ID A0A6J4KF50_9BACT Unreviewed; 736 AA. AC A0A6J4KF50; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 07-APR-2021, entry version 4. DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000256|HAMAP-Rule:MF_00685}; DE EC=2.4.1.18 {ECO:0000256|HAMAP-Rule:MF_00685}; DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000256|HAMAP-Rule:MF_00685}; DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685}; DE AltName: Full=Glycogen branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685}; DE Short=BE {ECO:0000256|HAMAP-Rule:MF_00685}; GN Name=glgB {ECO:0000256|HAMAP-Rule:MF_00685}; GN ORFNames=AVDCRST_MAG68-617 {ECO:0000313|EMBL:CAA9303009.1}; OS uncultured Gemmatimonadetes bacterium. OC Bacteria; Gemmatimonadetes; environmental samples. OX NCBI_TaxID=203437 {ECO:0000313|EMBL:CAA9303009.1}; RN [1] {ECO:0000313|EMBL:CAA9303009.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AVDCRST_MAG68 {ECO:0000313|EMBL:CAA9303009.1}; RA Meier V. D.; RL Submitted (FEB-2020) 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:0000256|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:0000256|ARBA:ARBA00000826, ECO:0000256|HAMAP- CC Rule:MF_00685}; CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00685}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB CC subfamily. {ECO:0000256|ARBA:ARBA00009000, ECO:0000256|HAMAP- CC 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; CADCTW010000034; CAA9303009.1; -; Genomic_DNA. DR UniPathway; UPA00164; -. 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; cd02855; E_set_GBE_prok_N; 1. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 2.60.40.1180; -; 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 PANTHER; PTHR43651; PTHR43651; 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; SSF51445; 1. DR SUPFAM; SSF81296; SSF81296; 2. DR TIGRFAMs; TIGR01515; branching_enzym; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_00685}; KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP- KW Rule:MF_00685}; KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP- KW Rule:MF_00685}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_00685}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00685}. FT DOMAIN 255..625 FT /note="Aamy" FT /evidence="ECO:0000259|SMART:SM00642" FT ACT_SITE 414 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685, FT ECO:0000256|PIRSR:PIRSR000463-1" FT ACT_SITE 467 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685, FT ECO:0000256|PIRSR:PIRSR000463-1" SQ SEQUENCE 736 AA; 83865 MW; 679269D5604FEB7A CRC64; MAQATLQHDV RQIVRGEHND PFRVLGMHRV AVAGEIRLVV RAFIPGAREV ALLGTGIVSP RTLQRVNDDG FFEGLLPRGT EPFAYQLRVT WEDGSVVEMA DAYSFSSTVA EFDLYLIGEG THLRLYDVLG AHPDEIGGVQ GVRFAVWAPA AQRVSVVGEF NGWDGRRHTL RRHPGVGIWE MFIPGIPAGT AYKYELRGPH GEIFLKSDPV AFYAEHNPAT ASVVADLRGF EWTDDEWMER RRGEPGKDRP MAVYEVHLGS WKRVPEEGDR PLTYREMAHQ LGEYVTEMGF THVELLPVME HPYDPSWGYQ VTGYFAPTSR FGKPEDFKYL VNHLHSLGIG VILDWVPAHF PKDAHALRRF DGTALYEHED PRQGEHPDWG TLVFNFGRNE VRNFLLSNAL FWIDEYHADG LRVDAVASML YLDYSRQPGQ WVPNRYGGRE NLEAIDFLQQ LNATMRDRYP GALMIAEEST AWPGVTQPPH LGGLGFHMKW NMGWMNDFLR FVEEDPVYRK YHFNLITFSL MYAFSERFVL PFSHDEVVHL KGSLIGKMPG DAWQKAANLR MALGFMWSHP GKKLIFMGGE FGQWSEWSEG RSLDWHLLEN PLNAGVQRWM RDLNALYTKE RAFWDSDCTH EGFQWIDFHD VEQTVLSFLR RSTDTGEELL FACNFTPVPR PGYRIGVPRA GTYRELLNSD SAVYGGSNLG NHGSVASEPV PEHGRADSVR LMLPPLSILV LKRDEE //