ID   GLGB_MYCUA              Reviewed;         731 AA.
AC   A0PUI6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 111.
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=MUL_3936;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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}.
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DR   EMBL; CP000325; ABL06005.1; -; Genomic_DNA.
DR   RefSeq; WP_011741610.1; NC_008611.1.
DR   AlphaFoldDB; A0PUI6; -.
DR   SMR; A0PUI6; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GeneID; 72432813; -.
DR   KEGG; mul:MUL_3936; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_11; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000765; 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; Transferase.
FT   CHAIN           1..731
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_1000044986"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        464
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   731 AA;  81531 MW;  250FF1C8AAE0FA0B CRC64;
     MSRTDQLAGT HLAPEPNDLA LLVAGSHHNP HGVLGAHEYG DHIVIRAFRP HAAEVIAIVG
     DDRFPMQHIE SGLFAVALPF VDLIDYRLQV SYENSEPFTV ADAYRFLPTL GEVDLHLFAE
     GRHERLWEAL GAHPRSFTTA DGVVHGVSFA VWAPNAEGVS LIGDFNGWSG SEAPMRVLGS
     SGVWELFWPD FPADGLYKFR VHGADGVVSE RADPFAFGTE VPPQTASRVT VSDYSWGDGD
     WMTERAQRNP VFEPMSTYEV HLGSWRPGLS YRQLATELTD YVVAHKFTHV ELLPVAEHPF
     AGSWGYQVTS YYAPTSRFGT PDDFRALVDA LHQAGIGVIV DWVPAHFPKD AWALGRFDGT
     PLYEHSDPKR GEQLDWGTYV FDFGRPEVRN FLVANALYWI EQFHIDGLRV DAVASMLYLD
     YSRPQDGWTP NIYEGRENLE AVQFLQEMNA TAHKAAPGIV TIAEESTSWP GVTRPTSIGG
     LGFSMKWNMG WMHDTLDYVS RDPIYRSYHH HEMTFSMLYA FSENYVLPLS HDEVVHGKGT
     LWGRMPGSNH TKAAGLRSLL AYQWAHPGKQ LLFMGQEFGQ RAEWSEQRGL DWFQLDENGF
     SNGVLRLVRD INEIYCDHCA LWSQDTTPEG YSWIDANDSA NNVLSFLRHG SDGSVMACIF
     NFAGSEHSDY RLGLPIAGRW REVLNTDATI YNGSGVGNFG GVDATAEPWH GRPASAVLVL
     PPSSALWLEP A
//