GLGX_KLEP3
ID GLGX_KLEP3 Reviewed; 658 AA.
AC B5XTQ8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=KPK_0317;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI08191.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XTQ8; -.
DR SMR; B5XTQ8; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; B5XTQ8; -.
DR EnsemblBacteria; ACI08191; ACI08191; KPK_0317.
DR KEGG; kpe:KPK_0317; -.
DR HOGENOM; CLU_011725_1_1_6; -.
DR OMA; SEPWDCG; -.
DR OrthoDB; 99080at2; -.
DR UniPathway; UPA00165; -.
DR Proteomes; UP000001734; 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..658
FT /note="Glycogen debranching enzyme"
FT /id="PRO_1000165061"
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 658 AA; 73709 MW; 6B2A38CA2345AD5F CRC64;
MTSLAAGKPA PLGASYDGKG VNFALFSAHA ERVELCVFDE QGNEQRVDLP ARSGDIWHGW
LDAAGPGLRY GYRVHGPWDP AQGHRFNPAK LLLDPCAYRV EGDLPDDERL HGGMWEPDHR
DSAAIAPKSQ VVDLHYDWRG DKPPRTPWGE TVIYEAHVKG LTLLHPQLPE AIRGTYKALG
HPVMIAYFKS LGISALELLP VAQFASEPRL QRMGLSNYWG YNPLAWFALD PRYASDPARA
LDEFRDAVKA LHAAGIEVIL DIVLNHSAEI DLEGPTVSLR GIDNRSYYWV REDGDYHNWT
GCGNTLNLSH PGVVEWARQC LRFWVDECHV DGFRFDLASV MGRTPEFRQD APLFEAIRRD
SVLSQVKLIA EPWDIGPGGY QVANFPPLFA EWNDHFRDIS RRFWLQQNVS LGDFAQRFAA
SSDLFARDGK RPSATVNLVT AHDGFTLRDC VCFNQKHNEA NGEENRDGTN NNYSNNHGIE
GLDANLAVIE RRRASVHALL TTLLLAQGTP MLLAGDEQGH SQHGNNNAYC QDNALTWLDW
RQANPGLTAF TAALIHLRRR IPALTRNRWW QEGDGNVRWL NRNAQPLTAG EWQLGAACMQ
IQLSDRWLLT LNATAEVVDM VLPEGEWRAV PPFAGEDNPV IMAVWHGPAH GVCVFQRS