GLGB_MYCUA
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 03-AUG-2022, entry version 102.
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}; OrderedLocusNames=MUL_3936;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
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 STRING; 362242.MUL_3936; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; A0PUI6; -.
DR EnsemblBacteria; ABL06005; ABL06005; MUL_3936.
DR KEGG; mul:MUL_3936; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_11; -.
DR OMA; FGMKWMM; -.
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; cd02855; E_set_GBE_prok_N; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.1180; -; 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 PANTHER; PTHR43651; PTHR43651; 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; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
DR TIGRFAMs; TIGR01515; branching_enzym; 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
