ID GLGB_FRATH Reviewed; 640 AA. AC Q2A4U7; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 1. DT 27-MAR-2024, entry version 111. 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=FTL_0483; OS Francisella tularensis subsp. holarctica (strain LVS). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=376619; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LVS; RA Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S., RA Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R., RA Garcia E.; RT "Complete genome sequence of Francisella tularensis LVS (Live Vaccine RT Strain)."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. 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; AM233362; CAJ78923.1; -; Genomic_DNA. DR RefSeq; WP_011457385.1; NZ_CP009694.1. DR AlphaFoldDB; Q2A4U7; -. DR SMR; Q2A4U7; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; ftl:FTL_0483; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000001944; 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_0000260655" 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; 74923 MW; B041BD846B601814 CRC64; MKNKNSEQNT HYTIGEQDIH YFHEGKHIYA YEFMGAHKAC EEGIEGIRFT TWAPNAKSIC VIGDFNYWQV EDKNYMEPIT DAGLWSVFIP NAKNGDKYKF VVTNKDTSHY VYKSDPYAFF SELRPNTASI ITTETQYTWS DDKWLEKRAK TNYYDNPMNV YELHLASWKT KNGKFLTYDE LSETLPQYIK EMGYTHVEFM PLHEHPLDAS WGYQPTGFYS VNSRHGDIIG LKRLVDKLHN NDIGVILDWV PGHFCKDQHG LIYFDGSPCY EYQEPTKAIN KGWETHNFDL GRNEVKCFLI SNAMYWINEF HIDGLRVDAV SNILYLNYDR EDGQWIPNIY GGHENLEGIA FLKELNGVLK HTCKGVITIA EESSSWPDIS TPVEKGGLGF DFKWNMGWMN DTLRYISLDP VYRKYHHNLI TFSMVYHYSE KFILSISHDE VVHGKKSLIN KMWGDLWNKY AGLRLYMSYM IGHPGKKLIF MGSEFVQFVE WREYEQLQWQ VVDQYESHKQ TLHFFKKLND FYHNETALWQ CDYDHHGFRW IDANNSQQSI LSFIRSSKDN KQKLIFICNF TPVTYYDYHL GVPDAGSYKE VFNSDNLEFG GSGQVMATEI FSSPQSSHGF EQRIIIKIPP MATLVLKLIK //