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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//