ID   GLGX_ECO27              Reviewed;         657 AA.
AC   B7UKY8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=E2348C_3677;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; FM180568; CAS11225.1; -; Genomic_DNA.
DR   RefSeq; WP_000192570.1; NC_011601.1.
DR   AlphaFoldDB; B7UKY8; -.
DR   SMR; B7UKY8; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; CAS11225; CAS11225; E2348C_3677.
DR   KEGG; ecg:E2348C_3677; -.
DR   HOGENOM; CLU_011725_1_1_6; -.
DR   OMA; SEPWDCG; -.
DR   UniPathway; UPA00165; -.
DR   Proteomes; UP000008205; 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..657
FT                   /note="Glycogen debranching enzyme"
FT                   /id="PRO_1000165054"
FT   REGION          460..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        336
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT   ACT_SITE        371
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT   SITE            443
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
SQ   SEQUENCE   657 AA;  73681 MW;  C9E774C41986B769 CRC64;
     MTQLAIGKPT PLGAHYDGQG VNFTLFSAHA ERVELCVFDA NGQEHRYDLP GHSGDIWHGY
     LPDARPGLRY GYRVHGPWQP AEGHRFNPAK LLIDPCARQI DGEFKDNPLL HAGHNEPDYR
     DNAAIAPKCV VVVDHYDWED DAPPRTPWGS TIIYEAHVKG LTYLHPEIPV EIRGTYKALG
     HPVMINYLKQ LGITALELLP VAQFASEPRL QRMGLSNYWG YNPVAMFALH PAYACSPETA
     LDEFRDAIKA LHKAGIEVIL DIVLNHSAEL DLDGPLFSLR GIDNRSYYWI REDGDYHNWT
     GCGNTLNLSH PAVVDYASAC LRYWVETCHV DGFRFDLAAV MGRTPEFRQD APLFTAIQNC
     PVLSQVKLIA EPWDIAPGGY QVGNFPPLFA EWNDHFRDAA RRFWLHYDLP LGVFAGRFAA
     SSDVFKRNGR LPSAAINLVT AHDGFTLRDC VCFNHKHNEA NGEENRDGTN NNYSNNHGKE
     GLGGTLDLVE RRRDSIHALL TTLLLSQGTP MLLAGDEHGH SQHGNNNAYC QDNQLTWLDW
     SQASSGLTAF TAALIHLRKR IPALMENRWW EEGDGNVRWL NRYAQPLSTD EWQNGPKQLQ
     ILLSDRFLIA INATLEVTEI VLPAGEWHAI PPFAGEDNPV ITAVWQGPAH GLCVFQR