GLGB_THEFY
ID GLGB_THEFY Reviewed; 749 AA.
AC Q47SE7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 126.
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=Tfu_0582;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(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; CP000088; AAZ54620.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47SE7; -.
DR SMR; Q47SE7; -.
DR STRING; 269800.Tfu_0582; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q47SE7; -.
DR EnsemblBacteria; AAZ54620; AAZ54620; Tfu_0582.
DR KEGG; tfu:Tfu_0582; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_11; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
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..749
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260710"
FT ACT_SITE 427
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 480
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 749 AA; 84375 MW; ECE7BC0418FFE633 CRC64;
MTARPAVRQP AGLPCPQPCN RYGYPMTNAL LAEIDALVAG THHNPHALLG AHPGPEGVWV
RALRPLARSV HVLLANGSRV ELPHLHKGVF AGVVPGAEVP DYRLVVRYDD GTELTVDDPY
RHLPTLGELD IHLIQEGRHE ELWRVLGAHT KRFPSVLGDT EGTAFTVWAP NARGVRVIGD
FNHWDGTGHP MRSLGSCGVW ELFIPGVGDG TRYKYQVLGA DGVWREKADP VAFATQAPPE
TASVVFTSRY TWQDDEWLTQ RAAADLHRKP MSIYEVHLGS WRPGLSYREL ADQLVDYVRE
LGFTHVEFLP VAEHPFGGSW GYQVTSYYAP TARFGSPDDF RYLVDRLHQA GIGVFLDWVP
AHFPKDDWAL SRFDGTALYE HPDPRRGIHP DWDTLIFNYG RTEVRNFLVA NALFWLEEFH
IDGLRVDAVA SMLYLDYSRE SGQWEPNAYG GRENLDAIDF LRELNATAYR RNPGIAMIAE
ESTAWPGVTR STDTGGLGFG FKWNMGWMHD TLSYLQHDPV HRQYHHNEVT FSMVYAYSEN
YVLPLSHDEV VHGKRSLLYK MPGNEWQRCA NLRALLAYMW AHPGKQLLFM GNEIAQGDEW
SHDAGVQWWL LRYPHHAGMR RLVADLNRLY RNTRALWSQD TVPEGFTWLD GGDASGNTLS
FLRWGDDGSV LACLVNFSGR PHPERRVGLP YAGRWREILN TDAVLYGGSG VSQPGIIEAS
EETPWQGQPA SALVTYPPLG VSWLVFDGT
