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Database: UniProt
Entry: A0A179FU19_METCM
LinkDB: A0A179FU19_METCM
Original site: A0A179FU19_METCM 
ID   A0A179FU19_METCM        Unreviewed;      1558 AA.
AC   A0A179FU19;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=VFPPC_04933 {ECO:0000313|EMBL:OAQ68738.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ68738.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ68738.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ68738.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ68738.1}.
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DR   EMBL; LSBJ02000003; OAQ68738.1; -; Genomic_DNA.
DR   RefSeq; XP_018145588.1; XM_018284196.1.
DR   STRING; 1380566.A0A179FU19; -.
DR   GeneID; 28848190; -.
DR   KEGG; pchm:VFPPC_04933; -.
DR   OrthoDB; 1427975at2759; -.
DR   Proteomes; UP000078397; Chromosome 3.
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:UP000078397};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          41..141
FT                   /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14699"
FT   DOMAIN          145..588
FT                   /note="Glycogen debranching enzyme glucanotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF14701"
FT   DOMAIN          754..998
FT                   /note="Glycogen debranching enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF14702"
FT   DOMAIN          1081..1542
FT                   /note="Glycogen debranching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06202"
SQ   SEQUENCE   1558 AA;  175024 MW;  4B68934C55216A5C CRC64;
     MSPGTMTTTE VYLLPLNDDG SPDVERQYIY IAPPSNDPVT LRFSIEGTSS ICRNGSLWVN
     IPKKGKEFRR DSFREFKLTP DFNRSIEISI QIHQPGAYAF YTTYAELPSL EPHLSEDSSQ
     KAVELKKTPV YYIDVAPRLR LDGRPLPLPA LSVFSVISKF MGKYPTDWDS HLRGISDRGY
     NMIHFAPLQV RGSSNSPYSL YDQLGWDPEC FPHGERDVEK LVASLERDHS LLSLTDIVLN
     HTAHNTKWLQ EHPEAGYNLS TAPWLESAYE LDSKLLELSA NLASLGLPVH PKSPEDLLLI
     MEAIKKEVIA KIRLWEYYAL DVERDADAAV DAWTKTKTYT SQNTDGLQDE LEQLKDAGLA
     QQVSFLKKFG LLGAGQLGER FLRSVDPNVA ATLLAFTFGR YEGESADSAD KAAARSKMVE
     ILDAMNVPLY EEYDGDVKEI LEQLYNRIKY VRLDEHGPKL GPINDENPLI ETYFTRLPKN
     AATTKHNPRD LMLVNNGWVW GGNALVDNAG PDARVYLRRE VIVWGDCVKL RYGSKPDDSP
     WLWNHMTEYA RKLATHFAGL RIDNCHSTPI HVAEHILDEA RRVRPDLYVV AELFSGSEDT
     DYVFVKRLGL SSLIREAMQA WSTAELSRLV HRHGGRPIGS FEVDEISRGD PTLSPGSQNK
     KDLTREIIRR IKPTPVHALF MDCTHDNETP AQKRDARDTL PNAALVSMCS SATGSVMGYD
     EVYPKLVDLV NETRLYTSES SRSAPIKVGR GKNGIAGVKK LLNQIHTLMG KDGYDETHIH
     HEEEYITVHR VHPESRKGYF LIAHTAFPGY GNGNGALNPV HLAGTRAQHL GSWKLEVDDS
     PEATAKAVNE GQFLVGLPSR VVDITGVDLD VQGEDTIITV RDKFPPGSIA LFETWIPAAE
     HSAGLDTYVT SGAKAAWSQL DLIDLNFLMY RCAAEELDSN NGRDGTYDIP GYGTLVYAGL
     QGWWSLMKDI IRENNLAHPL CQNLRQGTWA LDYILGRLQR MSETEGKEQL ARPASWLKER
     FDAIRTIPSF LLPRYFGLVL RTAYNASRDR ALELMGENIE KGQWFLQSLA LVSVQQTGYV
     KSASLWPNKA VPSVAAGLPH FAVEWSRCWG RDVFISIRGL YLGTGRFDEA KEHILAFASV
     LKHGMIPNLL SSGDAPRYNS RDSIWFFLQT IQDYVHRAPE GTSLLKTSVK RRFLPYDDTW
     FPTDDPRAYS KESTIEDIIQ EALQRHASGM KYREANAGPQ IDSQMKDEGF NQDIHVDWET
     GIIFGGNQSN CGTWMDKMGE SERAGSKGVP GTPRDGAAIE ITGLLYSTLA WLVGLNEQGK
     YAYSSVKTGD GKSVSFKDWA ERIKANFERC YFVPLTTEDD AKYNVNPAVI NRRGIYKDLY
     KSGKEYEDYQ FRSNFPIAMA VAPSLFDPDH AMHALCLADS VLRGPTGMAT LDPADLNYRP
     YYRNSEDSDD FATSKGRNYH QGPEWLWPTG FFLRALLKFD LMRRTTPEGR TEAFQQVTRR
     LAGCKKMIQE SPWAGLTELT QKNGEFCPDS SPTQAWSAGC LIDLYMDGRE AQQEAAET
//
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