ID GLGB_BRADU Reviewed; 721 AA. AC Q89FD3; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 02-SEP-2026, entry version 138. 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=blr6768; OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / OS NBRC 14792 / USDA 110). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium. OX NCBI_TaxID=224911; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110; RX PubMed=12597275; DOI=10.1093/dnares/9.6.189; RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.; RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium RT Bradyrhizobium japonicum USDA110."; RL DNA Res. 9:189-197(2002). 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; BA000040; BAC52033.1; -; Genomic_DNA. DR AlphaFoldDB; Q89FD3; -. DR SMR; Q89FD3; -. DR FunCoup; Q89FD3; 601. DR STRING; 224911.AAV28_31440; -. DR PaxDb; 224911-AAV28_31440; -. DR EnsemblBacteria; BAC52033; BAC52033; BAC52033. DR KEGG; bja:blr6768; -. DR PATRIC; fig|224911.5.peg.6935; -. DR eggNOG; COG0296; Bacteria. DR HOGENOM; CLU_004245_3_2_5; -. DR InParanoid; Q89FD3; -. DR OrthoDB; 9800174at2; -. DR PhylomeDB; Q89FD3; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000002526; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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; IBA:GO_Central. 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; IPR054169; GlgB_N. 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 InterPro; IPR014756; Ig_E-set. 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 Pfam; PF22019; GlgB_N; 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 3: Inferred from homology; KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism; KW Glycosyltransferase; Reference proteome; Transferase. FT CHAIN 1..721 FT /note="1,4-alpha-glucan branching enzyme GlgB" FT /id="PRO_0000188688" FT ACT_SITE 404 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" FT ACT_SITE 457 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" SQ SEQUENCE 721 AA; 81677 MW; 41622A1E97207F87 CRC64; MPRAKPMPKL PAEAYAIIEG RHADPFHYLG LHPEGGKSVV RAFLPEASNV EAVGEHGEVA RLDRVHDAGL FVGALPNGSK HYQLRAKFGD SIVEFEDAYR FPPILTDFDL YLLGEGTHQR LYDKLGAHPM TLDGVDGIGF VVLAPNARRV SVVGDFNFWD SRRHPMRVRG SGYWELFIPH AKRGDHYKFD IVGPHGHQLP LKSDPMAFAS EVRPKTASIV FDEAHLPRPR PAPDGINALS APMSIYEVHL GSWRRKGDNE WLTYRELAEQ LPAYARDMGF THLEFLPVSE HPFDGSWGYQ PTGLYAPTSR FGTPEDFAAL VDACHREGVG VLLDWVPGHF PDDPHGLGSF DGTSLYEHAN PLQGRHLDWG TLIYNYGRTE VTNFLVSNAL FWLERYAIDG LRVDAVASML YLDYSRPPGA WIPNQYGGRE NIEAIAFLRR FNTELFARFP QATTAAEEST AWPQVSRPVE FGGLGFGYKW NMGWMHDTLN YISKDPIHRK HHHGEILFGL HYAFSENFIL PLSHDEVVHG KRSILGRMPG DEWQRFANLR AYYSFMFGHP GKKLLFMGAE IAQSREWNHD QSLDWHLLEY KYHSGIQALI RDLNRLYRAV PALHQMDCDQ AGFEWLITDD ANRNVFAWLR KGLDEHARCL VIVNFSPNVY RNYRVRVPFA GKWKEVLNSD SAHYGGSNVG NIGEVHAVDG KTPELRLTIP PLAAIFLVPE S //