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Database: UniProt
Entry: A0A093Y8C9_9PEZI
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ID   A0A093Y8C9_9PEZI        Unreviewed;      1539 AA.
AC   A0A093Y8C9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=O988_02817 {ECO:0000313|EMBL:KFY01276.1};
OS   Pseudogymnoascus sp. VKM F-3808.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFY01276.1, ECO:0000313|Proteomes:UP000029329};
RN   [1] {ECO:0000313|EMBL:KFY01276.1, ECO:0000313|Proteomes:UP000029329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFY01276.1,
RC   ECO:0000313|Proteomes:UP000029329};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY01276.1}.
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DR   EMBL; JPJR01000449; KFY01276.1; -; Genomic_DNA.
DR   STRING; 1391699.A0A093Y8C9; -.
DR   HOGENOM; CLU_001517_2_1_1; -.
DR   Proteomes; UP000029329; 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:UP000029329};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          42..137
FT                   /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14699"
FT   DOMAIN          140..577
FT                   /note="Glycogen debranching enzyme glucanotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF14701"
FT   DOMAIN          732..976
FT                   /note="Glycogen debranching enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF14702"
FT   DOMAIN          1054..1522
FT                   /note="Glycogen debranching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06202"
FT   REGION          1410..1437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1419..1434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1539 AA;  172780 MW;  D8F38FCD1BDEFCAF CRC64;
     MAPNTSNAAK EVYLLPLLDD GSPDVPGGYI YLEPTSAEPI IVRFAIEGTS SICRHGSLWV
     NINAPGEPFK RDAFREFKLE PDFNRTLEID IPIHSSGAFA FYTTYSPLPD LDDAGSKPSE
     PTKTPLYYID VAPRLSLGEK QLPMAALSLI SVLSKFMGKY PTDWQKHLRG ISERGYNMIH
     FTPLQVRGHS NSPYSIADQL GWDPECFPGG EKDIAQLVNV MEKEHGLLGL TDVVWNHTAD
     NSTWLQEHPE VGYNMSTAPW LESALQLDTE LLKFGRELEK LGLPTDIKTV EDLLLIMDGI
     KTKVIGGLKL WEYYAIDVKR DVDAAVDAWV SGNVKAPAEG FGSKDASPKE HAKFIVDKAM
     LGTDRLGERY RRKVDPAIAA ALLTEWHGKF NGNASNPADS EEVRSHTSKI FDEVNLPFYK
     EYDEDIAEVL EQIFNRVKYV RLDDHGPKLG PINDKNPLIE SYFTRLPQNA TTKKHKQEDL
     ALVNNGWIWA ANALVDNAGP NSRAYLRREV IVWGDCVKLK YGDGPQDSPY LWERMANYTR
     LMAKYFTGLR IDNAHSTPLH VAEYLLDEAR RVRPDLFVVA ELFTGSEEMD YVFVKRLGIN
     GLIREAMQAW NTGELSRLVH RHGGRPIGSF EVDEISGNDA KESTEIVRKI KQTPVRALFM
     DCTHDNEVPA QKRDARDTLP NAALVYMCAS ATGSVFGYDE IYPKIIDLVH ETRLYTSHSS
     EKPVDIKDGD GGIGGVRKLL NQIHILMGLD GYEETHIHHD DQYVTVHRVH PEFRKGYFLI
     AHTAFPGYKN GNGPFSPVHL TGTKANHLGS WMLEVDDSEE ARKAASEDKQ YLKGLPSKVT
     SVPGIKMESK DDETVITMGD KFPPGSIALF ETWIPAAEHA SGLDTFVTSG AKEAFSKVDL
     VDLNFIMYRC EGEELDSSDG KDGVYDIPSH GKLVYAGLEG WWSVLKKVIN ENDLAHPLAQ
     HLRSGQWALD YTVGRLQRKS KEEAFERLQA PALWLQERFD AIRKLPSFLL PRYFGLIIKT
     AYSAGFDRGV ELMSENVQKG QWFMKSLAMV SVQQTGFVKS ASLYPKRAVP SLAAGLPHFA
     VEWARCWGRD VFISARGLLL GTGRYAEARE HIIAFASVVK HGMIPNLLSS GNLPRYNSRD
     SVWFFLQTIQ DYTKIVPNGH DLLQEKISRR FLPYDDTYFE SDDPRAYSKT STLEDIIQEI
     FQRHASGMSF REANAGPKLD MQMKPEGFQI DIKVDWNTGI IFGGSQDNCG TWMDKMGESE
     KAGTRGVPGT PRDGAAVEIT GLSYSALKWV SQLNKNGKFK YSGVNTSDSS IKEISFADWA
     SKIRDNFERC YYVPASSKED ANYDVNPAII NRRGIYKDLY KSGKEYEDYQ LRPNFPIAMT
     VSPDLFDDKH ALGALFIADK ALRGPTGMAT LDPSDLNYRP DYHNSEDSTD KATSKGRNYH
     QGPEWLWPTG FFLRALLAFD LKRRDTPEGR TEAFQQVTRR LADSKKAIVE SEWAGLTELT
     NKNGSFCADS SPTQAWSAGC FIDLYHDAAQ YDISQLQEK
//
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