ID   GLGB_BACCL              Reviewed;         666 AA.
AC   P30537;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   13-SEP-2023, entry version 107.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB;
DE            EC=2.4.1.18;
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase;
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme;
DE   AltName: Full=Glycogen branching enzyme;
DE            Short=BE;
GN   Name=glgB;
OS   Bacillus caldolyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1296817; DOI=10.3109/10425179209034021;
RA   Kiel J.A.K.W., Boels J.M., Beldman G., Venema G.;
RT   "The glgB gene from the thermophile Bacillus caldolyticus encodes a
RT   thermolabile branching enzyme.";
RL   DNA Seq. 3:221-232(1992).
CC   -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages
CC       in glycogen by scission of a 1,4-alpha-linked oligosaccharide from
CC       growing alpha-1,4-glucan chains and the subsequent attachment of the
CC       oligosaccharide to the alpha-1,6 position. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC         primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is about 39 degrees Celsius.;
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; Z14057; CAA78440.1; -; Genomic_DNA.
DR   PIR; B56639; B56639.
DR   AlphaFoldDB; P30537; -.
DR   SMR; P30537; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   UniPathway; UPA00164; -.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd11322; AmyAc_Glg_BE; 1.
DR   CDD; cd02855; E_set_GBE_prok_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   HAMAP; MF_00685; GlgB; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR037439; Branching_enzy.
DR   InterPro; IPR006407; GlgB.
DR   InterPro; IPR044143; GlgB_N_E_set_prok.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   NCBIfam; TIGR01515; branching_enzym; 1.
DR   PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   PIRSF; PIRSF000463; GlgB; 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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..666
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000188677"
FT   REGION          622..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        309
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        352
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   666 AA;  78096 MW;  1F64C31495BB1B6E CRC64;
     MIAANPTDLE VYLFHEGRLY QSYELFGAHV IRGGGAVGTR FCVWAPHARE VRLVGSFNDW
     NGTNSPLTKV NDEGVWTIVV PENLEGHLYK YEIITPDGRV LLKADPYAFY SELRPHTASI
     VYDLKGYEWN DSPWQRKKRR KRIYDQPMVI YELHFGSWKK KPDGRFYTYR EMADELIPYV
     LERGFTHIEL LPLVEHPLDR SWGYQGTGYY SVTSRYGTPH DFMYFVDRCH QAGLGVIIDW
     VPGHFCKDAH GLYMFDGAPT YEYANEKDRE NYVWGTANFD LGKPEVRSFL ISNALFWLEY
     YHVDGFRVDA VANMLYWPNN DRLYENPYAV EFLRQLNEAV FAYDPNVWMI AEDSTDWPRV
     TAPTYDGGLG FNYKWNMGWM NDMLKYMETP PHERKYAHNQ VSFSLLYAYS ENFILPFSHD
     EVVHGKKSLL NKMPGSYEEK FAQLRLLYGY MMAHPGKKLL FMGSEFAQFD EWKFAEELDW
     VLFDFELHRK MDEYVKQLIA CYKRYKPFYE LDHDPRGFEW IDVHNAEQSI FSFIRRGKKE
     GDVLVIVCNF TNQAYDDYKV SVPLLAPYRE VLNSDAAEFG GSGHVNGKRL PAFSEPFHGK
     PYHVRMTIPP FGISILRPVQ KRGERKQNEE EVHRHVIGRR ARKPASLADE KHRETSRAVW
     GEVPDH
//