ID D4ASG4_ARTBC Unreviewed; 1506 AA.
AC D4ASG4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=ARB_07179 {ECO:0000313|EMBL:EFE34228.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE34228.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE34228.1}.
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DR EMBL; ABSU01000007; EFE34228.1; -; Genomic_DNA.
DR RefSeq; XP_003014617.1; XM_003014571.1.
DR STRING; 663331.D4ASG4; -.
DR GeneID; 9527171; -.
DR KEGG; abe:ARB_07179; -.
DR eggNOG; KOG3625; Eukaryota.
DR HOGENOM; CLU_001517_2_0_1; -.
DR OMA; YEEGHVH; -.
DR OrthoDB; 1427975at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:UP000008866};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 39..136
FT /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14699"
FT DOMAIN 139..571
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 726..966
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1056..1499
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
SQ SEQUENCE 1506 AA; 169885 MW; 185F03BD467343E5 CRC64;
MDSNNQELVY VVHLNDNGSP DAHHSYVNLP PPTTPAYSLR LQFEGSSPLC RYGSLWVNIP
SAGEEFQRDK YREYKLKPDF NKDIHVDIPI AISGAFDYYF TYRQLPKLFG PGSGSDTGKE
TRSETYYLNV RPAITLKGKA LPLESLSIFS VVSKFMGEYP TDWNKHLRGI GERGYNVVHF
TPLVKRGASN SPYSLYDQLE FEECFSNGQK DVADMTAKME KDYGLLALTD VVWNHVAHNS
QLLEDHPEVG YNIKNAPWLE AALELDTALL QYGNDLAKLG LPTEFKTEDD ILVVLRRARE
NVIDKIKLWE FYAIDVERDA AAALKSWESD NYEDAELGNA EEIRGWSMEK KAKFLRQKGV
TNANRVLGRY DRKADPNITA SFLAAMFGRH AESKADASTV KAELRKLLDA VNLPLFKEYD
KDVITILDQL FGRIKYLRVD EHGPKMGPVS NESPLIETYF TRLSSSGKRD PRLLALANNG
WVWNADAMKD NAGPDSRAYL LREVIVWGDC VKLNYGASRD DNPFLWDYMA DYSKLMAKYF
MGFRIDNCHS TPIPVAEYLL DEARRVRPNL VVFAELFTGS EKTDYIFAKR LGLTGLIREA
MQAWSAGELS RLVHRHGGRP IGSFEADLLS HGDHRESNQI VRQLQYTPLN ALFMDCTHDN
QMPAQKREAR DTLPNAALVA MCSSAIGSVM GYDEIYPKHV DLVNETRLYS SASSDGEVKS
RTGQGGIGGI KRLLNDLHTS MAVNCYDETH IHHEGQYITV HRVQPHTRKG VLLIAHTAFS
GSKDEHNLDP IVLSGTNAKM IGAWKLEIIS SNRDANTNTR FINGLHSKVS DIEEVSIEND
GNNTIIRVPA GLVPGSIALL ETWLPETNLL KDLSTFITSD AEAAFKSLDP VDLNFVLYKC
NPEERDISHG SDGVYDIPNF GPLVYAGLQG WWSVLEGVIR NNDVGHPICD NLRNGQWALD
FIVRRMHKAA SNEGYGRLKE PAEWLQGRFD AIRKLPSFLL PRYFAIVVKT AYEAALARGI
QLLGVTIEHG KDIIHELAMV SIQQVGFVNS ASLYPTKRVP CLAAGLPHFS TDWARCWGRD
VFISLRGLLL CTGRFDEAKE HILAFASVLK HGLMPNLLSD GKAPRYNARD AVWFFLQAIQ
DYTKIVPDGI QVLNEKVRRR FLPYDDTWFS HDDSRAYSET STVAEIIQEI FQRHASGISF
REYNAGPNLD MQMKDEGFQI DIRVDWETGL VFGGNQWNCG TWMDKMGEST KSGNKGHPGT
PRDGAAVEIS GLLYSTLSWL SSLADQGKFP FKGVEVGSGE SISYAEWAAK IKSNFERCYY
IPENQVDDSK YDIDSKIVHR RGIYKDLYRS GKPYEDYQFR PNFAVAMTVA PELFTLEKAL
RTLELADSVL RGPMGMATLD PKDLNYNPYY VNSEDSTNFA TSKGRNYHQG PEWLWPTGYF
LRALMKFVLM RRDSPQDRTD IFQQLTNRLE ECKKALRTSP WRGLTELTNK NGELCADSVS
CCFLSP
//
