ID   GLGX_ENT38              Reviewed;         657 AA.
AC   A4WFL4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=Ent638_3839;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000653; ABP62494.1; -; Genomic_DNA.
DR   RefSeq; WP_015960799.1; NC_009436.1.
DR   AlphaFoldDB; A4WFL4; -.
DR   SMR; A4WFL4; -.
DR   STRING; 399742.Ent638_3839; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABP62494; ABP62494; Ent638_3839.
DR   KEGG; ent:Ent638_3839; -.
DR   eggNOG; COG1523; Bacteria.
DR   HOGENOM; CLU_011725_1_1_6; -.
DR   OMA; SEPWDCG; -.
DR   OrthoDB; 99080at2; -.
DR   UniPathway; UPA00165; -.
DR   Proteomes; UP000000230; 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; 2.
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_1000165057"
FT   REGION          460..479
FT                   /note="Disordered"
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;  73784 MW;  D1FFAAC28ADD5206 CRC64;
     MTQLTAGKPA PLGASFDGKG VNFTLFSAHA ERVELCVFDR EGNEYRYDLP AREGDIWHGY
     LEDGKPGLRY GFRVHGPWQP EYGLRFNPAK LLIDPCALRV DGDVKDDPLF LDGEQQPDPR
     DSAAIAPRSV VVSDVYDWEG DSSPDIPWGN TVIYEAHVKG LTYLHPAIPK EIRGTYKALG
     HPVMIAYLKH LGITSLELLP IWHFASEPRL QRLGLTNYWG YNPLAMFALD PRYASHPERA
     RDEFRDAVKA LHQAGIEVIL DVVLNHSAEL DLDGPTLSLR GIDNRSYYWI REDGDYHNWT
     GCGNTLNLSH PAVAEYAHAC LKYWVETFHI DGFRFDLASV MGRTPAFSQQ APLLEAIKNC
     PVLSRVKLIA EPWDIGEGGY QVGNFPPPFA EWNDHYRDAT RRFWLEKSLS LGEFAGRFSA
     SSDVFKRQGR KPFSTVNLVT AHDGFTLRDC VCFNQKHNEA NGEENRDGTN NNHSFNHGIE
     GLGGSQDVIE RRRASVHALL TTLLLSQGTP MLLAGDEHGH SQHGNNNAYC QDNPLTWLDW
     EQANSGLTHF TAALIQLRQR IPALTADTWW EEGDGNVRWL NKDAQPLSAQ EWQNGMPCLQ
     ILLSDNWLIT FNATQDVVEI VLPDGEWRAI PPFAGEDNPV VVAVWHGPAH GVCVFQR