ID GLGB_RHILO Reviewed; 737 AA. AC Q985P4; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 27-MAR-2024, entry version 133. 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=mlr7587; OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OS (Mesorhizobium loti (strain MAFF 303099)). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=266835; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099; RX PubMed=11214968; DOI=10.1093/dnares/7.6.331; RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., RA Tabata S.; RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium RT Mesorhizobium loti."; RL DNA Res. 7:331-338(2000). 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; BA000012; BAB54018.1; -; Genomic_DNA. DR RefSeq; WP_010914966.1; NC_002678.2. DR AlphaFoldDB; Q985P4; -. DR SMR; Q985P4; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; mlo:mlr7587; -. DR PATRIC; fig|266835.9.peg.6068; -. DR eggNOG; COG0296; Bacteria. DR HOGENOM; CLU_004245_3_2_5; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000000552; 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; 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..737 FT /note="1,4-alpha-glucan branching enzyme GlgB" FT /id="PRO_0000188734" FT ACT_SITE 419 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" FT ACT_SITE 472 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" SQ SEQUENCE 737 AA; 82526 MW; BF88CA1D72A8AAEB CRC64; MRKPRVTAAT SGPDGLAPAS DVAAIVAGTH GDPFAVLGVH EVGKGLFARC FVPHAETVTA YTLTGIEAGA LSRRDDAGFF EGKLSIKKRQ PLRYHAHNAG GDWWLTDPYS FGPVLGPMDD YYIAEGSHLR LFDKLGAHVI EHEGATGVHF AVWAPNAKRV SVVGDFNDWD GRRHTMRDRR DTGIWEVFIP DIGAGRPYKY EIIGPDGVRL PLKADPFAFK SELRPATASV VAVPPAHDWG DEAHRNYWRN ADPRREAVSI YEVHAGSWQL HDDGTFLSWD ELADRLIPYV VETGFTHIEF MPISEHPYDP SWGYQTTGLY APSARFGDPD GFARFVDGAH RAGVGVILDW VPAHFPVDAH GLAHFDGTAL YEHADPRKGF HPDWNTAIYN FGRREVVSFL VNNALFWAEK YHVDGLRVDA VASMLYLDYS RKAGEWIPNE KGGRENLEAV SFLQKMNKEV YGHHPGVMTI AEESTSWPKV SAPVHEGGLG FGFKWNMGFM HDTLEYFSKE PIFRKHHHND LTFGLTYAFS ENFVLPLSHD EVVHGKGTLL SKMAGDDWQK FATLRAYYGF MWGYPGKKLL FMGQEFAQRR EWSEARALDW NLLDFRPHRG VWQTVRDLNY LYRSRPALHG RDCEPEGFSW LIVDDSQNSV FAWVRNAPGG SPVAVISNFT PVPRDNYRVP LPKAGKWREI INTDASEYGG SGMGNGGMVE ARAEGKNISA TMLLPPLSTI MLELVAD //