GLGX_DICCH
ID GLGX_DICCH Reviewed; 657 AA.
AC Q8KR69;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 99.
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}; Synonyms=amyX;
OS Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=556;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, AND
RP CHARACTERIZATION.
RC STRAIN=PY35;
RX PubMed=11554733; DOI=10.1006/bbrc.2001.5594;
RA Lim W.-J., Park S.-R., Cho S.-J., Kim M.-K., Ryu S.-K., Hong S.-Y.,
RA Seo W.-T., Kim H., Yun H.-D.;
RT "Cloning and characterization of an intracellular isoamylase gene from
RT Pectobacterium chrysanthemi PY35.";
RL Biochem. Biophys. Res. Commun. 287:348-354(2001).
RN [2]
RP GENE NAME GLGX.
RX PubMed=12480526; DOI=10.1016/s0006-291x(02)02763-8;
RA Lim W.-J., Park S.-R., Kim M.-K., An C.-L., Yun H.-J., Hong S.-Y.,
RA Kim E.-J., Shin E.-C., Lee S.-W., Lim Y.-P., Yun H.-D.;
RT "Cloning and characterization of the glycogen branching enzyme gene
RT existing in tandem with the glycogen debranching enzyme from Pectobacterium
RT chrysanthemi PY35.";
RL Biochem. Biophys. Res. Commun. 300:93-101(2003).
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 (By similarity). Hydrolyzes the
CC alpha-1,6-glycosidic linkages in amylopectin while does not hydrolyze
CC the alpha-1,4-glycosidic linkages in amylose. Native glycogen is a poor
CC substrate (PubMed:11554733). {ECO:0000255|HAMAP-Rule:MF_01248,
CC ECO:0000269|PubMed:11554733}.
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 -!- ACTIVITY REGULATION: Slightly activated by Ca(2+). Inhibited by
CC divalent cations such as Zn(2+), Cu(2+), Fe(2+), Mg(2+), Mn(2+), but
CC only slightly inhibited by EDTA.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.;
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.;
CC -!- PATHWAY: Glycan degradation; glycogen degradation. {ECO:0000255|HAMAP-
CC Rule:MF_01248}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:11554733) identified as an isoamylase
CC despite of its little activity on glycogen, but was renamed as glycogen
CC debranching enzyme due to the characterization of the flanking gene
CC coding for the glycogen branching enzyme (PubMed:12480526).
CC {ECO:0000305|PubMed:11554733, ECO:0000305|PubMed:12480526}.
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DR EMBL; AY044255; AAL02393.1; -; Genomic_DNA.
DR PIR; JC7767; JC7767.
DR AlphaFoldDB; Q8KR69; -.
DR SMR; Q8KR69; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR UniPathway; UPA00165; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Direct protein sequencing;
KW Glycogen metabolism; Glycosidase; Hydrolase.
FT CHAIN 1..657
FT /note="Glycogen debranching enzyme"
FT /id="PRO_0000054300"
FT REGION 457..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT ACT_SITE 369
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT SITE 441
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
SQ SEQUENCE 657 AA; 74152 MW; FC5206E4B6D925B2 CRC64;
MGELLAGRPR PLGSHFDGEG VNFALFSSGA SRVELCIFDG LREQRLPLTA RTGDIWHGYL
PDAQPGLCYG YRVDGAFDPS RGQRFNANKL LLDPCARQMD GWVVDDQRLH GGYHQPDPSD
SAEVMPPSVV VDEHYDWQGD RLPRTPWSQT VLYEAHVRGL TRRHPGIPAA IRGTYAALAH
PVMLDYLTQL GVTALELMPV QQHADEPRLQ SMGLRNYWGY NTLLPFAVDN SLAASDDPLN
EFRDTVRALH QAGIEVILDV VFNHSAELDV DGPTLTLRGI DNASYYWLTE NGDYHNWAGC
GNVLRLEHPA VLHWVIECLT FWHEVCHVDG FRFDLATILG RLPDFSSSAP FFTALRNHRS
LRDCKLIAEP WDISPGGYQL GQFPAPFAEW NDRFRDDMRR FWLHGDLPIG VLARRFAASS
EVFERGSRQP WASVNMLTSH DGFTLRDLVC FNHKHNDANG EQNRDGTNSN FSFNHGTEGL
EADETTQARR RVSQQALLTT LLLSQGTPML LAGDEFGNSQ QGNNNAYCQD NALAWLHWDQ
ADDALLAFTS GLIRLRRSIP ALQRGRWWRD DDEDDVRWLN AQGEALTPYE WEQGTHQLQI
QLSERWLLLV NATPQVSDFS LPEGEWRVAP PFSATDHLLD GQTWRGQANA VCVLVKQ
