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Database: UniProt
Entry: A0A059AEY0_EUCGR
LinkDB: A0A059AEY0_EUCGR
Original site: A0A059AEY0_EUCGR 
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}.
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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
//
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