ID GLGX_ECOL5 Reviewed; 657 AA.
AC Q0TC28;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 112.
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=ECP_3525;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG71501.1; -; Genomic_DNA.
DR RefSeq; WP_000192568.1; NC_008253.1.
DR AlphaFoldDB; Q0TC28; -.
DR SMR; Q0TC28; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; ecp:ECP_3525; -.
DR HOGENOM; CLU_011725_1_1_6; -.
DR UniPathway; UPA00165; -.
DR Proteomes; UP000009182; 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; cd11326; AmyAc_Glg_debranch; 1.
DR CDD; cd02856; E_set_GDE_Isoamylase_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 NCBIfam; TIGR02100; glgX_debranch; 1.
DR PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR PANTHER; PTHR43002:SF1; ISOAMYLASE 1, CHLOROPLASTIC; 1.
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; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 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_1000067101"
FT REGION 460..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; 73711 MW; 46AA0113427106ED CRC64;
MTQLAIGKPT PLGAHYDGQG VNFTLFSAHA ERVELCVFDA NGQEHRYDLP GHSGDIWHGY
LPDARPGLRY GYRVHGPWQP AEGHRFNPAK 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
SSDVFKRNDR LPSAAINLVT AHDGFTLRDC VCFNHKHNEA NGEENRDGTN NNYSNNHGKE
GLGGTLDLVE RRRDSIHALL TTLLLSQGTP MLLAGDEHGH SQHGNNNAYC QDNQLTWLDW
SQASSGLTAF TAALIHLRKR IPALMENRWW EEGDGNVRWL NRYAQPLSTD EWQNGPKQLQ
ILLSDRFLIA INATLEVTEI VLPAGEWHAI PPFAGEDNPV ITAVWQGPAH GLCVFQR
//
