GLGB_FRATN
ID GLGB_FRATN Reviewed; 640 AA.
AC A0Q593;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=FTN_0513;
OS Francisella tularensis subsp. novicida (strain U112).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=401614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112;
RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT "Comparison of Francisella tularensis genomes reveals evolutionary events
RT associated with the emergence of human pathogenic strains.";
RL Genome Biol. 8:R102.1-R102.16(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; CP000439; ABK89408.1; -; Genomic_DNA.
DR RefSeq; WP_003038522.1; NZ_CP009633.1.
DR AlphaFoldDB; A0Q593; -.
DR SMR; A0Q593; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; A0Q593; -.
DR EnsemblBacteria; ABK89408; ABK89408; FTN_0513.
DR KEGG; ftn:FTN_0513; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR BioCyc; FTUL401614:G1G75-535-MON; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000762; 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; -; 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_1000044978"
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; 74734 MW; 39B55F6664A14247 CRC64;
MKNKNSKQNT HSTIGEQDIH YFHEGKHIYA YEFMGAHKAC EGGIEGIRFT TWAPNAKSIC
VIGDFNYWQV EDKNYMEPIT DAGLWSVFIP NAKNGDKYKF VVTNKDTNHY VYKSDPYAFF
SELRPNTASI ITTETQYTWS DDKWLEKRAK TNYYDNPMNV YELHLASWKT KDGKFMTYDE
LSETLPQYIK EMGYTHVEFM PLHEHPLDAS WGYQPTGFYS VNSRHGDIIG LKRLVDKLHN
NDIGVILDWV PGHFCKDQHG LIYFDGTPCY EYQEHTKAIN KGWGTHNFDL GRNEVKCFLI
SNAMYWINEF HIDGLRVDAV SNILYLNYDR EDGQWIPNIY GGHENLEGIA FLKELNGVLK
HTCKGVVTIA EESSSWPDIS TPVEKGGLGF DFKWNMGWMN DTLRYISLDP VYRKYHHNLI
TFSMVYHYSE KFILSISHDE VVHGKKSLIN KMWGDLWNKY AGLRLYMSYM IGHPGKKLIF
MGSEFGQFVE WREYEQLQWQ VVDQYESHKQ TLHFFKKLND FYHNETALWQ CDYDHHGFRW
IDADNSQQSI LSFIRSSKDN KQKLIFICNF TPVTYYDYHL GVPDAGSYKE VFNSDNLEFG
GSGQVMATEI FSSPQSSHGF EQRITIKIPP MATLVLKLIK
