GLGX_YERE8
ID GLGX_YERE8 Reviewed; 662 AA.
AC A1JSI8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, 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}; OrderedLocusNames=YE4012;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM286415; CAL14030.1; -; Genomic_DNA.
DR RefSeq; WP_005174773.1; NC_008800.1.
DR RefSeq; YP_001008156.1; NC_008800.1.
DR AlphaFoldDB; A1JSI8; -.
DR SMR; A1JSI8; -.
DR STRING; 393305.YE4012; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; CAL14030; CAL14030; YE4012.
DR KEGG; yen:YE4012; -.
DR PATRIC; fig|393305.7.peg.4271; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_011725_1_1_6; -.
DR OMA; SEPWDCG; -.
DR UniPathway; UPA00165; -.
DR Proteomes; UP000000642; 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..662
FT /note="Glycogen debranching enzyme"
FT /id="PRO_1000067109"
FT ACT_SITE 338
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT ACT_SITE 373
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT SITE 445
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
SQ SEQUENCE 662 AA; 74267 MW; E9B7BDD766552802 CRC64;
MTTLTSGSPT PMGAHFDGVG INFTLFSAHA EQVELCLFDD NNQELRIPLP ARSGDIWHGY
LPGGKPGQRY GYRVSGPFNP QQGHRFNPHK LLIDPYARAL DRKVGDDPSL QGGVSQPDYR
DSAAVAPKCI VVHEEYDWQG DRRPTIPWGN TVIYEAHVRG LTQLHPDIPA DLRGTYAGLA
HPAMIQYLQK LGITTLELLP VQFHIDEPRL QKMGLSNYWG YNVLAPYAVD PDYASGREGI
SPLRELRDAV KALHQAGIEV ILDVVFNHSA ELDVFGPTLC QRGIDNASYY WLTSEGEYDN
MTGCGNTLRL SQPYVMQWVL DCLRYWVDSC HIDGFRFDLG TVLGRSPAFD QHAPLFAALA
ADKQLCNCKM IAEPWDIGLG GYQLGNFPTG FSEWNDQYRD AMRRFWLRGD LPLGQFAQHF
AASSNLFKHR ERLPSASINQ ITAHDGFTLQ DLLCFNQKHN QINGEENRDG SDNNLSNNFG
SEGLVADDAI WQRRKACQRA LLTTLLLSQG TPMLLAGDEH GHSQQGNNNA YCQNNILTWL
DWGSADRELT AFTAELIRLR QQIPALIQDS WWEDGDGNVQ WLDSQGEALS DGAWEQGCQK
QLQIRLSQRW LVVINATDQA CEMHLPVGEW VVIPPFEPSE HTEPLTVWNG SAHTVCVLTQ
KF