GLGX_ERWT9
ID GLGX_ERWT9 Reviewed; 658 AA.
AC B2VJR7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Glycogen debranching enzyme {ECO:0000255|HAMAP-Rule:MF_01248};
DE EC=3.2.1.196 {ECO:0000255|HAMAP-Rule:MF_01248};
DE AltName: Full=Limit dextrin alpha-1,6-maltotetraose-hydrolase {ECO:0000255|HAMAP-Rule:MF_01248};
GN Name=glgX {ECO:0000255|HAMAP-Rule:MF_01248}; OrderedLocusNames=ETA_32480;
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=465817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(2008).
CC -!- FUNCTION: Removes maltotriose and maltotetraose chains that are
CC attached by 1,6-alpha-linkage to the limit dextrin main chain,
CC generating a debranched limit dextrin. {ECO:0000255|HAMAP-
CC Rule:MF_01248}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches
CC with degrees of polymerization of three or four glucose residues in
CC limit dextrin.; EC=3.2.1.196; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01248};
CC -!- PATHWAY: Glycan degradation; glycogen degradation. {ECO:0000255|HAMAP-
CC Rule:MF_01248}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000305}.
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DR EMBL; CU468135; CAO98294.1; -; Genomic_DNA.
DR RefSeq; WP_012442921.1; NC_010694.1.
DR AlphaFoldDB; B2VJR7; -.
DR SMR; B2VJR7; -.
DR STRING; 465817.ETA_32480; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; CAO98294; CAO98294; ETA_32480.
DR KEGG; eta:ETA_32480; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_011725_1_1_6; -.
DR OMA; SEPWDCG; -.
DR OrthoDB; 99080at2; -.
DR UniPathway; UPA00165; -.
DR Proteomes; UP000001726; Chromosome.
DR GO; GO:0004133; F:glycogen debranching enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd02856; E_set_GDE_Isoamylase_N; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR HAMAP; MF_01248; GlgX; 1.
DR InterPro; IPR040784; GlgX_C.
DR InterPro; IPR044505; GlgX_Isoamylase_N_E_set.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR022844; Glycogen_debranch_bac.
DR InterPro; IPR011837; Glycogen_debranch_GlgX.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF18390; GlgX_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR02100; glgX_debranch; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen metabolism; Glycosidase; Hydrolase;
KW Reference proteome.
FT CHAIN 1..658
FT /note="Glycogen debranching enzyme"
FT /id="PRO_1000165060"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT ACT_SITE 370
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT SITE 442
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
SQ SEQUENCE 658 AA; 74200 MW; 8C5C26ABDDC10092 CRC64;
MMPIRDGQPA PRGASYDGKG VNFSLFSQRA ERVELCLYDD DGVETRLDLP AHSGDIWHGY
LPAVRPGQRY GYRVHGPWQP QQGLRFNPAK LLLDPCARGI EGEVTDNPCF QSGEEQPDTL
DSGPLAPKGV VLADDFDWED DTWPRVPWGS TVIYEAHVRG LTQLHPGIPA EMRGTYAALG
HPVMIDYFQR LGITSLQLLP VACFASEPRL LRLGLSNYWG YNPLACYALE SRYACGQNPR
EEFQQAVKTL HQAGIEVILD VVFNHSAELD ENGPTLSMRG IDNPTYYWLD GQGNYDNWTG
CGNTQNLVHP EAVASTLDCL RYWVEECHID GFRFDLATTL GRTPEYRRDA PLFQAIAADP
LLAQCKIIAE PWDIGPRGYQ VGNFPPPFAE WNDHFRDTAR RYWLHGDFSN GDFARRFAAS
SDLFQKQGRL PSASLNYITA HDGFTLRDLV SFEHKHNEAN GEDNRDGSNN NFSYNHGVEG
LKAPLLVTEH RRRSIHALLT TLLLAQGTPM LLAGDEHGHS QHGNNNAYCQ DNVLTWLDWK
HGDRGLFSFT AALIHLRRRI PALQQDRWWQ EGDGSVEWLN GQGRQLNRLE WEQGVHRLQI
RLSKQWLITL NATEEVCDLV LPPGKWHAVP PFAGEDNPIL LTVWHGAAQG VCVFQEKS