEMRILEN VDLPPAFAEL IKPEEDPVAS SEKEPETSKE LDINLEDEPH
NLQAQENNEE LPEPEPEPPK MVRMANLCVV CSHAVNGVAE IHSEIVKKEV FHEFFKLWPE
KFQNKTNGVT PRRWIPFCNP ELSKIITRWI GTEDWILHTD KLAELRKFAD NEDLQTQWRA
AKRSNKMKVV RFLKETTGYV VSPEAMFDIQ VKRIHEYKRQ LLNILGIVYR YKKMKAMNSA
ERTAKFVPRV CIFGGKAFAT YVQAKRIVKF ITDVAATINH DPEIGNLLKV IFVPDYNVSV
AELLIPASEL SQHISTAGME ASGTSNMKFA MNGCVLIGTL DGANVEIRQE VGEDNFFLFG
AQAHEIAGLR KERAEGKFVP DPRFEEVKAF VKSGVFGPYN YDELIESLEG NEGFGRGDYF
LVGKDFPSYI ECQEEVDEAY RDEKRWTRMS ILNTAGSHKF SSDRTIHEYA RDIWNIAPVG
VP
//