GLGB_FRATM
ID GLGB_FRATM Reviewed; 640 AA.
AC B2SFM7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=FTM_0569;
OS Francisella tularensis subsp. mediasiatica (strain FSC147).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=441952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSC147;
RX PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA Keim P., Johansson A.;
RT "Molecular evolutionary consequences of niche restriction in Francisella
RT tularensis, a facultative intracellular pathogen.";
RL PLoS Pathog. 5:E1000472-E1000472(2009).
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; CP000915; ACD30570.1; -; Genomic_DNA.
DR RefSeq; WP_012429313.1; NC_010677.1.
DR AlphaFoldDB; B2SFM7; -.
DR SMR; B2SFM7; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; ftm:FTM_0569; -.
DR HOGENOM; CLU_004245_3_2_6; -.
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; -; 1.
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; 1.
DR TIGRFAMs; TIGR01515; branching_enzym; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..640
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000131815"
FT ACT_SITE 318
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 371
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 640 AA; 74760 MW; BC3A22B98F0C2D3A CRC64;
MKNKNSEQNT HSTIGEQDIH YFHEGKHIYA YEFMGAHKAC EEGIEGIRFT TWAPNAKSIC
VIGDFNYWQV EDKNYMEPIT DAGLWSVFIP NAKNGDKYKF VVTNKDTNNY VYKSDPYAFF
SELRPNTASI ITTETQYTWS DDKWLEKRAK TNYYDNPMNV YELHLASWKT KNGKFLTYDE
LNETLPQYIK EMGYTHVEFM PLHEHPLDAS WGYQPTGFYS VNSRHGDIIG LKRLVDKLHN
NDIGVILDWV PGHFCKDQHG LIYFDGSPCY EYQEPTKAIN KGWGTHNFDL GRNEVKCFLI
SNAMYWINEF HIDGLRVDAV SNILYLNYDR EDGQWIPNIY GGHENLEGIA FLKELNGVLK
HTCKGVITIA EESSSWPDIS TPVEKGGLGF DFKWNMGWMN DTLRYISLDP VYRKYHHNLI
TFSMVYHYSE KFILSISHDE VVHGKKSLIN KMWGDLWNKY AGLRLYMSYM IGHPGKKLIF
MGSEFVQFVE WREYEQLQWQ VVDQYESHKQ TLHFFKKLND LYHNETALWQ CDYDHHGFRW
IDADNSQQSI LSFIRSSKDN KQKLIFICNF TPVTYYDYHL GVPDAGSYKE VFNSDNLEFG
GSGQVMATEI FSSPQSSHGF EQRITIKIPP MATLVLKLIK