GLGX_PECCP
ID GLGX_PECCP Reviewed; 658 AA.
AC C6DH78;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-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=PC1_3936;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT14951.1; -; Genomic_DNA.
DR RefSeq; WP_015842032.1; NC_012917.1.
DR AlphaFoldDB; C6DH78; -.
DR SMR; C6DH78; -.
DR STRING; 561230.PC1_3936; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; C6DH78; -.
DR EnsemblBacteria; ACT14951; ACT14951; PC1_3936.
DR KEGG; pct:PC1_3936; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_011725_1_1_6; -.
DR OMA; SEPWDCG; -.
DR OrthoDB; 99080at2; -.
DR UniPathway; UPA00165; -.
DR Proteomes; UP000002736; 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; 2.
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_1000214105"
FT REGION 457..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT ACT_SITE 370
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
FT SITE 442
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01248"
SQ SEQUENCE 658 AA; 74113 MW; 52FB146C2D75648C CRC64;
MAELQTGKPT PLGASFDGQG VNFALFSADA ERVELCIFDE RQQEQRLELT ARSGDIWHGY
LPAAQPGLRY GFRVDGPFEP SQGLRFNPHK LLLDPCARQL DGWVVDDDCL QGGIDQRDER
DSADIMAKCV VTAEDYDWQD DQHPHTLWHQ TVIYEAHVRG LTQLHPDIPE DIRGSYAALG
HPVMIDYLTS LGVTALELLP VQQHADEPRL QQLGLRNYWG YNVLLPFAVD NSLAAGDDAL
NEFRDAVKAL HRAGIEVILD VVFNHSAELD VEGPTLCQRG IDNRSYYWLG ENGEYHNWTG
CGNVLRLNHP AVIDWVMDCL RFWREVCHVD GFRFDLATVL GRTPDFTAAA PLLSAMKNDS
RLQGCKLIAE PWDIGHGGYQ LGQFPTPFAE WSDRYRDDMR RFWLHGDISL GAFARRFAAS
SDIFQQHDRL PFASINKLTA HDGFTLRDLV SFNHKHNDAN GEGNRDGTDS NFSNNHGTEG
LEADDDILQR RLASQKALLT TLILSQGTPM LLAGDELGHS QQGNNNAYCQ DNELTWLHWE
NANSALREFV AGLIQLRRTI PALQQETWWQ EGDGAVQWLN REGQPLTPQQ WEQGEHQLQI
LLSGRWLVLF NASLHAGEFM LPEGHWQVSP PFDETNPPEG GIWHGQAQAV CVLIKQTA
