ID GLGB_RHORT Reviewed; 740 AA. AC Q2RR72; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 118. 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=Rru_A2576; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / OS NCIMB 8255 / S1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1; RX PubMed=21886856; DOI=10.4056/sigs.1804360; RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K., RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C., RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y., RA Roberts G.P., Reslewic S., Schwartz D.C.; RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1)."; RL Stand. Genomic Sci. 4:293-302(2011). 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; CP000230; ABC23373.1; -; Genomic_DNA. DR RefSeq; WP_011390326.1; NC_007643.1. DR RefSeq; YP_427660.1; NC_007643.1. DR AlphaFoldDB; Q2RR72; -. DR SMR; Q2RR72; -. DR STRING; 269796.Rru_A2576; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblBacteria; ABC23373; ABC23373; Rru_A2576. DR KEGG; rru:Rru_A2576; -. DR PATRIC; fig|269796.9.peg.2685; -. DR eggNOG; COG0296; Bacteria. DR HOGENOM; CLU_004245_3_2_5; -. DR PhylomeDB; Q2RR72; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000001929; 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; 2. 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..740 FT /note="1,4-alpha-glucan branching enzyme GlgB" FT /id="PRO_0000260692" FT ACT_SITE 414 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" FT ACT_SITE 467 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" SQ SEQUENCE 740 AA; 83075 MW; 602E7CD8400F4F6F CRC64; MDPKAYSEAV AALVGARHSN PFAFLGPHEG RAEGGRGGFC IRCFRPKATA VSLISAADDT VLGRMKRLHP DGLFGIDLPE APGALAYRLR VSEGDEDRDI EDPYRFGPVL GELDRHLLGE GTHLDIYRKM GAHPMTRDGV RGTGFALWAP NATRVSVIGD FNGWDGRLHP MRAHPGSGVW DIFLPGVVEG HLYKYELLGP DGSLLPAKAD PYAFQAEKPP HTASVVRGLG TYAWNDGRWM SERADRVATS APVSIYEVHL GSWRHGGGDR SLSYREMAEQ LIPYVKEMGF THIELLPVSE FPFDGSWGYQ PIGLFAPTSR FGEPDDFRHF VDRCHQEGVG VILDWVAGHF PEDAHGLSWF DGTHLYEHSD PRQGRHMDWG TYIFNYGRNE VRNFLLANAL FWLEQFHIDG LRVDAVASML YLDYSRKAGE WVPNKFGGRE NLEAIDFLRR MNELVYGRFP GAVTIAEEST AWPMVSRPVH LGGLGFGYKW NMGWMNDTLS YMSQDPIYRR FHQHDLSFGL LYAFTENFVL PLSHDEVVHG KRSILGRMPG DAWQQFANLR AYYGFMWTHP GKKLLFMGCE FAQGREWNHN ASLDWHLLDI DWHKGVQALV RDLNGLYAGV PALHDRDTEG YGFSWIDCTD ADQSVLAFLR FGETAEDVVM VVCNFTPNPR HGYRLGAPIA GRWREIFNTD SAHYGGSNMG NSVVETEETK SHGHAQSVVL TLPPLATIVL RPDGPITRIA //