GLGX_PECAS
ID GLGX_PECAS Reviewed; 658 AA.
AC Q6CZK1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 113.
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=ECA4150;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG77047.1; -; Genomic_DNA.
DR RefSeq; WP_011095621.1; NC_004547.2.
DR AlphaFoldDB; Q6CZK1; -.
DR SMR; Q6CZK1; -.
DR STRING; 218491.ECA4150; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; CAG77047; CAG77047; ECA4150.
DR GeneID; 57210813; -.
DR KEGG; eca:ECA4150; -.
DR PATRIC; fig|218491.5.peg.4223; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_011725_1_1_6; -.
DR OMA; SEPWDCG; -.
DR OrthoDB; 99080at2; -.
DR UniPathway; UPA00165; -.
DR Proteomes; UP000007966; 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;
KW Reference proteome.
FT CHAIN 1..658
FT /note="Glycogen debranching enzyme"
FT /id="PRO_1000165059"
FT REGION 457..481
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; 74000 MW; 0C36AB4B51EF0672 CRC64;
MAELQTGKPT PLGASFDGNG VNFALFSADA ERVELCVFDE RQQEQRIVLT ARSGDIWHGY
LPDAQPGLRY GFRVDGPFEP SQGLRFNPHK LLLDPCARQL DGWVVDDASL QGGIDQRDER
DSAEIMAKCV VTAEDYDWQD DQHPQTPWNQ TVIYEAHVRG LTQLHPDIPE DIRGSYAALG
HPVMIDYLTS LGITALELLP VQQHADEPRL QQIGLRNYWG YNVLLPFAVD NSLAAGDDAL
NEFRDAVKAL HNAGIEVILD VVFNHSAELD VEGPTLCQRG IDNRSYYWLG DSGEYHNWTG
CGNVLRLNHP AVMDWVMDCL RFWREVCHVD GFRFDLATVL GRTPDFTAAA PLLSAMKNDN
RLQGCKLIAE PWDIGHGGYQ LGQFPTPFAE WSDRYRDDMR RFWLHGDISL GAFARRFAAS
SDIFQQRDRL PYASINKLTA HDGFTLRDLV SFNHKHNDAN GEGNRDGTDS NFSNNHGTEG
LEADDDIHQR RQASQKALLT TLILSQGTPM LLAGDELGHS QQGNNNAYCQ DNELTWLHWD
HADRGLREFV AGLIQLRRTI PALQQETWWQ EGDGAVQWLN REGQPLTPPQ WEQGEHQLQI
LLSGRWLVLV NASLHAGAFM LPEGHWQVSP PFDETNPPEG GMWHGQAQAV CVLIKQTA
