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Database: UniProt
Entry: D1BCZ1_SANKS
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ID   D1BCZ1_SANKS            Unreviewed;       822 AA.
AC   D1BCZ1;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   SubName: Full=Glycogen debranching enzyme GlgX {ECO:0000313|EMBL:ACZ20989.1};
GN   OrderedLocusNames=Sked_10400 {ECO:0000313|EMBL:ACZ20989.1};
OS   Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC   Sanguibacter.
OX   NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ20989.1, ECO:0000313|Proteomes:UP000000322};
RN   [1] {ECO:0000313|EMBL:ACZ20989.1, ECO:0000313|Proteomes:UP000000322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74
RC   {ECO:0000313|Proteomes:UP000000322};
RX   PubMed=21304646;
RA   Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C.,
RA   Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A.,
RA   Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., Pukall R.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Sanguibacter keddieii type strain (ST-74).";
RL   Stand. Genomic Sci. 1:110-118(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; CP001819; ACZ20989.1; -; Genomic_DNA.
DR   RefSeq; WP_012866058.1; NC_013521.1.
DR   AlphaFoldDB; D1BCZ1; -.
DR   STRING; 446469.Sked_10400; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ske:Sked_10400; -.
DR   eggNOG; COG1523; Bacteria.
DR   HOGENOM; CLU_011725_1_1_11; -.
DR   OMA; WVTEMGV; -.
DR   Proteomes; UP000000322; 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   NCBIfam; TIGR02100; glgX_debranch; 1.
DR   PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR43002:SF3; ISOAMYLASE 3, CHLOROPLASTIC; 1.
DR   Pfam; PF02922; CBM_48; 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;
FT   DOMAIN          244..665
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          140..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..589
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   822 AA;  88560 MW;  12D8D5DFC4ACFF10 CRC64;
     MSDTRAASVH GPVPPFGVHL DGGGVRVSVL ASHATAVDLC LIDVVHTAPG VEPRFTERRV
     RLTEQAYGVW HGYVPGVHEG QRYGFRTHGP WDPAAGLRHN PAKLLVDPYA RGLLGDLDLG
     PETYGHVTRL EDVVPSASAS DVSGAADASG AAGGPAPAGA TGDAATARAA GTAGSASTAP
     GTDLVALPGV PRTRTPMLGR HVVGDPYGPA DDRDSLGSVP HSVVVGPRHH HPPVRRPQVP
     WRDTVIYEAH VRGLTKNLEA LPEELRGTYA GLAHPATVAH LKDLGITTVE LLPIHASVPE
     PHLATKGLTN YWGYNTIGFF APHAAYATAA AQAAGPGAVL DEVKGMVHLL HEAGLEVLLD
     VVYNHTCEGG APGQHLSWRG LDNSVYYVHD GGSPARLVDH TGCGNSLDFR RPRVVQMALD
     SLRYWAQEVG VDGFRFDLAV TLGRDGAGFT STHPFLVGLQ TDPVINQLKL VAEPWDVGMG
     GWQTGGFPAP MAEWNDRFRN ATRSFWLSDP AAAAHGRGGH GIRELATRLA GSADLFGHSD
     PPLVRGAIAS VNYVTAHDGF TMADLVAYDH KHNQANGEDG RDGSDDNRSW NHGLEGPVPS
     DSLGMEIAPL RRRSIRNLMG MLLLSAGTPM ITAGDEIGRT QRGNNNAYCQ DGEISWTRWD
     LDPWREDLLE TTRHLLRLRR EHLALRVDGF FLGHPQPDDE PGQPDLAWYD AAASPVSHEQ
     WHDTSTRIVQ MLRRERRGHD AEEVDDSHVL LVLNGTLDDV HVTLAGRGNS TRAWTLAWDS
     AWERPDEREL TVAGAPHDVA AGTEVHLEPL SMQVYLAYED RA
//
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