ID   GLGX_SALPB              Reviewed;         658 AA.
AC   A9MTV3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, 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=SPAB_04392;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-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; CP000886; ABX69708.1; -; Genomic_DNA.
DR   RefSeq; WP_000192494.1; NC_010102.1.
DR   AlphaFoldDB; A9MTV3; -.
DR   SMR; A9MTV3; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; spq:SPAB_04392; -.
DR   PATRIC; fig|1016998.12.peg.4135; -.
DR   HOGENOM; CLU_011725_1_1_6; -.
DR   OMA; SEPWDCG; -.
DR   BioCyc; SENT1016998:SPAB_RS17880-MON; -.
DR   UniPathway; UPA00165; -.
DR   Proteomes; UP000008556; 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; 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..658
FT                   /note="Glycogen debranching enzyme"
FT                   /id="PRO_1000085789"
FT   REGION          459..484
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   658 AA;  73632 MW;  2A67721C339BFD62 CRC64;
     MTQLAIGEAT PHGATYDGHG VNFTLFSAHA ERVELCVFDS RGNERRYDLP GRRGDVWHGY
     LAGARPGLRY GYRVHGPWQP AQGHRFNPAK LLLDPYARRV EGELKDHPLL HGGHDEPDYR
     DNAAVAPKSV VISDHYDWED DAAPRTPWGK TVIYEAHVKG LTYLHPELPQ EIRGTYKALG
     HPVMVAYFKQ LGITALELLP VAQFASEPRL QRMGLTNYWG YNPMAMFALH SAWASSPEMA
     LDEFRDAVKA LHRAGIEVIL DIVLNHSAEL DLDGPTFSLR GIDNRSYYWI RDDGDYHNWT
     GCGNTLNLSH PGVVEYACEC LRYWVETCHV DGFRFDLASV MGRTPTFRQD APLFAAIKAC
     PVLSTVKLIA EPWDIGEGGY QVGNFPPPFA EWNDHFRDAA RRFWLPRNLT TGEFACRFAA
     SSDVFKRNGR APGASVNLLT AHDGFTLRDC VCFNQKHNEA NGEENRDGTN SNYSDNHGKE
     GLGGPLDLME RRRDSIHALL ATLLLSQGTP MLLAGDEHGH SQHGNNNAYC QDNALTWLDW
     QQANRGLTTF TAALIRLRQQ IPALTGNSWW EEGDGNVRWL NKNAQPLSAD EWQNGPKLMQ
     ILLSDRFLIA INATLEVTDI VLPEGEWRAV PPFAGEDNPV ITAVWQGPAH GLCVFQRG