ID   GLGX_CITK8              Reviewed;         657 AA.
AC   A8AQY2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=CKO_04850;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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; CP000822; ABV15895.1; -; Genomic_DNA.
DR   RefSeq; WP_012135536.1; NC_009792.1.
DR   AlphaFoldDB; A8AQY2; -.
DR   SMR; A8AQY2; -.
DR   STRING; 290338.CKO_04850; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; A8AQY2; -.
DR   EnsemblBacteria; ABV15895; ABV15895; CKO_04850.
DR   GeneID; 45138347; -.
DR   KEGG; cko:CKO_04850; -.
DR   HOGENOM; CLU_011725_1_1_6; -.
DR   OMA; SEPWDCG; -.
DR   OrthoDB; 99080at2; -.
DR   UniPathway; UPA00165; -.
DR   Proteomes; UP000008148; 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..657
FT                   /note="Glycogen debranching enzyme"
FT                   /id="PRO_1000067097"
FT   REGION          459..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;  73420 MW;  A121AD8C9D232C9A CRC64;
     MTQLATGKAT PHGATYDGHG VNFTLFSAHA ERVELCVFDA LGNEQRYDLP GRSGDVWHGY
     LADARPGLRY GYRVHGPWQP AQGHRFNPAK LLIDPCARRV EGELKDNPLL HGGYDEPDHR
     DNAAVALKCV VTADRYDWED DAAPRTPWGN TVIYEAHVKG LTYLHPAIPS EIRGTWKALG
     HPVMIAYFKQ LGITALELLP VAHFASEPRL QRLGLSNYWG YNPVAMFALH PAYACSPETA
     LDEFRDAIKA LHKAGIEVIL DIVLNHSAEL DLDGPLFSLR GIDNRSYYWI KEDGDYHNWT
     GCGNTLNLSH PGVVEFACEC LRYWVETCHV DGFRFDLASV MGRTPAFRQD APLFTAINNC
     PVLSSVKLIA EPWDIGEGGY QVGNFPPPFA EWNDHFRDAA RRFWLQRNLP LGEFAGRFAG
     SSDVFKRHDR LPNASVNLIT AHDGFTLRDC VCFNQKHNEA NGEENRDGTN NNYSDNHGKE
     GLGGTLDLIE RRRDSIHALL TTLLLSQGTP MLLAGDEHGH SQHGNNNAYC QDNALTWLDW
     QQANSGLTTF TAALIHLRQQ IPALVGNRWW EENDGNVRWL NKNAEPLSAG EWENGPKQMQ
     ILLSDRFLIA INATLEVTDI VLPEGEWHAI PPFAGEDNPV ITAVWQGPAH GLCVFQR