ID   GLGB_GEOSE              Reviewed;         639 AA.
AC   P30538;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 104.
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   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1503-4R;
RX   PubMed=1745226; DOI=10.1007/bf00290661;
RA   Kiel J.A.K.W., Boels J.M., Beldman G., Venema G.;
RT   "Molecular cloning and nucleotide sequence of the glycogen branching enzyme
RT   gene (glgB) from Bacillus stearothermophilus and expression in Escherichia
RT   coli and Bacillus subtilis.";
RL   Mol. Gen. Genet. 230:136-144(1991).
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 55 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}.
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; M35089; AAA22482.1; -; Genomic_DNA.
DR   PIR; S18599; S18599.
DR   AlphaFoldDB; P30538; -.
DR   SMR; P30538; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   BRENDA; 2.4.1.18; 623.
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; cd02855; E_set_GBE_prok_N; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 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   PANTHER; PTHR43651; PTHR43651; 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; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR01515; branching_enzym; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..639
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000188682"
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   639 AA;  74795 MW;  F5BD4446B371E03A CRC64;
     MIAVGPTDLE IYLFHEGSLY KSYELFGAHV IKKNGMVGTR FCVWAPHARE VRLVGSFNEW
     NGTNFNLMKV SNQGVWMIFI PENLEGHLYK YEITTNDGNV LLKSDPYAFY SELRPHTASI
     VYNIKGYQWN DQTWRRKKQR KRIYDQPLFI YELHFGSWKK KEDGSFYTYQ EMAEELIPYV
     LEHGFTHIEL LPLVEHPFDR SWGYQGIGYY SATSRYGTPH DLMYFIDRCH QAGIGVILDW
     VPGHFCKDSH GLYMFDGAPA YEYANMQDRE NYVWGTANFD LGKPEVRSFL ISNALFWMEY
     FHVDGFRVDA VANMLYWPNS DVLYKNTYAV EFLQKLNETV FAYDPNILMI AEDSTDWPRV
     TAPTYDGGLG FNYKWNMGWM NDILTYMETP PEHRKYVHNK VTFSLLYAYS ENFILPFSHD
     EVVHGKKSLL SKMPGTYEEK FAQLRLLYGY LLTHPGKKLL FMGGEFGQFD EWKDLEQLDW
     MLFDFDMHRN MNMYVKELLK CYKRYKPLYE LDHSPDGFEW IDVHNAEQSI FSFIRRGKKE
     DDLLIVVCNF TNKVYHGYKV GVPLFTRYRE VINSDAIQFG GFGNINPKPI AAMEGPFHGK
     PYHIQMTIPP FGISILRPVK KGSVKSFMKT PHPPSHGAS