ID GLGB_BACMK Reviewed; 645 AA. AC A9VMV8; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 02-SEP-2026, entry version 106. DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000255|HAMAP-Rule:MF_00685}; DE EC=2.4.1.18 {ECO:0000255|HAMAP-Rule:MF_00685}; DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000255|HAMAP-Rule:MF_00685}; DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685}; DE AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685}; DE Short=BE {ECO:0000255|HAMAP-Rule:MF_00685}; GN Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685}; GN OrderedLocusNames=BcerKBAB4_4710; OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=315730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KBAB4; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., RA Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). 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:0000255|HAMAP- CC Rule:MF_00685}. 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00685}; CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00685}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00685}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00685}. 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; CP000903; ABY45863.1; -; Genomic_DNA. DR RefSeq; WP_012261905.1; NC_010184.1. DR AlphaFoldDB; A9VMV8; -. DR SMR; A9VMV8; -. DR KEGG; bwe:BcerKBAB4_4710; -. DR eggNOG; COG0296; Bacteria. DR HOGENOM; CLU_004245_4_0_9; -. DR UniPathway; UPA00164; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-UniRule. 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 FunFam; 2.60.40.10:FF:000169; 1,4-alpha-glucan branching enzyme GlgB; 1. DR FunFam; 2.60.40.1180:FF:000002; 1,4-alpha-glucan branching enzyme GlgB; 1. DR FunFam; 3.20.20.80:FF:000003; 1,4-alpha-glucan branching enzyme GlgB; 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; IPR006047; GH13_cat_dom. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR006407; GlgB. DR InterPro; IPR044143; GlgB_N_E_set_prok. DR InterPro; IPR004193; Glyco_hydro_13_N. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR013783; Ig-like_fold. DR NCBIfam; TIGR01515; branching_enzym; 1. DR NCBIfam; NF003811; PRK05402.1; 1. DR NCBIfam; NF008967; PRK12313.1; 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; SSF51011; Glycosyl hydrolase domain; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism; KW Glycosyltransferase; Transferase. FT CHAIN 1..645 FT /note="1,4-alpha-glucan branching enzyme GlgB" FT /id="PRO_1000131811" FT REGION 619..645 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 636..645 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 309 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" FT ACT_SITE 352 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" SQ SEQUENCE 645 AA; 75819 MW; 4BF94A58401C1A13 CRC64; MDVINCEEVK RDEFHTEKYY DSYNIFGAHI VTEDGMRGVR CTVWAPHAKA MSVVGDFNEW DYEQHKMLQV TEEGIWSLFV PHIEENEIYK YAIETMDGDV ILKADPYAVY AEVRPNTASV VFDIEGYEWN DKNWIRKRKK KSIYKEAMTV YELHFGSWKK KEDGALYSYR EMAEELIPYV VEHQFTHIEI MPLVEHPYDR SWGYQGTGYY AATSRFGTPH DLMYFVDECH KYGIGVILDW VPGHFCKDAH GLYLFDGTPT YEYKDRDVQE NLVWGTVNFD LGKREVRNFL ISNALFWMKY FHIDGFRVDA VANMLYWNKE GKEQSNEHAV SFLRELNEAV FAEDEEFLMT AEDSTAWPLV TAPTYEGGLG FNYKWNMGWM NDVLKYMECA PEYRKYIHEK MTFSLIYAHS ENFILPLSHD EVVHGKKSLL NKMPGDYWDK FAQLRLLYGY FFTHPGKKLL FMGGEFGQFD EWKDLEDLDW NLHDFEMHRN MHDYFKELIA LYKRSKPLWQ LDHSPEGFQW IDANNNEQSI FSFIRQGDKQ EDALVVVCNF TKATYENYKV GVPDFEYYNE ILNSDSAQYG GSGQVNKKRL KTILEPYHNQ AAHVEITIPP FGVSILRPVK TRKGSKKQDG SKTKVRSNVT SRGKR //