ID GLGB_SYNE7 Reviewed; 774 AA. AC P16954; Q31PA4; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 163. DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB; DE EC=2.4.1.18; DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase; DE AltName: Full=Alpha-(1->4)-glucan branching enzyme; DE AltName: Full=Glycogen branching enzyme; DE Short=BE; GN Name=glgB; OrderedLocusNames=Synpcc7942_1085; OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) OS (Anacystis nidulans R2). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=1140; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2142668; DOI=10.1016/0378-1119(90)90208-9; RA Kiel J.A.K.W., Boels J.M., Beldman G., Venema G.; RT "Nucleotide sequence of the Synechococcus sp. PCC7942 branching enzyme gene RT (glgB): expression in Bacillus subtilis."; RL Gene 89:77-84(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Golden S., Richardson P.; RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."; RL Submitted (AUG-2005) 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: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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is about 35 degrees Celsius.; CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC -!- SUBUNIT: Monomer. 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; M31544; AAB39038.1; -; Genomic_DNA. DR EMBL; CP000100; ABB57115.1; -; Genomic_DNA. DR PIR; JQ0550; JQ0550. DR RefSeq; WP_011242776.1; NZ_JACJTX010000003.1. DR AlphaFoldDB; P16954; -. DR SMR; P16954; -. DR STRING; 1140.Synpcc7942_1085; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR PaxDb; 1140-Synpcc7942_1085; -. DR GeneID; 76399827; -. DR KEGG; syf:Synpcc7942_1085; -. DR eggNOG; COG0296; Bacteria. DR HOGENOM; CLU_004245_3_2_3; -. DR OrthoDB; 9800174at2; -. DR BioCyc; SYNEL:SYNPCC7942_1085-MONOMER; -. DR BRENDA; 2.4.1.18; 7781. DR UniPathway; UPA00164; -. DR Proteomes; UP000889800; 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; 2. DR PIRSF; PIRSF000463; GlgB; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF81296; E set domains; 2. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism; KW Glycosyltransferase; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..774 FT /note="1,4-alpha-glucan branching enzyme GlgB" FT /id="PRO_0000188756" FT ACT_SITE 440 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 493 FT /note="Proton donor" FT /evidence="ECO:0000250" SQ SEQUENCE 774 AA; 89195 MW; C4C8885EF103CCE4 CRC64; MTGTTPLPSS SLSVEQVNRI ASNQEQNPFD ILGPHPYEHE GQAGWVIRAY LPEAQEAAVI CPALRREFAM HPVHHPHFFE TWVPEETLEI YQLRITEGER ERIIYDPYAF RSPLLTDYDI HLFAEGNHHR IYEKLGAHPC ELENVAGVNF AVWAPSARNV SILGDFNSWD GRKHQMARRS NGIWELFIPE LTVGAAYKYE IKNYDGHIYE KSDPYGFQQE VRPKTASIVA DLDRYTWGDA DWLERRRHQE PLRQPISVYE VHLGSWMHAS SDAIATDAQG KPLPPVPVAD LKPGARFLTY RELADRLIPY VLDLGYSHIE LLPIAEHPFD GSWGYQVTGY YAATSRYGSP EDFMYFVDRC HQNGIGVILD WVPGHFPKDG HGLAFFDGTH LYEHADSRQG EHREWGTLVF NYGRHEVRNF LAANALFWFD KYHIDGIRVD AVASMLYLDY NRKEGEWIPN EYGGRENIEA ADFLRQVNHL IFSYFPGALS IAEESTSWPM VSWPTYVGGL GFNLKWNMGW MHDMLDYFSM DPWFRQFHQN NVTFSIWYAF SENFMLALSH DEVVHGKSNL IGKMPGDEWQ KFANLRCLLG YMFTHPGKKT LFMGMEFGQW AEWNVWGDLE WHLLQYEPHQ GLKQFVKDLN HLYRNAPALY SEDCNQAGFE WIDCSDNRHS IVSFIRRAHE SDRFLVVVCN FTPQPHAHYR IGVPVAGFYR EIFNSDARSY GGSNMGNLGG KWTDEWSCHN RPYSLDLCLP PLTTLVLELA SGPESLSEAA NSPL //