ID GLGB_SALRD Reviewed; 622 AA. AC Q2S4A0; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 116. 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=SRU_0846; OS Salinibacter ruber (strain DSM 13855 / M31). OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae; OC Salinibacter. OX NCBI_TaxID=309807; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13855 / CECT 5946 / M31; RX PubMed=16330755; DOI=10.1073/pnas.0509073102; RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., RA Legault B., Rodriguez-Valera F.; RT "The genome of Salinibacter ruber: convergence and gene exchange among RT hyperhalophilic bacteria and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005). 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; CP000159; ABC44792.1; -; Genomic_DNA. DR RefSeq; WP_011403610.1; NC_007677.1. DR RefSeq; YP_444981.1; NC_007677.1. DR AlphaFoldDB; Q2S4A0; -. DR SMR; Q2S4A0; -. DR STRING; 309807.SRU_0846; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblBacteria; ABC44792; ABC44792; SRU_0846. DR KEGG; sru:SRU_0846; -. DR PATRIC; fig|309807.25.peg.872; -. DR eggNOG; COG0296; Bacteria. DR HOGENOM; CLU_004245_3_2_10; -. DR OrthoDB; 9761875at2; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000008674; 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; Reference proteome; Transferase. FT CHAIN 1..622 FT /note="1,4-alpha-glucan branching enzyme GlgB" FT /id="PRO_0000260696" FT REGION 581..606 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 306 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" FT ACT_SITE 358 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" SQ SEQUENCE 622 AA; 71450 MW; D14B40C53CD8B114 CRC64; MPHLTDDDIY YWRQGTHTHS YERMGAHPNQ RGTWFGVWAP NADRVEVTGD FNDWRFGADV LDRREGGLWE GYVRGAQPGD KYKYHLRAGG EWFDRTDPYA FRMEPPAQNT YEGLSALITD LDTYTWGDDA WMTTREGPSG IDGPLSIYEV HLGSWRHEEH GASLSYREVA EPLADHVQNL GFTHVEFLPL AEHPYYGSWG YQILGYYAPT FRYGDPEGLM HLIDTLHQRG IGVIMDWVPG HFATDPQGLT YFDGSHLFEY EDPLMREHPD WGTRVFDFGK NGVRNFLLSN ALFWMDKYHV DGLRVDAVAS MLYRDYSREG DWSPNVHGGR ENLGAISLLQ DTNEHVYDEY PEAIMLAEES TAWPGVTTPT EHGGLGFLYK WNMGWMHDTL EYASKEPVHR KHHHGDLTWT LSWAFSENYT LPLSHDEVVH GKNSLWSKMP GDDWQKAANL RLLYAHMFGH PGKKLLFMGG EFGQHREWDH DRALEWDLAD EPLHEGLMEW LGDLNHLYQN APALWNDQED GFEWIAYDDR ENSVLTYRRL NGDRSLVFVL NFTPVVREDY RIGATGDGRW HERLNSDSDV YGGSNVGNRG AVHSDPVEKH GHSHSLSLTL PPLGALVLEP AE //