ID GLGB_FRATN Reviewed; 640 AA. AC A0Q593; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 104. 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=FTN_0513; OS Francisella tularensis subsp. novicida (strain U112). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=401614; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=U112; RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102; RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M., RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C., RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J., RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A., RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V., RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.; RT "Comparison of Francisella tularensis genomes reveals evolutionary events RT associated with the emergence of human pathogenic strains."; RL Genome Biol. 8:R102.1-R102.16(2007). 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; CP000439; ABK89408.1; -; Genomic_DNA. DR RefSeq; WP_003038522.1; NZ_CP009633.1. DR AlphaFoldDB; A0Q593; -. DR SMR; A0Q593; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; ftn:FTN_0513; -. DR BioCyc; FTUL401614:G1G75-535-MONOMER; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000000762; Chromosome. 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 3: Inferred from homology; KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism; KW Glycosyltransferase; Transferase. FT CHAIN 1..640 FT /note="1,4-alpha-glucan branching enzyme GlgB" FT /id="PRO_1000044978" FT ACT_SITE 318 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" FT ACT_SITE 371 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" SQ SEQUENCE 640 AA; 74734 MW; 39B55F6664A14247 CRC64; MKNKNSKQNT HSTIGEQDIH YFHEGKHIYA YEFMGAHKAC EGGIEGIRFT TWAPNAKSIC VIGDFNYWQV EDKNYMEPIT DAGLWSVFIP NAKNGDKYKF VVTNKDTNHY VYKSDPYAFF SELRPNTASI ITTETQYTWS DDKWLEKRAK TNYYDNPMNV YELHLASWKT KDGKFMTYDE LSETLPQYIK EMGYTHVEFM PLHEHPLDAS WGYQPTGFYS VNSRHGDIIG LKRLVDKLHN NDIGVILDWV PGHFCKDQHG LIYFDGTPCY EYQEHTKAIN KGWGTHNFDL GRNEVKCFLI SNAMYWINEF HIDGLRVDAV SNILYLNYDR EDGQWIPNIY GGHENLEGIA FLKELNGVLK HTCKGVVTIA EESSSWPDIS TPVEKGGLGF DFKWNMGWMN DTLRYISLDP VYRKYHHNLI TFSMVYHYSE KFILSISHDE VVHGKKSLIN KMWGDLWNKY AGLRLYMSYM IGHPGKKLIF MGSEFGQFVE WREYEQLQWQ VVDQYESHKQ TLHFFKKLND FYHNETALWQ CDYDHHGFRW IDADNSQQSI LSFIRSSKDN KQKLIFICNF TPVTYYDYHL GVPDAGSYKE VFNSDNLEFG GSGQVMATEI FSSPQSSHGF EQRITIKIPP MATLVLKLIK //