ID   D6Z5X4_DESAT            Unreviewed;       702 AA.
AC   D6Z5X4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Glycogen debranching enzyme GlgX {ECO:0000313|EMBL:ADH84856.1};
GN   OrderedLocusNames=DaAHT2_0143 {ECO:0000313|EMBL:ADH84856.1};
OS   Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfobulbaceae; Desulfurivibrio.
OX   NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH84856.1, ECO:0000313|Proteomes:UP000001508};
RN   [1] {ECO:0000313|Proteomes:UP000001508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19089 / UNIQEM U267 / AHT2
RC   {ECO:0000313|Proteomes:UP000001508};
RG   US DOE Joint Genome Institute;
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., Muyzer G.,
RA   Woyke T.;
RT   "Complete sequence of Desulfurivibrio alkaliphilus AHT2.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; CP001940; ADH84856.1; -; Genomic_DNA.
DR   RefSeq; WP_013162387.1; NC_014216.1.
DR   AlphaFoldDB; D6Z5X4; -.
DR   STRING; 589865.DaAHT2_0143; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; dak:DaAHT2_0143; -.
DR   eggNOG; COG1523; Bacteria.
DR   HOGENOM; CLU_011725_1_1_7; -.
DR   InParanoid; D6Z5X4; -.
DR   OrthoDB; 9760647at2; -.
DR   Proteomes; UP000001508; Chromosome.
DR   GO; GO:0004133; F:glycogen debranching enzyme activity; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005980; P:glycogen catabolic process; IEA:InterPro.
DR   CDD; cd11326; AmyAc_Glg_debranch; 1.
DR   CDD; cd02856; E_set_GDE_Isoamylase_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; IPR011837; Glycogen_debranch_GlgX.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR048644; Isoamylase_C.
DR   NCBIfam; TIGR02100; glgX_debranch; 1.
DR   PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR43002:SF1; ISOAMYLASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   Pfam; PF02922; CBM_48; 1.
DR   Pfam; PF21331; Isoamylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001508}.
FT   DOMAIN          161..569
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          468..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   702 AA;  79615 MW;  625A18D591D74CBD CRC64;
     MSDLKVWPGK PYPLGATFDG EGTNFSLFSS VAERVELCLC DGQGGETRLE LPEVTAYCWH
     GYIPGIRPGQ HYGYRVHGPW EPEQGRRCNP AKLLLDPYAK AVSGQVQWKE AVYPYRFGEP
     ESRNDHDSAP FVPCSVVIEP GFDWGDDRHP ATPWHQTIIY ELHVKGFTKN HPDIPPELRG
     TYAGLAHPAA IGYLQELGIT AVELMPVHQF IHYAHLVEKQ LRNYWGYSTI AFFAPHNEYG
     AASEPGRQVE EFKGMVKALH QAGIEVILDV VYNHTSEGNH LGPMLGLKGI DNAAYYRLTA
     EDPRYYMDYT GTGNSLNMLH PHVLQLIMDS LRYWVLEMHV DGFRFDLAAT LARELHEVDR
     LSAFFDIIQQ DPVISQVKLI AEPWDLGEGG YQVGNFPPLW SEWNGKYRDC VRDYWRGQDR
     TLAEFAGRLT GSSDLYENTG RRPYASINFV TAHDGFTLRD LVSYNDKHNE ANGEENRDGS
     DDNHSWNCGT EGPSDDPAVN ALRARQQRNF LATLFLSQGV PMLLGGDEIG RSQGGNNNAY
     CQDNEISWFN WDQADRELLA FSQRLISFYR EHPVFHRRRW FQGRPIHGAE VADIAWFTPE
     GHEMEEENWG EGYAKSFAVF LNGESLVTKG PRGERIGDDR FYLVFNAHHE ALTFALPGPE
     WAAGWVRVFD TAEGWRDEDK KLDPGGEFEV EARSLGVLRH AS
//