ID C9Y5I9_CROTZ Unreviewed; 692 AA.
AC C9Y5I9;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Glycogen operon protein glgX homolog {ECO:0000313|EMBL:CBA34634.1};
DE EC=3.2.1.68 {ECO:0000313|EMBL:CBA34634.1};
GN Name=glgX {ECO:0000313|EMBL:CBA34634.1};
GN OrderedLocusNames=Ctu_1p00970 {ECO:0000313|EMBL:CBA34634.1};
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OG Plasmid pCTU1 {ECO:0000313|EMBL:CBA34634.1,
OG ECO:0000313|Proteomes:UP000002069}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA34634.1, ECO:0000313|Proteomes:UP000002069};
RN [1] {ECO:0000313|Proteomes:UP000002069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC {ECO:0000313|Proteomes:UP000002069};
RC PLASMID=pCTU1 {ECO:0000313|Proteomes:UP000002069};
RX PubMed=21037008; DOI=10.1128/JB.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; FN543094; CBA34634.1; -; Genomic_DNA.
DR AlphaFoldDB; C9Y5I9; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; ctu:Ctu_1p00970; -.
DR PATRIC; fig|693216.3.peg.4084; -.
DR HOGENOM; CLU_011725_1_1_6; -.
DR Proteomes; UP000002069; Plasmid pCTU1.
DR GO; GO:0004133; F:glycogen debranching enzyme activity; IEA:InterPro.
DR GO; GO:0019156; F:isoamylase activity; IEA:UniProtKB-EC.
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:SF9; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF00128; Alpha-amylase; 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;
KW Glycosidase {ECO:0000313|EMBL:CBA34634.1};
KW Hydrolase {ECO:0000313|EMBL:CBA34634.1};
KW Plasmid {ECO:0000313|EMBL:CBA34634.1}.
FT DOMAIN 170..576
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 471..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 78929 MW; 331D13E6FD3185DA CRC64;
MSNDKAFEIT AGCSYPLGAN YDGEGVNFAI FSAHAERVEL CLYDPSGKHE IARLTLPEYT
HEVWHGYVPG LQPGALYGYR VHGPYDPENG HRFNPNKLLV DPYARDLVGN IEWNEAHFAY
DLLHEDKDLT FDERDSAPYM PKCRVIDPNE FDWQDQNRPS VVWPHTVVYE THVKGFTQLN
PAIPPELRGT YDGMAHKASV DYIKSLGITS VELLPVHWFP DDQHLLDKGL KNFWGYNSLN
FFAPASRYFG PRGIQGFRDM VRAYHDAGIE VILDVVYNHT AEGNELGPTL SFKGIDNFSY
YRTMPDQHRY YINDTGTGNT VNTSHPRVLQ MVMDSLRYWA ESMHIDGFRF DLGTILGREP
EGFDQRGGFF DAIMQDPVLS KVKLIGEPWD IGPGGYQVGG FPPGWAEWND KYRDTVREYW
KGDNVSTDFA ARLLGSGDLY DQRGRRPWAS VNFITAHDGF TLNDLVSYNG KHNEDNGEDN
NDGHNDNRSY NYGAEGPTDD EGINAVRERQ KRNFLATLFF SHGTPMLLAG DEFGRSQMGN
NNGYCQDSEI SWVHWENLPE SAEALREFTR HVIRLRAEQP LLRRESWRDG MEIKWFNAGG
GLQTPEQWDE GSTLGLYIGR SDLQEQEGIW HDVLMLFNPF EGTVPFRIPQ FGEEGGWVLE
LTTSDTANHG LVITKEKDFE LEGRSIALFR RP
//
