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
//