ID GLGB_ACTSZ Reviewed; 829 AA. AC A6VP15; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 108. 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=Asuc_1352; OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 / OS 130Z). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=339671; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z; RX PubMed=21118570; DOI=10.1186/1471-2164-11-680; RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A., RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L., RA Burkhart K.B., Harkins V., Vieille C.; RT "A genomic perspective on the potential of Actinobacillus succinogenes for RT industrial succinate production."; RL BMC Genomics 11:680-680(2010). 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; CP000746; ABR74712.1; -; Genomic_DNA. DR AlphaFoldDB; A6VP15; -. DR SMR; A6VP15; -. DR STRING; 339671.Asuc_1352; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; asu:Asuc_1352; -. DR eggNOG; COG0296; Bacteria. DR HOGENOM; CLU_004245_3_2_6; -. DR OrthoDB; 9800174at2; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000001114; 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; 2. 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; 2. 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..829 FT /note="1,4-alpha-glucan branching enzyme GlgB" FT /id="PRO_1000072735" FT REGION 758..829 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 778..793 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 804..818 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 405 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" FT ACT_SITE 458 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" SQ SEQUENCE 829 AA; 94021 MW; 5BE0A3BD25EFE7A5 CRC64; MTTFVTQDTI NAFFDGRHAD PFAVLGMHET DNGIEIRALL PDAGRVVVID KETQDEVCEL SRIDERGFFA GIMPQRNSFF NYQLQVSWGN EVLRIEDPYR FHPMIQELDN WLLAEGSHLR PYEVLGAHFM ECDHVSGVNF RLWAPNAKRV SVVGDFNYWD GRRHPMRFHQ ASGVWELFIP KVALGDLYKF ELLDNNNRLR LKSDPYAFAA QLRPDTASQI SVLPEIQEMT AARRKANQLD QPISIYEVHL GSWRRNLANN FWLNYDEIAD ELIPYVKEMG FTHIELLPIS EFPFDGSWGY QPIGLYAPTS RFGSPEGFKR FVDKAHAAGI NVILDWVPGH FPSDTHGLAT FDGTALYEHA DPKEGYHQDW NTLIYNYGRH EVKNYLSGNA LYWVERFGLD GIRVDAVASM IYRDYSRRDG EWIPNQYGGR ENLEAIEFLK HTNYILGTEH PGVMCVAEES TAFAGVTLPP ENGGLGFNFK WNMGWMNDTL SYMKLDPIYR QYNHSKLTFG MLYQYSENFV LPLSHDEVVH GKCSLLDKMP GDTWQKFANL RAYYGYMWAY PGKKLLFMGN EFAQGREWNY QESLDWYLLD EFHGGGWHSG VQRLVKDLNK TYQKQSALYQ LDTKPEGFEW LVVDDAQNSV FVFERRNAKG EPLIVVSNFT PVPRENYRFG VNVAGSYEEI LNTDADIYKG SGLNNGGVID SEEIESHGKT QSISITVPPL ATVYFKLKSA RKVASPRKVT KKKTTADGAE ATAKNASASK ATKVSTKKTV KSSEAKPVKA ATKSSVTKVA TKKSTDKPTA KATRTKKATV TKTAKASAKT TAKKTKDNA //