ID GLGB1_XANAC Reviewed; 724 AA. AC Q8PR13; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB 1; DE EC=2.4.1.18; DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase 1; DE AltName: Full=Alpha-(1->4)-glucan branching enzyme 1; DE AltName: Full=Glycogen branching enzyme 1; DE Short=BE 1; GN Name=glgB1; OrderedLocusNames=XAC0156; OS Xanthomonas axonopodis pv. citri (strain 306). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190486; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing host RT specificities."; RL Nature 417:459-463(2002). 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:0000250}. 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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB CC subfamily. {ECO:0000305}. 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; AE008923; AAM35048.1; -; Genomic_DNA. DR AlphaFoldDB; Q8PR13; -. DR SMR; Q8PR13; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; xac:XAC0156; -. DR eggNOG; COG0296; Bacteria. DR HOGENOM; CLU_004245_3_2_6; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000000576; 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..724 FT /note="1,4-alpha-glucan branching enzyme GlgB 1" FT /id="PRO_0000188764" FT ACT_SITE 403 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 456 FT /note="Proton donor" FT /evidence="ECO:0000250" SQ SEQUENCE 724 AA; 80101 MW; A753B478470FC4C0 CRC64; MSNRWDSGVV RALAEARHGD AFAVLGAHPS DKGRLLRTYL PGADRVGAVL DDGQVVALDA GPEPGLFAGE LPAHGGYRLR IGWPGGEQET ADPYAFGPQL SDFDLHLISE GHHLQLADAL GANVVEVEGV RGTRFAVWAP NASRVAVVGD FNSWDARRHP MRLRHQSGVW ELFVPDVGPG AHYKYQLRGP HGHELPAKAD PVARRAELAP GTASIVADPT PHQWSDDGWM ATRARRQAHD APMSIYEIHA GSWLREAGVD LDWDGLADRL IPYVADMGFT HVELMPVSEH PFGGSWGYQP LGLFAPTARF GTPDGFARFV DRCHREGIGV IVDWVPAHFP TDAHGLAHFD GTALYEHADP REGFHRDWNT LIYNHGRREV SGFLIASAME FLQRYHVDGL RVDAVASMLY RDYSRNAGEW IPNIHGGREN YETIAFLRRL NEVVREHTPG AVMIAEESTA FPGVTAEVAH GGLGFHYKWN MGWMHDTLHY AGLDPIYRRY HHGELTFSMV YAYSERFVLP ISHDEVVHGK GSLLGRMPGD DWQRFANLRA YLGFMFTHPG RKLLFMGCEF GQPTEWNHDA GLPWHLLDDP RHRGVQTLVR DLNRLYVQYP ALHAHDDDPS GFAWVVGDDA GNSVVAFLRK GKRGDAPVLV VINFTPVVQH AYRIGVPQGG QWREVFNSDA GIYGGSNLGN GGSVTAEQQS MHGHAQSLPL LLPPLGAIVL TPYG //