ID GLGB_CORDI Reviewed; 732 AA. AC Q6NHR6; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 121. 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=DIP1065; OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype OS gravis). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=257309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis; RX PubMed=14602910; DOI=10.1093/nar/gkg874; RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G., RA Parkhill J.; RT "The complete genome sequence and analysis of Corynebacterium diphtheriae RT NCTC13129."; RL Nucleic Acids Res. 31:6516-6523(2003). 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; BX248357; CAE49588.1; -; Genomic_DNA. DR RefSeq; WP_010934779.1; NC_002935.2. DR AlphaFoldDB; Q6NHR6; -. DR SMR; Q6NHR6; -. DR STRING; 257309.DIP1065; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; cdi:DIP1065; -. DR HOGENOM; CLU_004245_3_2_11; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000002198; 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; 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..732 FT /note="1,4-alpha-glucan branching enzyme GlgB" FT /id="PRO_0000188697" FT ACT_SITE 409 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" FT ACT_SITE 462 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" SQ SEQUENCE 732 AA; 82603 MW; 6A734BCBFC3B0441 CRC64; MVSPTQITPV HPDVLHALKI CQYHDPHGVY GWHEVDAERA VIRTRHIGAE RVETLLSDST VVELAAVGDD IFEAIVDHDA SCDYRLRIHW QGGQVTEQAD AYHFLPTLGD LDLHLINEGR HERLWEVLGA NPTTITTAMG DVEGTAFAVW APNASGVAVI GDFCGWNPSQ YPMRSLGSTG IWELFIPNIG VGTVYKFAIH THEGHRLDKA DPMAKRAEVA PATGSIIASS SYTWNDDTWM TNRAHTDHDN TAMSVYEVHL GSWSQGQNYE ELATNLVDYV KEMGYTHVEF LPVAEHPFGG SWGYQVSGYY APTSRWGTPD QLRLLIDAFH QAGIGVIVDW VPAHFPKDAF ALGRFDGQAL YEHPDWRRGE QKDWGTYVFD FGRNEVRNFL VANALYWLEE FHVDGLRVDA VASMLYLDYS REPGEWLPNI YGGRENLEAV QFLQEMNATV HKSHPGVMTI AEESTSWPGV TSPTWEGGLG FSMKWNMGWM NDTLEYFSHE PIHRMYHHND ITFSMVYAYS EKFVLPFSHD EVVHGKGSLW TRMPGDAWNK AAGLRTLYAY MYAHPGKNLL FQGQEFGQVK EWSEERSLDW GDMDGWEGEY HRGIRTLVQD LNALYKDSPA LYSQDNNPAG FSWTKSDDAA NNILSFVRYG ADGSKILAVF NFGGADHPSY KLGVPEGGNW KCILNTDAGI YEGEDNYLDS DVMAWDTDWD GYQHSLTVHI PAMSGQLYRW EA //