GLGX_SHIB3
ID GLGX_SHIB3 Reviewed; 657 AA.
AC B2U4G1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=SbBS512_E3893;
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512;
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) 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; CP001063; ACD07189.1; -; Genomic_DNA.
DR RefSeq; WP_000192517.1; NC_010658.1.
DR AlphaFoldDB; B2U4G1; -.
DR SMR; B2U4G1; -.
DR STRING; 344609.SbBS512_E3893; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ACD07189; ACD07189; SbBS512_E3893.
DR KEGG; sbc:SbBS512_E3893; -.
DR HOGENOM; CLU_011725_1_1_6; -.
DR OMA; SEPWDCG; -.
DR UniPathway; UPA00165; -.
DR Proteomes; UP000001030; 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_1000139880"
FT REGION 458..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; 73563 MW; E4DB47E12246B420 CRC64;
MTQLAIGKPA PLGAHYDGQG VNFTLFSAHA ERVELCVFDA NGQEHRYDLP GHSGDIWHGY
LPDARPGLRY GYRVHGPWQP ADGHRFNPAK 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 LGAFAGRFAA
SSDVFKRNGR LPSAAINLVT AHDGFTLRDC VCFNHKHNEA NGEENRDGTN NNYSNNHGKE
GLGGSLDLVE RRRDSIHALL TTLLLSQGTP MLLAGDEHGH SQHGNNNAYC QDNQLTWLDW
SQASSGLTAF TAALIHLRKR IPALVENRWW EEGDGNVRWL NRYAQPLSTD EWQNGPKQLQ
ILLSDRFLIA INATLEVTEI VLPAGEWHAI PPFAGEDNPV ITAVWQGPAH GLCVFQR