ID   GLGX_YERPG              Reviewed;         662 AA.
AC   A9R5L9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 87.
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};
GN   OrderedLocusNames=YpAngola_A4119;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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}.
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DR   EMBL; CP000901; ABX88352.1; -; Genomic_DNA.
DR   RefSeq; WP_012230174.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R5L9; -.
DR   SMR; A9R5L9; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ypg:YpAngola_A4119; -.
DR   PATRIC; fig|349746.12.peg.854; -.
DR   OMA; SEPWDCG; -.
DR   UniPathway; UPA00165; -.
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.
FT   CHAIN           1..662
FT                   /note="Glycogen debranching enzyme"
FT                   /id="PRO_1000139882"
FT   ACT_SITE        338
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT   ACT_SITE        373
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT   SITE            445
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
SQ   SEQUENCE   662 AA;  73843 MW;  3F9BA2C47F7AB316 CRC64;
     MAVLTHGSPT PSGAHFDGKG INFTLFSAHA EQVTLCLFDE QGQERQIAMP ARTGDIWHGY
     LPGGKPGQRY GYRVSGPFEP SRGHRFNPHK LLIDPRTRAL EGKVGDDPRF TGGVSQPDVR
     DSAAALPKCL VIHEEYDWQG DKPPAIPWGN TVIYEAHVRG LTQLHPDIPP ELRGTYAALA
     HPALIEHLKT LGITTLELLP VQFHIDEPRL QKMGLSNYWG YNVLAPFAVD PDYASGREGI
     SPLRELRDAV KALHNAGIEV ILDVVFNHSA ELDVFGPTLC QRGIDNASYY WLTPDGEYDN
     ITGCGNALRL SHPYVTQWVI DCLNYWRDSC HVDGFRFDLG TVLGRTPAFD QHAPLFAALA
     ADERLSACKL IAEPWDIGLG GYQLGNFPTG FSEWNDQYRD AMRGFWLRGE VPRGTFAQHF
     AASSSLFEQR GRLPSASINQ ITAHDGFTLL DLLCFNQKHN QMNGEENRDG SDNNHSNNFG
     CEGLVADAAI WQRRKACQRA LLTTLLLSQG TPMLLAGDEQ GHSQQGNNNA YCQNNILTWL
     DWGSADRALM TFTADLIRLR QQIPALTQDQ WWQSGDSNVQ WLDSQGQALS DAAWEQGCQQ
     QLQILLSQRW LVLINATDHE CEMHLPEGEW EGIPPFGVSD HAERLTTWRG SAHTICVLIK
     RD