ID GLGB_LACAC Reviewed; 638 AA. AC Q5FL68; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 109. 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=LBA0680; OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=272621; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM; RX PubMed=15671160; DOI=10.1073/pnas.0409188102; RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L., RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S., RA Hamrick A., Cano R., Klaenhammer T.R.; RT "Complete genome sequence of the probiotic lactic acid bacterium RT Lactobacillus acidophilus NCFM."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(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; CP000033; AAV42556.1; -; Genomic_DNA. DR RefSeq; WP_011254224.1; NC_006814.3. DR RefSeq; YP_193587.1; NC_006814.3. DR AlphaFoldDB; Q5FL68; -. DR SMR; Q5FL68; -. DR STRING; 272621.LBA0680; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR GeneID; 56942312; -. DR KEGG; lac:LBA0680; -. DR PATRIC; fig|272621.13.peg.650; -. DR eggNOG; COG0296; Bacteria. DR HOGENOM; CLU_004245_3_2_9; -. DR OrthoDB; 9800174at2; -. DR BioCyc; LACI272621:G1G49-702-MONOMER; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000006381; 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..638 FT /note="1,4-alpha-glucan branching enzyme GlgB" FT /id="PRO_0000188711" FT ACT_SITE 303 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" FT ACT_SITE 356 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" SQ SEQUENCE 638 AA; 74582 MW; F66FC75355225AAC CRC64; MVTIVEVKQH IKKFAAGNEL YLQEVLGCHY ENDIYTFRVW APNAQKVWLV GDFNDWDKSL EMSQTLDGVW EIKTSLPKEG QLYKFLVKQA DGREVMKIDP MAFELEPRPG SAAVIVKLPN KKWLDGAWMG RNKRSNHFAR PINIYEVHAS SWKRHTDGSL YTLKDLQKEL IPYVKEQGFN YIEFLPLTAH PLDASWGYQT IGYYALERTY GTPRELQDFV EACHKENIGV LADWVPGHFC INDDALAYYD GTPCYEFSEK WRAENKGWGA LNFDLGKPEV QSFLLSSALF WLEFYHLDGL RVDAVSNMIY RDYDRSDGEW KTDKFGGNRN LEGIEFLQKL NRTIKGKHPE CLMIAEESSA QVKITGRIED GGLGFDFKWN MGWMNDILRF YEMDPLFRKF NFNLATFSFM YRMSENFILP LSHDEVVHGK RSLMNKMFGD RDKQFAQLRN LLTLQMTYPG KKLLFMGSEF GQYLEWRYND GLDWAELKDE LNAKMKHFDQ DLNSFYLNEP ALWQLEQRED SVQIIDADNK DESVLSFIRQ GKTRHDFLIV ILNFTPVDRK KITIGVPYAG KYCEVFNSAR KEYGGSWNQE KQNLKTQNNS FKNFNYQVQL DIPGFSAVIL KPVDVHIKRR INRKTKTK //