ID   GLGX_YERPS              Reviewed;         662 AA.
AC   Q664I3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=YPTB3786;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH23024.1; -; Genomic_DNA.
DR   RefSeq; WP_011193250.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q664I3; -.
DR   SMR; Q664I3; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; CAH23024; CAH23024; YPTB3786.
DR   GeneID; 66843790; -.
DR   KEGG; ypo:BZ17_2799; -.
DR   KEGG; yps:YPTB3786; -.
DR   PATRIC; fig|273123.14.peg.2933; -.
DR   OMA; SEPWDCG; -.
DR   UniPathway; UPA00165; -.
DR   Proteomes; UP000001011; 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.
FT   CHAIN           1..662
FT                   /note="Glycogen debranching enzyme"
FT                   /id="PRO_1000067114"
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;  73924 MW;  B1BCCECD772D0D62 CRC64;
     MAVLTHGSPT PSGAYFDGKG INFTLFSAHA EQVTLCLFDE QGQERQIAMP ARTGDIWHGY
     LPGGKPGQRY GYRVSGPFDP 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
     AASSRLFEQR GRLPSASINQ ITAHDGFTLL DLLCFNQKHN QMNGEENRDG SDNNHSNNFG
     CEGLVADAAI WQRRKACQRA LLTTLLLSQG TPMLLAGDEQ GHSQQGNNNA YCQNNILTWL
     DWGSADRALM TFTADLIRLR QQIPALTQDQ WWQSGDSNVQ WLDSQGQALS DAAWEQGCQQ
     QLQILLSQRW LVLINATDHE CEMHLPEGEW EGIPPFGVSD HAERLTTWRG SAHTICVLIK
     RD