GLGX_YERP3
ID GLGX_YERP3 Reviewed; 662 AA.
AC A7FNX4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=YpsIP31758_4005;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS47528.1; -; Genomic_DNA.
DR RefSeq; WP_012105900.1; NC_009708.1.
DR AlphaFoldDB; A7FNX4; -.
DR SMR; A7FNX4; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABS47528; ABS47528; YpsIP31758_4005.
DR KEGG; ypi:YpsIP31758_4005; -.
DR HOGENOM; CLU_011725_1_1_6; -.
DR OMA; SEPWDCG; -.
DR UniPathway; UPA00165; -.
DR Proteomes; UP000002412; 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_1000067110"
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; 73938 MW; B30C96DF6B75CB89 CRC64;
MAVLTHGSPT PSGAYFDGKG INFTLFSAHA EQVTLCLFDE QGQERQIAMP ARTGDIWHGY
LPGGKPGQRY GYRVSGPFDP SRGHRFNPHK LLIDPRTRAL EGKVGDDPRF TGGVSQPDVR
DSAAALPKCL VIHEEYDWQG DKPPAIPWGN TVIYEAHVRG LTQLHPDIPP ELRGTYAALA
HPALIEHLKT LGITTLELLP VQFHIDEPRL QKMGLSNYWG YNVLAPFAVD PDYASGREGI
SPLRELRDAI KALHNAGIEV ILDVVFNHSA ELDVFGPTLC QRGIDNASYY WLTPDGEYDN
ITGCGNALRL SHPYVTQWVI DCLNYWRDSC HVDGFRFDLG TVLGRTPAFD QHAPLFAALA
ADERLSACKL IAEPWDIGLG GYQLGNFPTG FSEWNDQYRD AMRGFWLRGE VPRGTFAQHF
AASSRLFEQR GRLPSASINQ ITAHDGFTLL DLLCFNQKHN QMNGEENRDG SDNNHSNNFG
CEGLVADAAI WQRRKACQRA LLTTLLLSQG TPMLLAGDEQ GHSQQGNNNA YCQNNILTWL
DWGSADRALM TFTADLIRLR QQIPALTQDQ WWQSGDSNVQ WLDSQGQALS DAAWEQGCQQ
QLQILLSQRW LVLINATDHE CEMHLPEGEW EGIPPFGVSD HAERLTTWRG SAHTICVLIK
RD