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 24-JAN-2024, entry version 109. 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; Bacillota; 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; 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; 2. 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..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 //