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Database: UniProt
Entry: A0A0F8UGN8_9EURO
LinkDB: A0A0F8UGN8_9EURO
Original site: A0A0F8UGN8_9EURO 
ID   A0A0F8UGN8_9EURO        Unreviewed;      1537 AA.
AC   A0A0F8UGN8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=ARAM_001207 {ECO:0000313|EMBL:KKK18703.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK18703.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK18703.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK18703.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) 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:KKK18703.1}.
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DR   EMBL; JZBS01002430; KKK18703.1; -; Genomic_DNA.
DR   STRING; 308745.A0A0F8UGN8; -.
DR   OrthoDB; 1427975at2759; -.
DR   Proteomes; UP000034291; 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; 1.
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:UP000034291};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          36..131
FT                   /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14699"
FT   DOMAIN          135..574
FT                   /note="Glycogen debranching enzyme glucanotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF14701"
FT   DOMAIN          738..982
FT                   /note="Glycogen debranching enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF14702"
FT   DOMAIN          1066..1526
FT                   /note="Glycogen debranching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06202"
SQ   SEQUENCE   1537 AA;  173499 MW;  B4907A4BDDED0BF6 CRC64;
     MASETVYLLP LKDDGSPDIP GGYIYLSPPD NAPYALRFVI EGSSSICRDG TLWVNIPETG
     KSFDRSSFRG FKLSPDFSKN IQIDVPITCP GSFAFYVTYS PLPDFSLSSN SNLESTRTPK
     HYIDVSPRLS LGHRNIPLNA LSIFSVNSKF MGKYPEDWNR CLSSISRRKY NMIHFTPLMK
     RGDSNSPYSI FDQLQFDDVS FPNGENDVFQ LVRNMEEEYS LLSLTDVVWN HTANNSKWLE
     EHPEAGYSVD TAPWLEAALD LDTALLKFGK ELGQYGLPTE FKTVDDLTKV MNGVKDHVIK
     DLRLWEFYIV NVKYNTQQIL DTWKSSKDIN LTNGRWAQLG LENYKTLTLE QQTTLIREQG
     IPNYKQIRGR YERNIDVELG AAIATAVFGA FDPRSSDLAS AENTISNLVD VVNVAFYEEY
     NSDLSEIMNQ LFNRIKYLRI DDHGPRLGPV TDDSPFIESY FTRLPLNEVT KKHSSKALAL
     ANNGWIWNAD AMRDNAGPDS RAYLRREVIV WGDCVKLRYG NGPEDSPFLW EFMTKYTRLM
     AKYFSGFRID NCHSTPLVVA EHLIDEARRV RPNLAIFAEL FTGSEEADYI FVKRLGINAL
     IREAMQAWST GELSRLVHRH GGRPIGSFEL DLPSPGLNFS VAEGSSKKVV VRHIRPKPVP
     ALFMDCTHDN EMPAQKRTAK DTLPNAALVA MCASAIGSVL GYDEIYPKIV DLVHETRQYA
     FEDLPESPSL DELANIPGIC GLKRLLNELH TKMGVDGYDE THIHHDGEYI TVHRVHPQSR
     KGVFLIAHTA FPGKDNKDIL APTHLVATRV KHIGTWLLTV DEGDEAKSRV LEDPDYLSGL
     PSQVQQINGT KVEENDNETV ISVLDTLVPG SIALFETSLP VVEDTDGLDN KSITQGADEA
     FSQLNLVDLN YVLYRCEAEE RDSSGGQEGV YDIPSSGPLV YAGLQGWWSI LEDIIKYNNL
     GHPMCDHLRQ GQWALDYIVG RLAKAGEKQD YTALKGPAEW LEKKFTAVRS LPNFLLPRYF
     AIIVQTAYVS AWNRGIQLLG SNVRKGQVFI QQLAMVSVQQ TGFANSASLW PTKRVPTLAA
     GLPHFATDWA RCWGRDVFIS LRGLFLCTER FDDAKEHILA FSSVLKHGMI PNLLSSGKLP
     RYNSRDSIWF LLQAIQDYTK MAPNGRELLR EKVPRRFLPY DDTWFPFDDP RAYSQSSTVI
     EVIQEVFQRH AHGLSFREYN AGPELDMQMK PQGFQIDIKV DWKTGLIFGG SQFNCGTWQD
     KMGESEKAGN KGFPGTPRDG AAIEITGLVY SALTWVSGLF EEGIYPHDRV EIGDGKSITF
     KDWAAKIKEN FERCYYIPTD PTEDGQHDIN PKIVNRRGIY KDLYKSGKPY EDYQLRSNFP
     IAMVVSPDLF TPSKALGALA LADSVTVGPV GMATLDPSDL NYRPNYYNSD DSTDFATSKG
     RNYHQGPEWV WQRGYFLRAM LYFDLARRKT AEQQTEAFQQ VTRRLEGCKE ALRESPWKGL
     TELTNKNGAF CSDSSPTQSW SAGCLLDLYY DASRYTR
//
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