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Database: UniProt
Entry: F8MYW4_NEUT8
LinkDB: F8MYW4_NEUT8
Original site: F8MYW4_NEUT8 
ID   F8MYW4_NEUT8            Unreviewed;      1566 AA.
AC   F8MYW4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=NEUTE1DRAFT_149613 {ECO:0000313|EMBL:EGO51962.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO51962.1};
RN   [1] {ECO:0000313|EMBL:EGO51962.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO51962.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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; GL891382; EGO51962.1; -; Genomic_DNA.
DR   RefSeq; XP_009855606.1; XM_009857304.1.
DR   GeneID; 20827134; -.
DR   KEGG; nte:NEUTE1DRAFT149613; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_149613; -.
DR   HOGENOM; CLU_001517_2_1_1; -.
DR   OrthoDB; 1427975at2759; -.
DR   Proteomes; UP000008065; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          41..142
FT                   /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14699"
FT   DOMAIN          146..588
FT                   /note="Glycogen debranching enzyme glucanotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF14701"
FT   DOMAIN          755..999
FT                   /note="Glycogen debranching enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF14702"
FT   DOMAIN          1089..1545
FT                   /note="Glycogen debranching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06202"
FT   REGION          641..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1566 AA;  176309 MW;  966E43A479B820CB CRC64;
     MIPRTMVSNE VYLLPLKDDG SPDVPGEYIY IAPKSKDPVT IRFAIEGTSS ICSHGSLWVN
     IPEHGEQFQR NKFREYKLVP DFNRTLEISI PIYEAGAYAF YTTYAELPDL ASSLVNADGT
     VTKATQKKTP LYYIDVAPRL SLDGQPLPLP ALSIFSIISK FMGKYPTDWE RHLRGISDRG
     YNMIHFTPLQ VRGASNSPYS LYDQLGWDPA CFPAGEPDVQ KMVESLEKNH SLLSLTDIVL
     NHTAHNSEWL LEHPEAGYNL TTAPWLESAY LLDTKLLELG TRLEELGLPT ELKDVDDLVK
     IMDAIKKEVI AEIRLWEYYT LDVERDADAA VKSWAANDID FPQASVGAGG IDSLHSATPK
     EQADFLIQHG LQNMDYLGER FRRRANPKVA AALLSAIFGR YEGETKDTAD QAAARTKIVD
     ILEIVNVPFY KEYDDEVAEI LQQLFNRIKY VRLDDHGPKL GPINAENPLI ETYFTRLPVN
     EKTKKHKKED LVLANNGWVW GGNALVDNAG PDSRVYLRRE VIVWGDCTKL RYGSGPEDSP
     WLWEHMTKYA RMLAKYFAGF RIDNCHSTPL HVAEHILDEA RRVRPDLYVV AELFTGSEEM
     DYVFVKRLGI SALIREAMQA WSTGELSRLV HRHGGRPIGS FEVDEVSSNE GRSSSISGTN
     GDGVYTREVI RRIRPVPVQA LFMDCTHDNE VPAQKRDARD TLPNAALVAM CASATGSVMG
     YDEIYPKLVD LVGETRLYTF EASKAPVKTG EGKDGIAGVK KLLNQIHTLM GMDGYDETHI
     HHEDEYVTVH RVHQESRKGY FLIAHTAFPG YGNGNGAFNP VHLTGTKARH LGSWMLEVDA
     SKEAVEEVLG DKKHLRGLPS RLVGLPGVRM EVKGQDTIIT VREKFPPGSI ALFETWIPAA
     EHSSGLDNFV TSGAKAAMDE LDLVDLNFLL YKCEPEERDA SEGQDGTYDI PGHGKIVYAG
     LQGWWSILKD VIKDNNLAHP LCQHLRDGQW ALDYIVGRLE RASKKEDFRR LAKPAQWLKE
     RFDAIRPIPS FLLPRYFGLV LRTAYNAAFE RGISLMNNNV IKGQWFLQSL AMVSVQMTGL
     VKSASLYPNR LVPSLAAGLP HFAVEWARCW GRDVFISLRG LYLGTGRYAE AREHIHAFAS
     VLKHGMIPNL LGSGNNPRYN SRDSVWFFLQ CIQDYTRLVP DGLSILDDKV KRRFLPYDDT
     YFDVDDERAY SKESTIAEII QEVFQRHAEG MKYREANAGP NLDMQMSDAG FNQEIKVDWS
     NGFIFGGNQA NCGTWMDKMG ESERAGSKGV PGTPRDGAAV EITGMLYSNL KWAASLNEAG
     KFKHSSVRKS DGTEITLKDW AALIKDNFER CYFVPISPDE DSKYDVNPAI INRRGIYKDL
     YRSGKEYEDY QLRSNFPIAM TCAADLFVPE HAMHALWVAD AALRGPTGMA TLDPSDMNYR
     PYYNNSEDSD DFATSKGRNY HQGPEWLWPT GFFLRALLKF DLMRRGRDDA EGRTEAFQQV
     TRRLIGCKEM IQRSPWAGLT ELTNKNGEEC HDSSPTQAWS AGCLIDLYMD AAEEQAKLEK
     HSLPLR
//
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