GLGX_YERPA
ID GLGX_YERPA Reviewed; 662 AA.
AC Q1C1E0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=YPA_3770;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(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; CP000308; ABG15732.1; -; Genomic_DNA.
DR RefSeq; WP_002209499.1; NZ_CP009906.1.
DR AlphaFoldDB; Q1C1E0; -.
DR SMR; Q1C1E0; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABG15732; ABG15732; YPA_3770.
DR GeneID; 57974763; -.
DR KEGG; ypa:YPA_3770; -.
DR OMA; SEPWDCG; -.
DR UniPathway; UPA00165; -.
DR Proteomes; UP000001971; 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_1000067111"
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; 73912 MW; 9E5C79A9C9A18EB5 CRC64;
MAVLTHGSPT PSGAHFDGKG INFTLFSAHA EQVTLCLFDE QGQERQIAMP ARTGDIWHGY
LPGGKPGQRY GYRVSGPFEP SRGHRFNPHK LLIDPRTRAL EGKVGDDPRF TGGVSQPDVR
DSAAALPKCL VIHEEYDWQG DKPPAIPWGN TVIYEAHVRG LTQLHPDIPP ELRGTYAALA
HPALIEHLKT LGITTLELLP VQFHIDEPRL QKMGLSNYWG YNVLAPFAVD PDYASGREGI
SPLRELRDAV 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