ID E6U338_ETHHY Unreviewed; 634 AA. AC E6U338; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAR-2024, entry version 78. 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 OrderedLocusNames=Ethha_1992 {ECO:0000313|EMBL:ADU27510.1}; OS Ethanoligenens harbinense (strain DSM 18485 / JCM 12961 / CGMCC 1.5033 / OS YUAN-3). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Ethanoligenens. OX NCBI_TaxID=663278 {ECO:0000313|EMBL:ADU27510.1, ECO:0000313|Proteomes:UP000001551}; RN [1] {ECO:0000313|EMBL:ADU27510.1, ECO:0000313|Proteomes:UP000001551} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18485 / JCM 12961 / CGMCC 1.5033 / YUAN-3 RC {ECO:0000313|Proteomes:UP000001551}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Wang A., RA Mouttaki H., He Z., Zhou J., Hemme C.L., Woyke T.; RT "Complete sequence of Ethanoligenens harbinense YUAN-3."; RL Submitted (DEC-2010) 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. CC {ECO:0000256|ARBA:ARBA00002953, ECO:0000256|HAMAP-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; CP002400; ADU27510.1; -; Genomic_DNA. DR RefSeq; WP_013485858.1; NZ_CP025286.1. DR AlphaFoldDB; E6U338; -. DR STRING; 663278.Ethha_1992; -. DR KEGG; eha:Ethha_1992; -. DR eggNOG; COG0296; Bacteria. DR HOGENOM; CLU_004245_3_2_9; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000001551; 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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. 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 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; SSF51011; Glycosyl hydrolase domain; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_00685}; Cellulose degradation {ECO:0000256|ARBA:ARBA00023001}; 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}; Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001}; KW Reference proteome {ECO:0000313|Proteomes:UP000001551}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00685}. FT DOMAIN 156..516 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT ACT_SITE 313 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685, FT ECO:0000256|PIRSR:PIRSR000463-1" FT ACT_SITE 366 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685, FT ECO:0000256|PIRSR:PIRSR000463-1" SQ SEQUENCE 634 AA; 73621 MW; B7417F916BBDD377 CRC64; MYTNAPKKTG REQELQCFHE SVYPLSFEYF GGHSSHRSKK SGVVFRVWAP KAVSVSIVGD FNNWDASKNP MISVDDQGVW EGFVPGIKSF DIYKYQIETA DGKTLLKSDP YATHMETRPD TASRYYNLSG YHWKDQEWQK KKEKKSAYDV PMNIYELHAG SWKKYPDGNP FEYRKLAEEL IPYLQKMGYT HVELMPIMEY PLDNSWGYQV TGYFAPTSRY GSPRDFMAFV DYCHQADIGV IMDWVPAHFP KDAHGLYRFD GDCCYEYTDP LKQEHKSWGT CVFDYSKSEV RSFLVSNAIF WLQKYHIDGL RVDAVASMLY LDYDRKNGEW RPNQYGGHEN LEAVSFLQEL NREVFSRFPN ALMIAEESTA WPLVTKPVDV GGLGFNFKWN MGWMNDMLDY VSTDPYFRKD HHKDITFSFH YAFSENYILP ISHDEVVHGK RSLLEKMPGD KAEQFAGVRV FLAYMIAHPG KKLLFMGSEF GQVHEWDCHD ALQWQLLGEK GHQNLQDFTA ALNHFYLDQS PLWQNDFSWE GFQWISYDDN LQNIIAFRRI DRKGEELVCL FNFAPVKRDD YRIGIPAAGY YQEAFNTDAE QFGGTGESNK EPVPTEKIPL HGYQQSIALT VPPMAALFLK HQPK //