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Database: UniProt
Entry: E3RH37_PYRTT
LinkDB: E3RH37_PYRTT
Original site: E3RH37_PYRTT 
ID   E3RH37_PYRTT            Unreviewed;      1569 AA.
AC   E3RH37;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Glycogen debranching enzyme {ECO:0000256|ARBA:ARBA00020723};
DE            EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560};
DE            EC=3.2.1.33 {ECO:0000256|ARBA:ARBA00012778};
DE   AltName: Full=Glycogen debrancher {ECO:0000256|ARBA:ARBA00031477};
GN   ORFNames=PTT_07191 {ECO:0000313|EMBL:EFQ94963.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ94963.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ94963.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
CC   -!- FUNCTION: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-
CC       alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase
CC       in glycogen degradation. {ECO:0000256|ARBA:ARBA00003530}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in
CC         glycogen phosphorylase limit dextrin.; EC=3.2.1.33;
CC         Evidence={ECO:0000256|ARBA:ARBA00000927};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC         position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC         glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the glycogen debranching enzyme family.
CC       {ECO:0000256|ARBA:ARBA00025780}.
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DR   EMBL; GL533036; EFQ94963.1; -; Genomic_DNA.
DR   RefSeq; XP_003296942.1; XM_003296894.1.
DR   STRING; 861557.E3RH37; -.
DR   EnsemblFungi; EFQ94963; EFQ94963; PTT_07191.
DR   KEGG; pte:PTT_07191; -.
DR   eggNOG; KOG3625; Eukaryota.
DR   HOGENOM; CLU_001517_2_0_1; -.
DR   OrthoDB; 1427975at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0005980; P:glycogen catabolic process; IEA:InterPro.
DR   CDD; cd11327; AmyAc_Glg_debranch_2; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR010401; AGL/Gdb1.
DR   InterPro; IPR032788; AGL_central.
DR   InterPro; IPR029436; AGL_euk_N.
DR   InterPro; IPR032792; AGL_glucanoTrfase.
DR   InterPro; IPR032790; GDE_C.
DR   InterPro; IPR006421; Glycogen_debranch_met.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   NCBIfam; TIGR01531; glyc_debranch; 1.
DR   PANTHER; PTHR10569; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR10569:SF2; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   Pfam; PF06202; GDE_C; 1.
DR   Pfam; PF14701; hDGE_amylase; 1.
DR   Pfam; PF14702; hGDE_central; 1.
DR   Pfam; PF14699; hGDE_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          49..143
FT                   /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14699"
FT   DOMAIN          147..592
FT                   /note="Glycogen debranching enzyme glucanotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF14701"
FT   DOMAIN          753..997
FT                   /note="Glycogen debranching enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF14702"
FT   DOMAIN          1087..1542
FT                   /note="Glycogen debranching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06202"
SQ   SEQUENCE   1569 AA;  177331 MW;  D1E6006A6D9843C6 CRC64;
     MAVALPHHSK SSSPRKVVYL LPLTDYGCPD VAGTYIYMPP PTDPAYSICF QIQGTSSICR
     EGSLWVNIPA KGEKFERSNY REYKLQPNFT GLCEIEIPIH EANAFSFYTT YSPLPQWSFT
     DVASPKPTRT DTYYIDVCPS LRLKGEHLPV EAVCIFSTLS KFMGNYPTDW DNHLRGISQR
     GYNMVHFTPL MMRGSSNSPY SIYDQLKFDD AIFKNGEQDI ADMVQKMHSE FNLLAMTDVV
     WNHTANNSPW LEEHPEAGYN VDTAPHLRPA LELDTALLQF GQELAERGLP TTFNNEADLL
     KVMQGIKAHV LSKVKLWEYY VLDVERDTKA TMEAWISGQV NFVDGSFSEA GLRGLDAVKD
     WPLKQKADWL VEHALRGGDR MGERFRRTMD PNISASLLCA LFGRFDTRTS DKPDERAAQG
     TMTAIFNEVN LPFYREYDGD QSEILEQLFN RIKYVRIDAH GPKLGEVTEA NPLIETYFTR
     LPLNDTTKKH NPEALALVNN GWVWAADAMR DNAGPKSRAY LRREVIVWGD CVKLRYGNGP
     EDNPFLWEHM AKYTRLMAKY FQGFRIDNCH STPIHLAEYM LDQARSVNSN IMVCAELFTG
     SEEMDYKFCM KLGICALIRE AMQSWSTQEM SRLVHRHGGV PIGSFETDEV MNAAQATDGS
     DQTKPIIKKI KRSPVHALFM DCTHDNETPA QKRDARDTLP SAALVAMCDC ATGSVFGFDE
     VYPELIELVH EKRLYSSANS TGGPIKPQAG EGGIGGIRKI INEIHVKMGR EEYNETYIHH
     DNEYITVHRV NPHTRKGYFL IAHTAFPGYG NGNGGFGKTN LPGTQAKLIG AWNLEVDDSP
     ETKARIIGDK TTLRGLPSKT NNLQGVNIEL SGDDTTITIP DKFPPGSIAL FETWVPSAEH
     ADGLDKFVTS GARTAFSGVN LTDLNYILYR CEEEERDATD HKDGTYNIPG HGNLVYAGLQ
     GWWSVLRDIV NDNNLGHPLC NHLREGQWAL DYCLGRLEHI SQKDNYANIK GPAKWLKSKF
     DAIRKVPSYM LPRYFALVIQ TAYNAAVERA IELMGENVRE GNQFLKSLAL VSCQVTGYMN
     SASLWPEKSV PSMAAGLPHF AYDWARCWGR DITISARGLY MGTGRYDDAK EHIYAFASVL
     KHGMVPNLLG GGKNPRYNSR DSVWWFLQNI QDYTKIVPKG MELLKDQVKR RFLPYDDTWF
     AHTDKQAYSK SSTIEDVIQE ALQRHASGIE FREYDAGPNI DSQMKSEGFN IKIWTDWETG
     LIFGGNQWNC GTWMDKMGES EKAGSKGVPG TPRDGAPVEI IGMLYSTVRW CANMYEAGQF
     KYEGVTLDDG KKTVTYKEWA DLIKANFERC FYVPRSAEED SKYDVNSAIV NRRGIYKDLY
     RSGKEYEDYQ LRPNFPVTMT VAPDLFDPEH ALYALQMADR VLLGPQGMKT LDPSDLNYRG
     YYINSEDSTD FHTSKGRNYH QGPEWVWPTG FFLRALLKFD LKRRKTPEER IESYQQVTRR
     LAGCMKAIQE SPWAGLTELT NKDGAFCGDS CPTQSWSASC IIDLFQDARE YEMEGSGTGA
     SKSKKQPSS
//
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