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Database: UniProt
Entry: G3JE01_CORMM
LinkDB: G3JE01_CORMM
Original site: G3JE01_CORMM 
ID   G3JE01_CORMM            Unreviewed;       953 AA.
AC   G3JE01;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   ORFNames=CCM_04198 {ECO:0000313|EMBL:EGX92826.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX92826.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX92826.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX92826.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126401; EGX92826.1; -; Genomic_DNA.
DR   RefSeq; XP_006669409.1; XM_006669346.1.
DR   AlphaFoldDB; G3JE01; -.
DR   STRING; 983644.G3JE01; -.
DR   GeneID; 18166221; -.
DR   KEGG; cmt:CCM_04198; -.
DR   VEuPathDB; FungiDB:CCM_04198; -.
DR   eggNOG; KOG2099; Eukaryota.
DR   HOGENOM; CLU_010198_1_1_1; -.
DR   InParanoid; G3JE01; -.
DR   OMA; WLKQANP; -.
DR   OrthoDB; 5473321at2759; -.
DR   Proteomes; UP000001610; 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:0005975; P:carbohydrate 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:SF3; GLYCOGEN PHOSPHORYLASE; 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   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:UP000001610};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         802
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   953 AA;  107896 MW;  81A23DEC909AB13B CRC64;
     MPMPTPAAPV RFCHFTFEPP PRARACRYFL LKLSTPPPLL HPLAYLHRLP SPLLVFLSAL
     SPKQHLQHPY PSHQPTMASE RPLPIRQRRP STSAPIVDIQ GSVGPAGVSR PKHKRTFTGF
     GAGEIKTSIP EPQRAAWEKH AIKSFEDKDG FEREVVRHVE TTLARSLFNC DEKAAYAATS
     LAFRDRLITD WNKTQQQQTF SDTKRVYYLS LEFLMGRALD NAMLNVGHKD IAKAGLADLG
     FRIEDIITQE NDAALGNGGL GRLAACFLDS LASLNYPAWG YGLRYRYGIF KQEIIDGYQV
     EVPDYWLDFN PWEFPRHDIQ FYGTVRKSTD AKGKTVSVWD GGEVVQAVAY DVPIPGYATP
     TTNNLRLWSS KASGGEFDFQ KFNNGDYESS VADQQRAETI SAVLYPNDNL ERGKELRLKQ
     QYFWVAASLY DIVRRFKKTN RAWAEFPEQV AIQLNDTHPT LAIVELQRIL IDVEGLEWNQ
     AWDIVTNTFG YTNHTVLPEA LEKWHVGLMQ NLLPRHLQII FDINLFFLQQ VEKKFPDDRD
     MLRRVSIVEE SQPKMIRMAY LAIVGSHKVN GVAELHSDLI QTTIFKDFVA IYGPDKFTNV
     TNGVTPRRWL HQANPRLSEL IASKCGGNGF LTDLTNLSKL EQFVGDKGFR KEWAEIKYAN
     KVRLAKHIKK TLGVTVNPAS LFDIQVKRIH EYKRQQMNIF GVIHRYLTLK KMSPTERKKQ
     LPRVSIFGGK AAPGYWMAKQ IIHLINSVGS VVNNDGDIGD LLKVIFLEDY NVSKAEIICP
     ASDISEHIST AGTEASGTSN MKFVLNGGLI IGTCDGANIE ITREVGENNI FLFGNLSEDV
     EDLRHAHTYG SHAIDSDLDA VFEEIEKGTF GTPHDFGALV AAVRQHGDYY LVSDDFHSYI
     ETQRLVDESY RNQDEWVSKC ITAVARMGFF SSDRCINEYA ESIWNIEPLP IRE
//
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