ID   GLGX_KLEP7              Reviewed;         658 AA.
AC   A6TF50;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=KPN78578_37600; ORFNames=KPN_03797;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR79184.1; -; Genomic_DNA.
DR   RefSeq; WP_015959100.1; NC_009648.1.
DR   AlphaFoldDB; A6TF50; -.
DR   SMR; A6TF50; -.
DR   STRING; 272620.KPN_03797; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; A6TF50; -.
DR   EnsemblBacteria; ABR79184; ABR79184; KPN_03797.
DR   KEGG; kpn:KPN_03797; -.
DR   HOGENOM; CLU_011725_1_1_6; -.
DR   OMA; SEPWDCG; -.
DR   UniPathway; UPA00165; -.
DR   Proteomes; UP000000265; 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_1000165062"
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   658 AA;  73651 MW;  56CEB75456B5D41F CRC64;
     MTSLAAGKPA PLGASYDGKG VNFALFSAHA ERVELCVFDE QGNEQRFDLP ARSGDIWHGW
     LAAAGPGLRY GYRVHGPWDP AQGHRFNPAK LLIDPSAHRV EGDLPDDERL HGGMWQPDRR
     DSAAVAPKSQ VVDLRYDWRG DKPPRTPWGE TVIYEAHVKG LTLLNPQLPE AIRGTYKALG
     HPAMIAYFKS LGISALELLP VAQFASEPRL QRMGLSNYWG YNPLAWFALD PRYASDPDRA
     LDEFRDAVKA LHAAGIEVIL DIVLNHSAEI DLEGPTVSLR GIDNRSYYWV REDSDYHNWT
     GCGNTLNLSH PGVVEWARQC LRFWVDECHV DGFRFDLASV MGRTPEFRQD APLFEAIRRD
     SVLSQVKLIA EPWDIGPGGY QVGNFPPLFA EWNDHFRDSA RRFWLQQNVS LGDFAQRFAA
     SSDLFARDGK PPSATVNLVT AHDGFTLRDC VCFNQKHNEA NGEENRDGTN NNYSNNHGIE
     GLEANFAVIE RRRASAHALL TTLLLAQGTP MLLAGDEQGH SQHGNNNAYC QDNALTWLDW
     RQANPGLTAF TAALIHLRRR IPALTRNRWW QEGDGNVRWL NRNAQPLTAA EWQQGAACMQ
     IQLSDRWLLT LNATAEVVDM VLPEGEWRAV PPFAGEDNPV IMAVWHGPAH GVCVFQRS