ID   GLGX_SERP5              Reviewed;         661 AA.
AC   A8GKU9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=Spro_4646;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) 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; CP000826; ABV43739.1; -; Genomic_DNA.
DR   RefSeq; WP_012147321.1; NC_009832.1.
DR   AlphaFoldDB; A8GKU9; -.
DR   SMR; A8GKU9; -.
DR   STRING; 399741.Spro_4646; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; A8GKU9; -.
DR   EnsemblBacteria; ABV43739; ABV43739; Spro_4646.
DR   KEGG; spe:Spro_4646; -.
DR   eggNOG; COG1523; Bacteria.
DR   HOGENOM; CLU_011725_1_1_6; -.
DR   OMA; SEPWDCG; -.
DR   OrthoDB; 99080at2; -.
DR   UniPathway; UPA00165; -.
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..661
FT                   /note="Glycogen debranching enzyme"
FT                   /id="PRO_1000165064"
FT   REGION          460..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   661 AA;  73764 MW;  6AE7B539C2898673 CRC64;
     MTELTPGIAA PLGAYYDGNG INFSLYSAHA TGVELCLFDE QQREVRLPLA TRSGDIWHGY
     LPGGKPGQRY GYRVHGPFDP AQGLRFNPNK LLLDPAARAV EGPVADDPYL HGGYDRPDRH
     DSAELMPKCV VIDEAYDWQD DCPPATPWGK TVIYEAHVRG LTLQHPEIPQ VLRGSFAALG
     HPVMIAYFKR LGITALELLP VQQHSSEPRL QRLGLINYWG YNVLAPYAPD NRYSSLRTDM
     TPLREFRDAV KALHKAGIEV ILDVVFNHSA ELDTDGPTLS LRGIDNPGYY WLTPDGGYVN
     DTGCGNTLRL DQPQGVAWVM DCLRFWVGEC HVDGFRFDLG SVLGRTPAFD RDAPLFQAML
     ADDLLSRCKL IAEPWDIGPG GYQVGEFPGR FAEWNDHYRD DMRRFWLQGD ISLGQFAQRF
     AASSDLFNQR GRAPYASINM LTAHDGFTLQ DLVSFSRKHN QLNGEGNRDG SDRNFSNNHG
     VEGPIADDAI VQRRRASRQA LLATLLLSQG TPMLLAGDEH GHSQQGNNNA YCQDNAITWL
     DWATADDSLT AYTAALIHLR QQIPALQHDR WWQEGDGNVQ WLNAQGQSLS AQQWEQGDLQ
     LQICLSQRWL VVVNATQQAV EMTLPAGDWQ LVAPFTQEDS RAVLPAWNQA AHSICVLVKK
     K