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}.
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; 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
//