ID B2VZS2_PYRTR Unreviewed; 1567 AA.
AC B2VZS2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=PTRG_02912 {ECO:0000313|EMBL:EDU45435.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU45435.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231616; EDU45435.1; -; Genomic_DNA.
DR RefSeq; XP_001933245.1; XM_001933210.1.
DR STRING; 426418.B2VZS2; -.
DR EnsemblFungi; EDU45435; EDU45435; PTRG_02912.
DR GeneID; 6341136; -.
DR eggNOG; KOG3625; Eukaryota.
DR HOGENOM; CLU_001517_2_0_1; -.
DR InParanoid; B2VZS2; -.
DR OMA; YEEGHVH; -.
DR OrthoDB; 1427975at2759; -.
DR Proteomes; UP000001471; 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:UP000001471};
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 1567 AA; 176945 MW; 16222688BE2AF527 CRC64;
MAVALPHHSK SSSPRKVVYL LPLTDYGCPD VAGTYIYMPP PTDPAYSICF QIQGTSSICR
EGSLWVNIPA KGKKFERSNY REYKLQPNFT GLCEIEIPIY EANAFSFYTT YSPLPQWSFT
DVASPKPTRT DTYYIDVCPS LRLKGEHLPV EAVCIFSTLS KFMGNYPTDW DNHLRGIGQR
GYNMVHFTPL MMRGSSNSPY SIYDQLKFDD AIFKNGEQDI ADMVQKMHSE FNLLAMTDVV
WNHTANNSPW LEEHPEAGYN VDTAPHLRPA FELDTALLQF GQELGERGLP TTFNNEADLL
KVMQGIKAHV LSKVKLWEFY VLDVERDTKA TMEAWISGQV NFVDGSFSEA GLRGLDAVKD
WPLKQKADWL VEHALRGGDR MGERFRRTMD PNISASLLCA LFGRFDTRTS DKPDERAAQG
TMTAIFNEVN LPFYREYDGD QSEILEQLFN RIKYVRIDAH GPKLGEVNDA NPLIETYFTR
LPLNDTTKKH NPEALALVNN GWVWAADAMR DNAGPKSRAY LRREVIVWGD CVKLRYGNGP
EDNPFLWEHM AKYTRLMAKY FQGFRIDNCH STPIHLAEYM LDQARSVNSN IMVCAELFTG
SEEMDYKFCM KLGICALIRE AMQSWSTQEM SRLVHRHGGV PIGSFETDEV MNAAQATDGA
DQTKPIIKKI KRSPVHALFM DCTHDNETPA QKRDARDTLP SAALVAMCDC ATGSVFGFDE
VYPELIELVH EKRLYSSANS TGGPIKPQAG EGGIGGIRKI INEIHVKMGK EEYNETYIHH
DNEYITVHRV NPHTRKGYFL IAHTAFPGYG NGNGGFGKTN LPGTQAKLIG AWNLEVDDSP
ETKARIIGDK TTLRGLPSKT NNLQGVNIES SGDDTTITIP DKFPPGSIAL FETWVPSAEH
ADGLDKFVTS GGRAAFSGVN LTDLNYILYR CEEEERDATD HKDGTYNIPG HGNLVYAGLQ
GWWSVLRDIV NDNNLGHPLC NHLREGQWAL DYCLGRLEHI SQKEKYANIK GPAKWLKSKF
DAIRKVPSYM LPRYFALVIQ TAYNAAVDRA IELMGENVRE GNQFLKSLAL VSCQVTGYMN
SASLWPEKSV PSMAAGLPHF AYDWARCWGR DITISARGLY MGTGRYADAK EHIFAFASVL
KHGMVPNLLG GGKNPRYNSR DSVWWFLQNI QDYTKIVPNG MELLKEQVKR RFLPYDDTWF
AHTDKQAYSK SSSIEDVIQE ALQRHASGIE FREYDAGPNI DSQMKSEGFN IKIWTDWETG
LIFGGNQWNC GTWMDKMGES EKAGSKGVPG TPRDGAPVEI IGMLYSTVRW CANMYEAGQF
KYEGVTLDDG KKTVTYKEWA DLIKANFERC FYVPRSAEED SKYDVNSAIV NRRGIYKDLY
RSGKEYEDYQ LRPNFPVTMT VAPDLFEPEH ALYALQMADR VLLGPQGMKT LDPSDLNYRG
YYINSEDSTD FHTSKGRNYH QGPEWVWPTG FFLRALLKFD LQRRKTPEER IESYQQVTRR
LAGCMKAIQE SPWAGLTELT NKDGAFCGDS CPTQSWSASC IIDLFQDARE YEMEGSGTGA
SKKESSS
//
